The Vendruscolo Laboratory

2024

R. I. Horne, E. Andrzejewska, P. Alam, Z. F. Brotzakis, A. Srivastava, A. Aubert, M. Nowinska, R. C. Gregory, R. Staats, A. Possenti, S. Chia, P. Sormanni, B. Ghetti, B. Caughey, T. P. J. Knowles and M. Vendruscolo.
Discovery of potent inhibitors of alpha-synuclein aggregation using structure-based iterative learning.
Nat. Chem. Biol. in press.
S. Chia, R. Lessa Cataldi, F. S. Ruggeri, R. Limbocker, I. Condado-Morales, K. Pisani, A. Possenti, S. Linse, T. P. J. Knowles, J. Habchi, B. Mannini and M. Vendruscolo.
A relationship between structures and neurotoxic effects of Abeta oligomers stabilized by different metal ions.
ACS Chem. Neurosci. in press.
T. Amico, S. Dada, A. Lazzari, A. Trovato, M. Vendruscolo, M. Fuxreiter and A. Maritan.
A scale-invariant log-normal droplet size distribution below the transition concentration for protein phase separation.
eLife, 13, RP94214 (2024).
A. Miller, S. Chia, E. Klimont, T. P. J. Knowles, M. Vendruscolo and F. S. Ruggeri.
Characterization of the maturation-dependent changes in the structure and seeding capacity of Abeta42 amyloid fibrils.
Comm. Biol. 7, 153 (2024).
A. Rontgen, Z. Toprakcioglu, J. E. Tomkins and M. Vendruscolo.
Modulation of alpha-synuclein aggregation kinetics by its alternative splice isoforms.
Proc. Natl. Acad. Sci. USA, 121, e2313465121 (2024).
R. I. Horne, J. Wilson-Godber, A. Gonzalez-Diaz, Z. F. Brotzakis, S. Seal, R. C. Gregory, A. Possenti, S. Chia and M. Vendruscolo.
Using generative modelling to endow with potency inert starting compounds with good bioavailability and low toxicity.
J. Chem. Inf. Model. 6, 590-596 (2024).
R. Chandra, R. I. Horne and M. Vendruscolo.
Bayesian optimization in the latent space of a variational autoencoder for the generation of selective FLT3 inhibitors.
J. Chem. Theory Comp. 20, 469-476 (2024).
D. Rinauro, F. Chiti, M. Vendruscolo and R. Limbocker.
Misfolded protein oligomers: Mechanisms of formation, cytotoxic effects, and pharmacological approaches.
Mol. Neurodegener. 1, 20 (2024).

2023

S. E. Sandler, R. I. Horne, S. Rocchetti, R. Novak, N.-S. Hsu, M. Castellana Cruz, Z. F. Brotzakis, R. C. Gregory, S. Chia, G. J. L. Bernardes, U. F. Keyser and and M. Vendruscolo.
Multiplexed digital characterisation of misfolded protein oligomers via solid-state nanopores.
J. Am. Chem. Soc. 14, 25776-25788 (2023).
C. Olivieri, Y. Wang, C. Walker, M. V. Subrahmanian, K. N. Ha, D. A. Bernlohr, J. Gao, C. Camilloni, M. Vendruscolo, S. S. Taylor and G. Veglia.
The alphaC-beta4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A.
eLife, 12, RP91506 (2023).
M. Oeller, R. Kang, H. Bolt, A. Gomes dos Santos, A. Langborg Weinmann, A. Nikitidis, P. Zlatoidsky, W. Su, W. Czechtizky, L. De Maria, P. Sormanni and M. Vendruscolo.
Sequence-based prediction of the solubility of peptides containing non-natural amino acids.
Nat. Comm..14, 7475 (2023).
R. I. Horne, M. A. Metrick II, W. Man, D. Rinauro, Z. F. Brotzakis, S. Chia, G. Meisl and M. Vendruscolo.
Secondary processes dominate the quiescent, spontaneous aggregation of alpha-synuclein at physiological pH with sodium salts.
ACS Chem. Neurosci. 14, 3125-3131 (2023).
C. M. Lim, A. Gonzalez-Diaz, M. Fuxreiter, F. Pun, A. Zhavoronkov and M. Vendruscolo.
Multiomic prediction of therapeutic targets for human diseases associated with protein phase separation.
Proc. Natl. Acad. Sci. USA, 120, e2300215120 (2023).
R. Staats, Z. F. Brotzakis, S. Chia, R. I. Horne and M. Vendruscolo.
Optimization of a small molecule that inhibits secondary nucleation in alpha-synuclein aggregation.
Front. Mol. Biosci. 10},1155753 (2023).
S. Errico, G. Lucchesi, D. Odino, E. Youssef Osman, R. Cascella, L. Neri, C. Capitini, M. Calamai, F. Bemporad, C. Cecchi, D. Barbut, A. Relini, C. Canale, G. Caminati, R. Limbocker, M. Vendruscolo, M. Zasloff and F. Chiti.
Quantitative attribution of the protective effects of aminosterols against misfolded protein oligomers to their chemical structures and ability to modulate the physicochemical properties of membranes.
J. Med. Chem. 66, 9519–9536 (2023).
Z. F. Brotzakis, T. Lohr, S. Truong, S. E. Hoff, M. Bonomi and M. Vendruscolo.
Determination of the structure and dynamics of the fuzzy coat of an amyloid fibril of IAPP using cryo-electron microscopy.
Biochemistry, 62, 2407–2416 (2023).
M. Wilson, S. Satapathy and M. Vendruscolo.
Extracellular protein homeostasis: The dawning of a new age for human disease therapies?
Clin. Transl. Med. 13, e1305 (2023).
M. Vendruscolo.
Thermodynamic and kinetic approaches for drug discovery to target protein misfolding and aggregation.
Expert Opin. Drug Discov. 18, 881-891 (2023).
S. Koga, M. Metrick II, L. Golbe, A. Santambrogio, A. Soto-Beasley, R. Walton, M. Baker, C. Fernandez De Castro, M. DeTure, D. Russell, B. Navia, C. Sandiego, O. Ross, M. Vendruscolo, B. Caughey and D. Dickson.
Case report of a patient with unclassified tauopathy with molecular and neuropathological features of both progressive supranuclear palsy and corticobasal degeneration.
Acta Neuropathol. Commun. 11, 88 (2023).
T. C. T. Michaels, D. Qian, A. Saric, M.Vendruscolo, S. Linse and T. P. J. Knowles.
Amyloid formation as a protein phase transition.
Nat. Rev. Phys. 5, 379-397 (2023).
A. M. Miller, S. Meehan, C. M. Dobson, M. E. Welland, D. Klenerman, M. Vendruscolo, F. S. Ruggeri and T. P. J. Knowles.
Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.
Proc. Natl. Acad. Sci. USA, 120, e2216234120 (2023).
M. Vendruscolo and M. Fuxreiter.
Towards sequence-based principles for protein phase separation predictions.
Curr. Op. Chem. Biol. 75, 102317 (2023).
R. Limbocker, R. Cascella, N. Cremades, P. Tessier, M. Vendruscolo and F. Chiti.
Characterization of pairs of toxic and nontoxic misfolded protein oligomers elucidates the structural determinants of oligomer toxicity in protein misfolding diseases.
Acc. Chem. Res. 56, 1395-1405 (2023).
A. Hatos, J. M. C. Teixeira, S. Barrera-Vilarmau, A. Horvath, S. Tosatto, M.Vendruscolo and M. Fuxreiter.
FuzPred: A web server for the sequence-based prediction of the context-dependent binding modes of proteins.
Nucl. Acids Res. 51, W198-W206 (2023).
R. I. Horne, M. H. Murtada, D. Huo, Z. D. Brotzakis, R. C. Gregory, A. Possenti, S. Chia and M. Vendruscolo.
Exploration and exploitation approaches based on generative machine learning to identify potent small molecule inhibitors of alpha-synuclein secondary nucleation.
J. Chem. Theory Comp. 19, 4701-4710 (2023).
N. A. Erkamp, M. Oeller, T. Sneideris, H. Ausserwoger, A. Levin, T. Welsh, R. Qi, D. Qian,N. Lorenzen, H. Zhu, P. Sormanni, M. Vendruscolo and T. P.J. Knowles.
Multi-dimensional protein solubility optimization with an ultra-high-throughput microfluidic platform.
Anal. Chem. 95, 5362-5368 (2023).
R. Bell, M. Vendruscolo and J. R. Kumita.
Probing the effects of N-terminal acetylation on alpha-synuclein structure, aggregation and cytotoxicity.
Meth. Enzymol. 686, 45 (2023).
H. Hampel, Y. Hu, J. Hardy, K. Blennow, C. Chen, G. Perry, S.-H. Kim, V. L. Villemagne, P. Aisen, M. Vendruscolo, T. Iwatsubo, C. Masters, M. Cho, L. Lannfelt, J. L. Cummings and A. Vergallo.
The amyloid-beta pathway in Alzheimer's disease: A plain language summary.
Neurodegener. Dis. Manag. 13, 141-149 (2023).
M. R. Wilson, S. Satapathy and M. Vendruscolo.
Extracellular protein homeostasis in neurodegenerative diseases.
Nat. Rev. Neurosci. 19, 235-245 (2023). [PDF]
S. T. Dada, M. C. Hardenberg, Z. Toprakcioglu, L. K. Mrugalla, M. P. Cali, M. O. McKeon, E. Klimont, T. C. T. Michaels, T. P. J. Knowles and M. Vendruscolo.
Spontaneous nucleation and fast aggregate-dependent proliferation of alpha-synuclein aggregates within liquid condensates at neutral pH.
Proc. Natl. Acad. Sci. USA, 120, e2208792120 (2023). [PDF]
T. Bhardwaj, K. Gadhave, S. K. Kapuganti, P. Kumar, Z. F. Brotzakis, K. U. Saumya, N. Nayak, A. Kumar, N. Garg, M. Vendruscolo and R. Giri.
Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes.
Nat. Comm. 14, 945 (2023). [PDF]
M. Oeller, R. Kang, R. Bell, H. Ausserwoger, P. Sormanni and M. Vendruscolo.
Sequence-based prediction of pH-dependent protein solubility using CamSol.
Briefings Bioinform. 24, bbad004 (2023). [PDF]
J. M. Gabriel, T. Tan, D. J. Rinauro, C. M. Hsu, C. J. Buettner, M. Gilmer, A. Kaur, T. L. McKenzie, M. Park, S. Cohen, S. Errico, F. Chiti, M. Vendruscolo and R. Limbocker.
EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity.
Chem.-Biol. Interact. 371, 110307 (2023). [PDF]
K. N. Baumann, G. Sneideriene, M. Sanguanini, M. Schneider, O. Rimon, A. Gonzalez Diaz, H. Greer, D. Thacker, S. Linse, T. P. J. Knowles, M. Vendruscolo.
A kinetic map of the influence of biomimetic lipid model membranes on Abeta42 aggregation.
ACS Chem. Neurosci. 14, 323-329 (2023). [PDF]
A. Miller, S. Chia, Z. Toprakcioglu, T. Hakala, R. Schmid, Y. Feng, T. Kartanas, A. Kamada, M. Vendruscolo, F. S. Ruggeri and T. P. J. Knowles.
Enhanced surface nano-analytics of transient biomolecular processes.
Sci. Adv. 9, eabq3151 (2023). [PDF]
P. Joshi, S. Chia, X. Yang, M. Perni, J. M. Gabriel, M. Gilmer, R. Limbocker, J. Habchi and M. Vendruscolo.
Combinations of vitamin A and vitamin E metabolites confer resilience against amyloid-beta aggregation.
ACS Chem. Neurosci. 14, 657-666 (2023). [PDF]
S. Chia, F. Brotzakis, R. I. Horne, A. Possenti, B. Mannini, R. Cataldi, M. Nowinska, R. Staats, S. Linse, T. P. J. Knowles, J. Habchi and M. Vendruscolo.
Structure-based discovery of small molecule inhibitors of the autocatalytic proliferation of alpha-synuclein aggregates.
Mol. Pharm. 20, 183-193 (2023). [PDF]

2022

A. Horvath, M. Vendruscolo and M. Fuxreiter.
Sequence-based prediction of the cellular toxicity associated with amyloid aggregation within protein condensates.
Biochemistry, 61, 2461-2469 (2022).
L. Julian, J. C. Sang, Y. Wu, G. Meisl, J. H. Brelstaff, A. Miller, M. R. Cheetham, M. Vendruscolo, T. P. J. Knowles, F. S. Ruggeri, C. Bryant, S. Ros, K. M. Brindle, D. Klenerman.
Characterization of full-length p53 aggregates and their kinetics of formation.
Bioph. J. 121, 4280-4298 (2022)
M. Aguilar Rangel, A. Bedwell, E. Costanzi, S. Ricagno, J. Frydman, M. Vendruscolo and P. Sormanni.
Fragment-based computational design of antibodies targeting structured epitopes.
Sci. Adv. 8, eabp9540 (2022).
K. Kulenkampff, D. Emin, R. Staats, Y. P. Zhang, L. Sakhnini, A. Kouli, O. Rimon, E. Lobanova, C. H. Williams-Gray, P. Sormanni, D. Klenerman and M. Vendruscolo.
An antibody scanning method for the detection of alpha-synuclein oligomers in the serum of Parkinson's disease patients.
Chem. Sci. in press.
D. Emin, Y. P. Zhang, E. Lobanova, A. Miller, X. Li, Z. Xia, H. Dakin, D. I. Sideris, J. Y. L. Lam, R. T. Ranasinghe, A. Kouli, Y. Zhao, S. De, T. P. J. Knowles, M. Vendruscolo, F. S. Ruggeri, F. I. Aigbirhio, C. H. Williams-Gray and D. Klenerman.
Small soluble alpha-synuclein aggregates are the toxic species in Parkinson's disease.
Nat. Comm. 13, 5512 (2022).
M. Vendruscolo and M. Fuxreiter.
Protein condensation diseases: Therapeutic opportunities.
Nat. Comm. 13, 5550 (2022).
R. Bell, M. Castellana-Cruz, A. Nene, R. J. Thrush, C. K. Xu, J. R. Kumita and M. Vendruscolo.
Effects of N-terminal acetylation on the aggregation of disease-related alpha-synuclein variants.
J. Mol. Biol. in press.
R. Bell, R. Thrush, M. Castellana Cruz, M. Oeller, R. Staats, A. Nene, P. Flagmeier, C. Xu, S. Satapathy, C. Galvagnion, M. R. Wilson, C. M. Dobson, J. R. Kumita and M. Vendruscolo.
The N-terminal acetylation of alpha-synuclein slows down its aggregation process and alters the morphology of the resulting aggregates.
Biochemistry, 61, 1743-1756 (2022).
G. Fani, G. E. La Torre, R. Cascella, C. Cecchi, M. Vendruscolo and F. Chiti.
An intracellular Ca2+ increase induced by misfolded protein oligomers enhances the production of reactive oxidative species.
Cell. Mol. Life Sci. 79, 500 (2022).
R. Taylor, M. Aguilar Rangel, M. Geeson, P. Sormanni, M. Vendruscolo and G. J. L. Bernardes.
pi-Clamp-mediated homo- and heterodimerisation of antibodies via site-specific homobifunctional conjugation.
J. Am. Chem. Soc. 144, 13026-13031 (2022).
A. Horvath, M. Fuxreiter, M. Vendruscolo, C. Holt and J. A. Carver.
Are casein micelles extracellular condensates formed by liquid-liquid phase separation?
FEBS Lett. 596, 2072-2085 (2022).
C. Olivieri, G. Li, Y. Wang, M. V. Subrahmanian, C. Walker, J. Kim, C. Camilloni, A. De Simone, M. Vendruscolo, D. Bernlohr, S. Taylor, G. Veglia.
ATP-competitive inhibitors modulate the substrate binding cooperativity of a kinase by altering its conformational entropy.
Sci. Adv. 8, eabo0696 (2022).
H. Mikolajek, M. Weckener, Z. F. Brotzakis, J. Huo, E. V. Dalietou, A. Le Bas, P. Sormanni, P. J. Harrison, P. N. Ward, S. Truong, L. Moynie, D. Clare, M. Dumoux, J. Dormon, C. Norman, N. Hussain, V. Vogirala, R. J. Owens, M. Vendruscolo and J. H. Naismith.
Correlation between the binding affinity and the conformational entropy of nanobodies targeting the SARS-CoV-2 spike protein.
Proc. Natl. Acad. Sci. USA, 119, e2205412119 (2022).
T. Lohr, P. Sormanni and M. Vendruscolo.
Conformational entropy as a potential liability of computationally designed antibodies.
Biomolecules, 12, 718 (2022).
T. Lohr, K. Kohlhoff, G. T. Heller, C. Camilloni and M. Vendruscolo.
A small molecule stabilises the disordered native state of the Alzheimer's Abeta peptide.
ACS Chem. Neurosci. 13, 1738-1745 (2022).
A. Hatos, S. Tosatto, M. Vendruscolo and M. Fuxreiter.
FuzDrop on AlphaFold: Visualising the sequence-dependent propensity of liquid-liquid phase separation and aggregation of proteins.
Nucleic Acids Res. 50, W337-W344 (2022). [web server]
Z. Toprakcioglu, A. Kamada, T. C. T. Michaels, M. Xie, J. Krausser, A. Saric, M. Vendruscolo and T. P. J. Knowles.
Protein adsorption energy predicts amyloid nucleation rates.
Proc. Natl. Acad. Sci. USA, 119, e2109718119 (2022).
J. S. Lum, T. Berg, C. G. Chisholm, M. Vendruscolo and J. J. Yerbury.
Vulnerability of the spinal motor neuron presynaptic terminal sub-proteome in ALS.
Neurosci. Lett. 778, 136614 (2022).
R. P. Kreiser, A. K. Wright, L. R. Sasser, D. J. Rinauro, T. McKenzie, J. A. Albright, L. Richardson, V. A. Jaffett, D. E. Riegner, L. T. Nguyen, K. LeForte, M. Zasloff, F. Chiti, J. E. Hollows, M. Vendruscolo and R. Limbocker.
A brain permeable aminosterol regulates cell membranes to mitigate the toxicity of diverse pore-forming agents.
ACS Chem. Neurosci. 13, 1219-1231 (2022).
M. Vendruscolo.
Lipid homeostasis and its links with protein misfolding diseases.
Front. Mol. Neurosci. 15, 829291 (2022).
T. C. T. Michaels, A. Dear, S. I. A. Cohen, M. Vendruscolo and T. P. J. Knowles.
Kinetic profiling of therapeutic strategies for inhibiting the formation of amyloid oligomers.
J. Chem. Phys. 156, 164904 (2022).
M. Vendruscolo and M. Fuxreiter.
Sequence determinants of the aggregation of proteins within condensates generated by liquid-liquid phase separation.
J. Mol. Biol. 434, 167201 (2022).
R. Limbocker, S. Errico, D. Barbut, T. P. J. Knowles, M. Vendruscolo, F. Chiti and M. Zasloff.
Squalamine and trodusquemine: Two natural products for neurodegenerative diseases, from physical chemistry to the clinic.
Nat. Prod. Rep. 39, 742-753 (2022).
A.-M. Wolf Perez, N. Lorenzen, M. Vendruscolo and P. Sormanni.
Assessment of therapeutic antibody developability by combinations of in vitro and in silico methods.
Methods Mol. Biol. 2313, 57-113 (2022).

2021

Z. F. Brotzakis, P. R. Lindstedt, R. Taylor, D. J. Rinauro, N. C. T. Gallagher, G. J. L. Bernardes and M. Vendruscolo.
A structural ensemble of a tau-microtubule complex reveals regulatory tau phosphorylation and acetylation mechanisms.
ACS Cent. Sci. 7, 1986-1995 (2021).
M. Runfola, M. Perni, X. Yang, M. Marchese, A. Bacci, S. Mero, F. M. Santorelli, B. Polini, G. Chiellini, D. Giuliani, A. Vilella, M. Bodria, E. Daini, S. Pioli, S. Gul, M. J. O. Wakelam, M. Vendruscolo and S. Rapposelli.
Identification of a thyroid hormone derivative as a pleiotropic agent for the treatment of Alzheimer's disease.
Pharmaceuticals, 14, 1330 (2021).
M. Oeller, P. Sormanni and M. Vendruscolo.
An open-source automated PEG precipitation assay to measure the relative solubility of proteins with low material requirement.
Sci. Rep. 11, 21932 (2021).
D. C. Rodriguez Camargo, E. Sileikis, S. K. R. Chia, E. Axell, K. Bernfur R. L. Cataldi, S. I. A. Cohen, G. Meisl, J. Habchi, T.P. J. Knowles, M. Vendruscolo and S. Linse.
Proliferation of tau 304-380 fragment aggregates through autocatalytic secondary nucleation.
ACS Chem. Neurosci. 12, 4406-4415 (2021).
D. C. Rodriguez Camargo, S. Chia, J. Menzies, B, Mannini, G. Meisl, M. Lundqvist, K. Bernfur, V. Lattanzi, J. Habchi, S. I. A. Cohen, T. P. J. Knowles, M. Vendruscolo and S. Linse.
Surface-catalyzed secondary nucleation dominates the generation of toxic IAPP aggregates.
Front. Mol. Biosci. 8, 757425 (2021).
J. West, S. Satapathy, D. R Whiten, M. Kelly, N. J. Geraghty, P. Sormanni, M. Vendruscolo, J. N. Buxbaum, M. Ranson and M. R. Wilson.
Neuroserpin and transthyretin are amyloid-selective extracellular chaperones.
Sci. Adv. 7, eabf7606 (2021).
A. Deckert, A. M.E. Cassaignau, X. Wang, T. Wlodarski, S. H.S. Chan, C. A. Waudby, J. Kirkpatrick, M. Vendruscolo, L. D. Cabrita and J. Christodoulou.
Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.
Proc. Natl. Acad. Sci. USA, 118, e2103015118 (2021).
K. Gadhave, T. Bhardwaj, V. N. Uversky, M. Vendruscolo and R. Giri.
The signal peptide of the amyloid precursor protein forms amyloid-like aggregates and enhances Abeta42 aggregation.
Cell Rep. Phys. Sci. 2, 100599 (2021).
A. Pras, B. Houben F. A. Aprile, R. I. Seinstra, R. Gallardo, L. Janssen, W. Hogewerf, M. De Vleeschouwer, A. Matacabana, M. Koopman, E. Stroo, M. De Vries, S. Edwards, M. Vendruscolo, F. Falsone, F. Rousseau, J. Schymkowitz and E. A.A. Nollen.
The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation.
EMBO J. 40, e107568 (2021).
A. S. Morgunov, K. L. Saar, M. Vendruscolo and T. P. J. Knowles.
New frontiers for machine learning in protein science.
J. Mol. Biol. 433, 167232 (2021).
M. M. Schneider, S. Gautam, T. W. Herling, E. A. Andrzejewska, G. Krainer, A. M. Miller, Q. A. E. Peter, F. S. Ruggeri, M. Vendruscolo, A. Bracher, C. M. Dobson, F. U. Hartl, T. P. J. Knowles.
The Hsc70 disaggregation machinery removes monomer units directly from alpha-synuclein fibril ends.
Nat. Comm. 12, 5999 (2021).
J. Lin, C. Figazzolo, Michael A. Metrick II, P. Sormanni and M. Vendruscolo.
Computational maturation of a single-domain antibody against Abeta42 aggregation.
Chem. Sci. 12, 13940-13948 (2021).
F. S. Ruggeri, A. Miller, M. Vendruscolo and T. P. J. Knowles.
Unraveling the physicochemical determinants of protein liquid-liquid phase separation by nanoscale infrared vibrational spectroscopy.
Bio-Protoc. 11, e4122 (2021).
H. Hampel, J. Hardy, K. Blennow, C. Chen, G. Perry, S.-H. Kim, V. L. Villemagne, P. Aisen, M. Vendruscolo, T. Iwatsubo, C. Masters, M. Cho, L. Lannfelt, J. L. Cummings and A. Vergallo.
The amyloid pathway in Alzheimer's disease.
Mol. Psychiatry 26, 5481-5503(2021). [PDF]
T. Scheidt, J. A. Carozza, C. C. Kolbe, F. A. Aprile, O. Tkachenko, M. M. Bellaiche, G. Meisl, Q. A. E. Peter, T. W. Herling, S. Ness, M. Castellana-Cruz, J. L. P. Benesch, M. Vendruscolo, C. M. Dobson, P. Arosio and T. P. J. Knowles.
The binding of the small heat-shock protein alphaB-crystallin to fibrils of alpha-synuclein is driven by entropic forces.
Proc. Natl. Acad. Sci. USA, 118, e2108790118 (2021).
S. Errico, H. Ramshini, C. Capitini, C. Canale, M. Spaziano, D. Barbut, M. Calamai, M. Zasloff, R. Oropesa-Nunez, M. Vendruscolo and Fabrizio Chiti.
Quantitative measurement of the affinity of toxic and nontoxic misfolded protein oligomers for lipid bilayers, and of its modulation by lipid composition and trodusquemine.
ACS Chem. Neurosci. 12, 3189-3202 (2021).
U. Nowicka, P. Chroscicki, K. Stroobants, M. Sladowska, M. Turek, B. Uszczynska-Ratajczak, R. Kundra, T. Goral, M. Perni, C. M. Dobson, M. Vendruscolo and A. Chacinska.
Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins.
eLife, 10, e65484 (2021).
P. G. Bolhuis, Z. F. Brotzakis and M. Vendruscolo.
A maximum caliber approach for continuum path ensembles.
Eur. Phys. J. B, 94, 188 (2021).
M. Perni, B. Mannini. C. Xu. J. R. Kumita, C. M. Dobson, F. Chiti and M. Vendruscolo.
Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans.
Sci. Rep. 11, 14391 (2021).
Z. F. Brotzakis, T. Lohr and M. Vendruscolo.
Determination of intermediate state structures in the opening pathway of SARS-CoV-2 spike using cryo-electron microscopy.
Chem. Sci. 12, 9168-9175 (2021).
R. Bell and M. Vendruscolo.
Modulation of the interaction between alpha-synuclein and lipid membranes by post-translational modifications.
Front. Neurol. 12, 661117 (2021).
D. I. Sideris, J. S. H. Danial, D. Emin, F. S. Ruggeri, Z. Xia, Y. P. Zhang, E. Lobanova, H. Dakin, S. De, A. Miller, J. C. Sang, T. P. J. Knowles, M. Vendruscolo, G. Fraser, D. Crowther and D. Klenerman.
Soluble inflammatory Abeta aggregates are present throughout the brain at early stages of Alzheimer's disease.
Brain Comm. 3, fcab147 (2021).
M. M. Leal-Lasarte, B. Mannini, F. Chiti, M. Vendruscolo, C. M. Dobson, C. Roodveldt and D. Pozo.
Distinct responses of human peripheral blood cells to different misfolded protein oligomers.
Immunology, 164, 358-371 (2021).
P. Joshi, M. Perni, R. Limbocker, B. Mannini, S. Casford, S. Chia, J. Habchi, J. Labbadia, C. M. Dobson and M. Vendruscolo.
Two human metabolites rescue a C. elegans model of Alzheimer's disease via a cytosolic unfolded protein response.
Comm. Biol. 4, 843 (2021).
M. Fuxreiter and M. Vendruscolo
Generic nature of the condensed states of proteins.
Nat. Cell Biol. 23, 587-594 (2021). [PDF]
R. Limbocker, R. Staats, S. Chia, F. S. Ruggeri, B. Mannini, C. K. Xu, M. Perni, R. Cascella, A. Bigi, L. Sasser, N. R. Block, A. K. Wright, R. P. Kreiser, E. T. Custy, G. Meisl, S. Errico, J. Habchi, P. Flagmeier, T. Kartanas, J. E. Hollows, L. T. Nguyen, K. LeForte, D. Barbut, J. R. Kumita, C. Cecchi, M. Zasloff, T. P. J. Knowles, C. M. Dobson, F. Chiti and M. Vendruscolo.
Squalamine and its derivatives modulate the aggregation of amyloid beta and alpha-synuclein and suppress the toxicity of their oligomers.
Front. Neurosci. 15, 680026 (2021).
F. Buhr, P. Ciryam and M. Vendruscolo.
A mistranslation-prone transcriptome in repeat expansion diseases.
Nat. Rev. Mol. Cell Biol. 22, 583-584 (2021).
M. Perni, A. van der Goot, R. Limbocker, T. J. van Ham, F. A. Aprile, C. K. Xu, P. Flagmeier, K. Thijssen, P. Sormanni, G. Fusco, S. W. Chen, P. K. Challa, J. B. Kirkegaard, R. F. Laine, K. Y. Ma, M. B. D. Mu ̈ller, T. Sinnige, J. R. Kumita, S. I. A. Cohen, G. S. Kaminski Schierle, C. F. Kaminski, D. Barbut, A. De Simone, T. P. J. Knowles, M. Zasloff, E. A. A. Nollen, M. Vendruscolo and C. M. Dobson.
Comparative studies in the A30P and A53T alpha-synuclein C. elegans strains for testing candidate drugs in familial forms of Parkinson's disease.
Front. Cell Dev. Biol. 9, 552549 (2021).
T. Sinnige, G. Meisl, T. C. T. Michaels, M. Vendruscolo, T. P. J. Knowles and R. I. Morimoto.
Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans.
Proc. Natl. Acad. Sci. USA, 118, e2021888118 (2021).
T. Ikenoue, F. A. Aprile, P. Sormanni and M. Vendruscolo.
Rationally designed bicyclic peptides prevent the conversion of Abeta42 assemblies into fibrillar structures.
Front. Neurosci. 15, 623097 (2021).
K. Kulenkampff, A.-M. Wolf Perez, P. Sormanni, J. Habchi and M. Vendruscolo.
Quantification of misfolded protein oligomers as drug targets and biomarkers in Alzheimer's and Parkinson's diseases.
Nat. Rev. Chem. 5, 277-294 (2021).
G. Fani, B, Mannini, G. Vecchi, R. Cascella, C. Cecchi, C. M. Dobson, M. Vendruscolo and F. Chiti.
Abeta oligomers dysregulate calcium homeostasis by a mechanosensitive activation of AMPA and NMDA receptors.
ACS Chem. Neurosci. 12, 766-781 (2021).
W. K. Man, B. Tahirbechi, M. Vrettas, S. Preet, L. Ying, M. Vendruscolo, A. De Simone and G. Fusco.
The docking of synaptic vesicles on the presynaptic membrane induced by alpha-synuclein is modulated by lipid composition.
Nat. Comm. 12, 927 (2021).
P. R. Lindstedt, R. Taylor, G. J. L. Bernardes and M. Vendruscolo.
Facile installation of post-translational modifications on the tau protein via chemical mutagenesis.
ACS Chem. Neurosci. 12, 557-561 (2021).
G. Musteikyte, A. K. Jayaram, C. K. Xu, M. Vendruscolo, G. Krainer, T. P. J. Knowles.
Interactions of alpha-synuclein oligomers with lipid membranes.
BBA Biomembranes, 1863, 183536 (2021).
F. S. Ruggeri, J. Habchi, S. Chia, M. Vendruscolo and T. P. J. Knowles.
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Abeta42 oligomers.
Nat. Comm. 12, 668 (2021).
T. Lohr, K. Kohlhoff, G. T. Heller, C. Camilloni and M. Vendruscolo.
A kinetic ensemble of the Alzheimer's Abeta peptide.
Nat. Comp. Sci. 1, 71-78 (2021).
Z. F. Brotzakis, M. Vendruscolo and P. G. Bolhuis.
A method of incorporating rate constants as kinetic constraints in molecular dynamics simulations.
Proc. Natl. Acad. Sci. USA, 118, e2012423118 (2021).
R. Lessa Cataldi, S. Chia, K. Pisani, F. S. Ruggeri, C. Xu, T. Sneideris, M. Perni, S. Sarwat, P. Joshi, J. R. Kumita, S. Linse, J. Habchi, T. P. J. Knowles, B. Mannini, C. M. Dobson and M. Vendruscolo.
A dopamine metabolite stabilizes neurotoxic amyloid-beta oligomers.
Comm. Biol. 4, 19 (2021).
M. C. Hardenberg, T. Sinnige, S. Casford, S. Dada, C. Poudel, L. Robinson, M. Fuxreiter, C. Kaminksi, G. S. Kaminski Schierle, E. A. A. Nollen, C. M. Dobson and M. Vendruscolo.
Observation of an alpha-synuclein liquid droplet state and its maturation into Lewy body-like assemblies.
J. Mol. Cell Biol. 13, 282-294 (2021).
P. R. Lindstedt, D. A. Aprile, P. Sormanni, R. Rakoto, C. M. Dobson, G. J. L. Bernardes and M. Vendruscolo.
Systematic activity maturation of a single-domain antibody with non-canonical amino acids through chemical mutagenesis.
Cell Chem. Biol. 28, 70-77 (2021).

2020

G. T. Heller, F. A. Aprile, T. C. T. Michaels, R. Limbocker, M. Perni, F. S. Ruggeri, B. Mannini, T. Lohr, M. Bonomi, C. Camilloni, A. De Simone, I. C. Felli, R. Pierattelli, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
Small molecule sequestration of amyloid-beta as a drug discovery strategy for Alzheimer's disease.
Sci. Adv. 6, eabb5924 (2020).
R. P. Kreiser, A. K. Wright, N. R. Block, J. E. Hollows, L. T. Nguyen, K. LeForte, B. Mannini, M. Vendruscolo, R. Limbocker.
Therapeutic strategies to reduce the toxicity of protein misfolded oligomers.
Int. J. Mol. Sci. 21, 8651 (2020).
S. Errico, G. Lucchesi, D. Odino, S. Muscat, C. Capitini, C. Bugelli, C. Canale, R. Ferrando, G. Grasso, D. Barbut, M. Calamai, A. Danani, M. Zasloff, A. Relini, G. Caminati, M. Vendruscolo and F. Chiti.
Making biological membrane resistant to the toxicity of misfolded protein oligomers: a lesson from trodusquemine.
Nanoscale, 12, 22596-22614 (2020).
M. C. Hardenberg, A. Horvath, M. Fuxreiter and M. Vendruscolo.
Widespread occurrence of the droplet state of proteins in the human proteome.
Proc. Natl. Acad. Sci. USA, 117, 33254-33262 (2020).
R. Staats, T. C. T. Michaels, P. Flagmeier, S. Chia, R. Horne, J. Habchi, S. Linse, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
Screening of small molecules using as selection parameter the inhibition of oligomer formation in alpha-synuclein aggregation.
Comm. Chem. 3, 191 (2020).
M. Davies, B. Bhushan, Y. Kulaberoglu, P. Urriola-Munoz, J. Bertrand-Michel, M. Pergande, A. Smith, S. Preet, T. Park, M. Vendruscolo, K. Rankin, S. Cologna, J. Kumita, N. Cenac and E. St John Smith.
Cholesterol-rich naked mole-rat brain lipid membranes are susceptible to amyloid beta-induced damage in vitro.
Aging, 12, 22266 (2020).
A. E. Conicella, R. Huang, Z. A. Ripstein, A. Nguyen, E. Wang, T. Lohr, P. Schuck, M. Vendruscolo, J. L. Rubinstein and L. E. Kay.
An intrinsically disordered motif regulates the interaction between the p47 adaptor and the p97 AAA+ ATPase.
Proc. Natl. Acad. Sci. USA, 117, 26226-26236 (2020).
T. C. T. Michaels, A. Saric, G. Meisl, G. T. Heller, S. Curk, P. Arosio, S. Linse, C. M. Dobson, M. Vendruscolo and T. P. J. Knowles.
Thermodynamic and kinetic design principles for protein aggregation inhibitors.
Proc. Natl. Acad. Sci. USA, 117, 24251-24257 (2020).
Kinetic fingerprints differentiate the mechanisms of action of anti-Abeta antibodies.
S. Linse, T. Scheidt, K. Bernfur, M. Vendruscolo, C. M. Dobson, S. I. A. Cohen, E. Sileikis, M. Lundquist, F. Qian, T. O'Malley, T. Bussiere, P. H. Weinreb, C. K Xu, G. Meisl, S. Devenish, T. P. J. Knowles and O. Hansson.
Nat. Struct. Mol. Biol. 27, 1125-1133 (2020).
R. Limbocker, B. Mannini, F. S. Ruggeri, R. Cascella, C. K. Xu, M. Perni, S. Chia, S. W. Chen, J. Habchi, A. Bigi, R. P. Kreiser, A. K. Wright, J. A. Albright, T. Kartanas, J. R. Kumita, N. Cremades, M. Zasloff, C. Cecchi, T. P.J. Knowles, F. Chiti, M. Vendruscolo and C. M. Dobson.
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
Comm. Biol. 3, 435 (2020).
T. Ikenoue, F. A. Aprile, P. Sormanni, F. S. Ruggeri, M. Perni, G. T. Heller, C. P. Haas, C. Middel, R. Limbocker, B. Mannini, T. C. T. Michaels, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
A rationally designed bicyclic peptide remodels Abeta42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease.
Sci. Rep. 10, 1-15 (2020).
P. Flagmeier, S. De, T. C. T. Michaels, X. Yang, A. J. Dear, C. Emanuelsson, M. Vendruscolo, S. Linse, D. Klenerman, T. P. J. Knowles and C. M. Dobson.
Direct measurement of lipid membrane disruption connects kinetics and toxicity of Abeta42 aggregation.
Nat. Struct. Mol. Biol. 27, 886-891 (2020).
R. Limbocker, B. Mannini, R. Cataldi, S. Chhangur, A. K. Wright, R. P. Kreiser, J. A. Albright, S. Chia, J. Habchi, P. Sormanni, J. R. Kumita, F. S. Ruggeri, C. M. Dobson, F. Chiti, F. A. Aprile and M. Vendruscolo.
Rationally designed antibodies as research tools to study the structure-toxicity relationship of amyloid-beta oligomers.
Int. J. Mol. Sci. 21, 4542 (2020).
L. Marrone, S. Qamar, P. St George-Hyslop and M. Vendruscolo.
P525L promotes the aggregation of FUS by altering its biochemical and biophysical properties.
Matters 6, e202004000008 (2020).
F. S. Ruggeri, B. Mannini, R. Schimdt, M. Vendruscolo and T. P. J. Knowles.
Single molecule secondary structure determination of proteins through infrared absorption nanospectroscopy.
Nat. Comm. 11, 1-9 (2020).
T. Sinnige, K. Stroobants, C. M. Dobson and M. Vendruscolo.
Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases.
Q. Rev. Biophys. 53, e10 (2020).
F. A. Aprile, P. Sormanni, M. Podpolny, S. Chhangur, L.-M. Needham, F. S. Ruggeri, M. Perni, R. Limbocker, G. T. Heller, T. Sneideris, T. Scheidt, B. Mannini, J. Habchi, S. F. Lee, P. C. Salinas, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
Rational design of a conformation-specific antibody for the quantification of Abeta oligomers.
Proc. Natl. Acad. Sci. USA, 117 13509-13518 (2020). [Scholar] [PDF] [GEN]
A. Horvath, M. Miskei, V. Ambrus, M. Vendruscolo and M. Fuxreiter.
Sequence-based prediction of protein binding mode landscapes.
PLoS Comp. Biol. 16, e1007864 (2020).
E. Kelmer Sacramento, J. M. Kirkpatrick, M. Mazzetto, M. Baumgart, A. Bartolome, S. Di Sanzo, C. Caterino, M. Sanguanini, N. Papaevgeniou, M. Lefaki, D. Childs, S. Bagnoli, E. Terzibasi Tozzini, D. Di Fraia, N. Romanov, P. H. Sudmant, W. Huber, N. Chondrogianni, M. Vendruscolo, A. Cellerino and A. Ori.
Reduced proteasome activity in the aging brain results in ribosome stoichiometry loss and aggregation.
Mol. Sys. Biol. 16, e9596-e9596 (2020).
M. Sanguanini, K. N. Baumann, S. Preet, S. K. R. Chia, J. Habchi, T. P. J. Knowles and M. Vendruscolo.
Complexity in lipid membrane composition induces resilience to Abeta42 aggregatin.
ACS Chem. Neurosci. 11,1347-1352 (2020).
T. C. T. Michaels, A. Saric, S. Curk, K. Bernfur, P. Arosio, G. Meisl, A. J. Dear, S. I. A. Cohen, M. Vendruscolo, C. M. Dobson, S. Linse and T. P. J. Knowles.
Dynamics of oligomer populations formed during the aggregation of Alzheimer's Abeta42 peptide.
Nat. Chem. 12, 445-451 (2020).
M. Koopman, Q. Peter, R. I. Seinstra, M. Perni, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles and E. A. A. Nollen.
Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform.
Nat. Protoc. 15, 2071-2106 (2020).
M. Miskei, A. Horvath, M. Vendruscolo and M. Fuxreiter.
Sequence-based determinants and prediction of fuzzy interactions in protein complexes.
J. Mol. Biol. 432, 2289-2303 (2020).
R. Kundra, C. M. Dobson and M. Vendruscolo.
A cell and tissue specific weakness of the protein homeostasis system underlies brain vulnerability to protein aggregation.
iScience, 23, 100934 (2020).
S. A. Ghadami, S. K. R. Chia, F. S. Ruggeri, G. Meisl, F. Bemporad, J. Habchi, C. M. Dobson, M. Vendruscolo, T. P. J. Knowles and F. Chiti.
Transthyretin inhibits primary and secondary nucleations of amyloid-beta peptide aggregation and reduces the toxicity of Its oligomers.
Biomacromolecules 21, 1112-1125 (2020).
M. A. Metrick, N. do Carmo Ferreira, E. Saijo, A. Kraus, K. Newell, G. Zanusso, M. Vendruscolo, B. Ghetti and B. Caughey.
A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases.
Acta Neuropathol. Commun. 8, 1-13 (2020). [PDF]
X. Sui, D. E. V. Pires, A. R. Ormsby, D. Cox, S. Nie, G. Vecchi, M. Vendruscolo, D. B. Ascher, G. E. Reid, D. M. Hatters.
Widespread remodeling of proteome solubility in response to different protein homeostasis stresses.
Proc. Natl. Acad. Sci. USA 117, 2422-2431 (2020). [PDF]
G. Vecchi, P. Sormanni, B. Mannini, A. Vandelli, G. G. Tartaglia, C. M. Dobson, F. U. Hartl and M. Vendruscolo.
Proteome-wide observation of the phenomenon of life on the edge of solubility.
Proc. Natl. Acad. Sci. USA 117, 1015-1020 (2020). [PDF]
W. K. Man, A. De Simone, J. D. Barritt, M. Vendruscolo, C. M. Dobson and G. Fusco.
A role of cholesterol in modulating the binding of cholesterol in the binding of alpha-synuclein with synaptic-like vesicles.
Front. Neurosci. 14, 18 (2020). [PDF]
T. P. J. Knowles and M. Vendruscolo.
Chris Dobson (1949-2019).
Nat. Chem. Biol. 16, 105, 2020. [PDF]
G. Portella, M. Orozco and M. Vendruscolo.
Determination of a structural ensemble representing the dynamics of a G-quadruplex DNA.
Biochemistry 59, 379-388 (2020).
M. Maritan, M. Romeo, L. Oberti, P. Sormanni, M. Tasaki, R. Russo, A. Ambrosetti, P. Motta, P. Rognoni, A. Barbiroli, G. Palladini, M. Vendruscolo, L. Diomede, M. Bolognesi, G. Merlini, F. Lavatelli, S. Ricagno.
Inherent biophysical properties modulate the toxicity of soluble amyloidogenic light chains.
J. Mol. Biol. 432, 845-860 (2020).
M. Runfola, A. De Simone, M. Vendruscolo, C. M. Dobson and G. Fusco.
The N-terminal acetylation of alpha-synuclein changes the affinity for lipid membranes but not the structural properties of the bound state.
Sci. Rep. 10, 204, 2020. [PDF]

2019

J. Baum, F. Chiti, A. De Simone, T. P. J. Knowles, J. R. Kumita, S. E. Radford, C. V. Robinson, X. Salvatella, K. Valelli, M. Vendruscolo, A. Pastore, G. G. Tartaglia.
Homage to Chris Dobson.
Front. Mol. Biosci. 6, 137 (2019).
P. Ciryam, M. Antalek, F. Cid, G. G. Tartaglia, C. M. Dobson, A. Guttsches, B. Eggers, M. Vorgerd, K. Marcus, R. A. Kley, R. I. Morimoto, M. Vendruscolo and C. C. Weihl.
A metastable subproteome underlies inclusion formation in muscle proteinopathies.
Acta Neuropathol. Commun. 7, 197 (2019).
G. Meisl, T. C. T. Michaels, P, Arosio, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Dynamics and control of peptide self-assembly and aggregation.
Adv. Exp. Med. Biol. 1174, 1-33 (2019)
R. Freer, P. Sormanni, P. Ciryam, B. Rammner, S. O. Rizzoli, C. M. Dobson and M. Vendruscolo.
Supersaturated proteins are enriched at synapses and underlie cell and tissue vulnerability in Alzheimer's disease.
Heliyon, 5, e02589 (2019).
M. A. Metrick, E. Saijo, N. do Carmo Ferreira, A. G. Hughson, A. Kraus, C. D. Orru, I. Litvan, M. W. Miller, G. Zanusso, B. Ghetti, M. Vendruscolo and B. Caughey.
Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens using Hofmeister ion effects.
Proc. Natl. Acad. Sci. USA, 116, 23029-23039 (2019). [PDF]
T. Lohr, C. Camilloni, M. Bonomi, M. Vendruscolo.
A practical guide to the simultaneous determination of protein structure and dynamics using metainference.
Methods Mol Biol. 2022, 313-340 (2019).
Y.-C. Liao, M. Fernandopulle, G. Wang, H. Choi, L. Hao, C. M. Drerup, S. Qamar, J. Nixon-Abell, Y. Shen, W. Meadows, M. Vendruscolo, T. P. J. Knowles, M. Nelson, M. Czekalska, G. Musteikyte, R. Patel, C. Stephens, A. Pasolli, L. Forrest, P. St George-Hyslop, J. Lippincott-Schwartz and M. E. Ward.
RNA granules hitchhike on lysosomes for long-distance transport, using annexin A11 as a molecular tether.
Cell, 179, 147-164 (2019).
X. Wang, J. P. Kirkpatrick; H. M. M. Launay, A. De Simone, D. Haussinger, C. M. Dobson, M. Vendruscolo, L. D. Cabrita, C. A. Waudby and J. Christodoulou.
Probing the dynamic stalk region of the ribosome using solution NMR.
Sci. Rep. 9, 1-9 (2019).
B. Mannini, G. Vecchi, A. Labrador-Garrido, B. Fabre, G. Fani. J. Munoz Franco, K. Lilley, D. Pozo, M. Vendruscolo, F. Chiti, C. M. Dobson, C. Roodveldt.
Differential interactome and innate immune response activation of two structurally distinct misfolded protein oligomers.
ACS Chem. Neurosci. 10, 3464-3478 (2019).
S. De, D. R. Whiten, F. S. Ruggeri, C. Hughes, M. Rodrigues, D. I. Sideris, C. G. Taylor, F. A. Aprile, S. Muyldermans, T. P. J. Knowles, M. Vendruscolo, C. Bryant, K. Blennow, I. Skoog, S. Kern, H. Zetterberg, D. Klenerman.
Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression.
Acta Neuropathol. Commun. 7, 120 (2019).
D. C. Delivoria, S. Chia, J. Habchi, M. Perni, I. Matis, N. Papaevgeniou, N. Chondrogianni, C. M. Dobson, M. Vendruscolo and C. Skretas.
Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation.
Sci. Adv. 5, eaax5108 (2019).
M. Bonomi, G. Bussi, C. Camilloni, G. A. Tribello, P. Banas, A. Barducci, M. Bernetti, P. G. Bolhuis, S. Bottaro, D. Branduardi, R. Capelli, P. Carloni, M. Ceriotti, A. Cesari, H. Chen, W. Chen, F. Colizzi, S. De, M. De La Pierre, D. Donadio, V. Drobot, B. Ensing, A. L. Ferguson, M. Filizola, J. S. Fraser, H. Fu, P. Gasparotto, F. L. Gervasio, F. Giberti, A. Gil-Ley, T. Giorgino, G. T. Heller, G. M. Hocky, M. Iannuzzi, M. Invernizzi, K. E. Jelfs, A. Jussupow, E. Kirilin, A. Laio, V. Limongelli, K. Lindorff-Larsen, T. Lohr, F. Marinelli, L. Martin-Samos, M. Masetti, R. Meyer, A. Michaelides, C. Molteni, T. Morishita, M. Nava, C. Paissoni, E. Papaleo, M. Parrinello, J. Pfaendtner, P. Piaggi, G. Piccini, A. Pietropaolo, F. Pietrucci, S. Pipolo, D. Provasi, D. Quigley, P. Raiteri, S. Raniolo, J. Rydzewski, M. Salvalaglio, G. C. Sosso, V. Spiwok, J. Sponer, D. W. H. Swenson, P. Tiwary, O. Valsson, M. Vendruscolo, G. A. Voth and A. White.
Promoting transparency and reproducibility in enhanced molecular simulations.
Nat. Methods, 16, 670-673 (2019).
P. R. Lindstedt, F. A. Aprile, M. J. Matos, M. Perni, J. B. Bertoldo, B, Bernardim, Q. Peter, F. Corzana, G. Jimenez-Oses, T. P. J. Knowles, C. M. Dobson, M. Vendruscolo and G. J. L. Bernardes.
Enhancement of the anti-aggregation activity of a molecular chaperone using a rationally designed post-translational modification.
ACS Cent. Sci. 5, 1417-1424 (2019).
L. Zhao, G. Vecchi, M. Vendruscolo, R. Korner, M. Hayer-Hartl and F. U. Hartl.
The Hsp70 chaperone system stabilizes a thermo-sensitive subproteome in E. coli.
Cell Rep. 28, 1335-1345 (2019).
F. S. Ruggeri, T. Sneideris, S. Chia, M. Vendruscolo and T. P. J. Knowles.
Characterising individual amyloid aggregates by infrared nanospectroscopy and atomic force microscopy.
JoVE, 151, e60108 (2019).
T. Sinnige, P. Ciryam, S. Casford, C. M. Dobson, M. de Bono and M. Vendruscolo.
Expression of the amyloid-beta peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response.
PLoS One, 14, e0217746 (2019).
R. F. Laine T. Sinnige, K. Y. Ma, A. Haack, C. Poudel, P. Gaida, N. Curry, M. Perni, E. A.A. Nollen, C. M. Dobson, M. Vendruscolo, G. S Kaminski Schierle and C. F. Kaminski.
Fast fluorescence lifetime imaging reveals the maturation process of alpha-synuclein aggregates in ageing Caenorhabditis elegans.
ACS Chem. Biol. 14, 1628-1636 (2019).
R. Cascella, M. Perni, S. W Chen, G. Fusco, C. Cecchi, M. Vendruscolo, F. Chiti, C. M. Dobson and A. De Simone.
Probing the origin of the toxicity of oligomeric aggregates of alpha-synuclein with antibodies.
ACS Chem. Biol. 14, 1352-1362 (2019).
C. Huang, S. Wagner-Valladolid, A. D Stephens, R. Jung, C. Poudel, T. Sinnige, M. C. Lechler, N. Schlorit, R. F Laine, C. H. Michel, M. Vendruscolo, C. F. Kaminski, G. S. Kaminski Schierle and D. David.
Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans.
eLife, 8, e43059 (2019).
C. Torrini, R. J. Cubero, E. Dirkx, L. Braga, H. Ali, G. Prosdocimo, M. I. Gutierrez, C. Collesi, D. Licastro, L. Zentilin, M. Mano, M. Vendruscolo, M. Marsili, A. Samal and M. Giacca.
Common regulatory pathways mediate activity of microRNAs inducing cardiomyocyte proliferation.
Cell Rep. 27, 2759-2771 (2019).
L. Eshun-Wilson, R. Zhang, D. Portran, M. Nachury, D. Toso, T. Lohr, M. Vendruscolo, M. Bonomi, J. Fraser and E. Nogales.
Effects of alpha-tubulin acetylation on microtubule structure and stability.
Proc. Natl. Acad. Sci. USA, 116, 10366-10371 (2019).
J. J. Yerbury, L. Ooi, I. Blair, P. Ciryam, C. M. Dobson and M. Vendruscolo.
The metastability of the proteome of spinal motor neurons underlies their selective vulnerability in ALS.
Neurosci. Lett. 704, 89-94 (2019).
N. Ahmed, P. Sormanni, P. Ciryam, M. Vendruscolo, C. M. Dobson and E. P. O'Brien.
Identifying A- and P-site locations on ribosome-protected mRNA fragments using integer programming.
Sci. Rep. 9, 6256 (2019).
P. Kukic, G. M. Lo Piccolo, M. O. Nogueira, D. Svergun, M. Vendruscolo, I. C. Felli and R. Pierattelli.
The free energy landscape of the oncogene protein E7 of human papillomavirus type 16 reveals a complex interplay between ordered and disordered regions.
Sci. Rep. 9, 5822 (2019).
S. De, D. C. Wirthensohn, P. Flagmeier, C. Hughes, F. A. Aprile, F. S. Ruggeri, D. R. Whiten, D. Emin, J. A. Varela, P. Sormanni, F. Kundel, T. P. J. Knowles, C. M. Dobson, C. Bryant, M. Vendruscolo, D. Klenerman.
Different soluble aggregates of Abeta42 can give rise to cellular toxicity through different mechanisms.
Nat. Comm. 10, 1541 (2019).
T. Scheidt, U. Lapinska, J. R. Kumita, D. R. Whiten, D. Klenerman, M. R. Wilson, S. I. A. Cohen, S. Linse, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles and P. Arosio.
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-beta aggregates.
Sci. Adv. 5, eaau3112 (2019).
F. S. Ruggeri, T. Sneideris, M. Vendruscolo, T. P. J. Knowles.
Atomic force microscopy for single molecule characterisation of protein aggregation.
Arch. Biochem. Biophys. 664, 134-148 (2019).
C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
The amyloid phenomenon and its significance in biology and medicine.
Cold Spring Harb. Perspect. Biol. 033878 (2019).
P. Sormanni and M. Vendruscolo.
Protein solubility predictions using the CamSol method in the study of protein homeostasis.
Cold Spring Harb. Perspect. Biol. a033845 (2019).
M. Ahn, B. I. Lee, S. Chia, J. Habchi, J. R. Kumita, M. Vendruscolo, C. M. Dobson and C. B. Park.
Chemical and mechanistic analysis of photodynamic inhibition of Alzheimer's beta-amyloid aggregation.
Chem. Comm. 55, 1152-1155 (2019).
A. M. da Silva Neto, S. R. Silva, M. Vendruscolo, C. Camilloni and R. W. Montalvao.
A superposition free method for protein conformational ensemble analyses and local clustering based on a differential geometry representation of backbone.
Proteins, 87, 302-312 (2019).
K. Sanagavarapu, E. Nuske, I. Nasir, G. Meisl, J. N. Immink, P. Sormanni, M. Vendruscolo, T. P. J. Knowles, A. Malmendal, C. Cabaleiro-Lago and S. Linse.
A method of predicting the fibril formation propensity of Abeta40 mutants based on their inclusion body levels in E. coli.
Sci. Rep. 9, 3680 (2019).
A.-M. Wolf Perez, P. Sormanni, J. S. Andersen, L. I. Sakhnini, I. Rodriguez-Leon, J. R. Bjelke, A. J. Gajhede, L. De Maria, D. E. Otzen, M. Vendruscolo and N. Lorenzen.
In vitro and in silico assessment of the developability of a designed monoclonal antibody library.
mAbs, 11, 388-400 (2019). [PDF]
M. Bonomi and M. Vendruscolo.
Determination of protein structural ensembles using cryo-electron microscopy.
Curr. Op. Struct. Biol. 56, 37-45, (2019). [PDF]
H. Fu, A. Possenti, R. Freer, Y. Nakano, N. C. Hernandez Villegas, M. Tang, P. V. M. Cauhy, B. A. Lassus, S. Chen, S. L. Fowler, H. Y. Figueroa, E. D. Huey, G. V. W. Johnson, M. Vendruscolo and K. E. Duff.
A tau homeostasis signature is linked with the cellular and regional vulnerability of excitatory neurons to tau pathology.
Nat. Neurosci. 22, 47-56 (2019). [PDF] [Alzforum]
R. Limbocker, S. Chia, F. S. Ruggeri, M. Perni, R. Cascella, G. T. Heller, G. Meisl, B. Mannini, J. Habchi, T. C. T. Michaels, P. K. Challa, M. Ahn, S. T. Casford, N. Fernando, C. K. Xu, N. D. Kloss, S. I. A. Cohen, J. R. Kumita, C. Cecchi, M. Zasloff, S. Linse, T. P. J. Knowles, F. Chiti, M. Vendruscolo, C. M. Dobson.
Trodusquemine enhances Abeta42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes.
Nat. Comm. 10, 225 (2019). [PDF]

2018

P. Sormanni, F. A. Aprile and M. Vendruscolo.
Third generation antibody discovery methods: In silico rational design.
Chem. Soc. Rev. 47, 9137-9157 (2018). [PDF]
R. Rangan, M. Bonomi, G. T. Heller, A. Cesari, G. Bussi and M. Vendruscolo.
Determination of structural ensembles of proteins: restraining vs reweighting.
J. Chem. Theory Comput. 14, 6632-6641 (2018).
M. Perni, S. Casford, F. A. Aprile, E. A. A. Nollen, T. P. J. Knowles, M. Vendruscolo and C. M. Dobson.
Automated behavioural analysis of large C. elegans populations using a wide field of view tracking platform.
JoVE, 141, e58643 (2018).
S. Chia, J. Habchi, T. C. T. Michaels, S. I. A. Cohen, S. Linse, C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
SAR by kinetics for drug discovery for protein misfolding diseases.
Proc. Natl. Acad. Sci. USA 115, 10245-10250 (2018). [PDF]
M. Bonomi, S. Hanot, C. H. Greenberg, A. Sali, M. Nilges, M. Vendruscolo and R. Pellarin.
Bayesian weighting of electron cryo-microscopy data for integrative structural modeling.
Structure, 27, 175-188 (2019).
F. S. Ruggeri, J. Charmet, T. Kartanas, Q. Peter, S. K. R. Chia, J. Habchi, C. M. Dobson, M. Vendruscolo and T. P. J. Knowles.
Microfluidic deposition for resolving single molecule protein architecture and heterogeneity.
Nat. Comm. 9, 3890 (2018) [PDF]
C. A. Waudby, M.-E. Karyadi, T. Wlodarski, A. M. E. Cassaignau, S. Chan, J. M. Schmidt-Engler, A. S. Wentink, C. Camilloni, M. Vendruscolo, C. D. Cabrita and J. Christodoulou.
Systematic mapping of free energy landscapes of a growing filamin domain during biosynthesis.
Proc. Natl. Acad. Sci. USA, 115, 9744-9749 (2018). [PDF]
G. Tomba, C. Camilloni and M. Vendruscolo.
Determination of the conformational states of strychnine using NMR residual dipolar couplings in a tensor-free approach.
Methods, 148, 4-8 (2018). [PDF]
B. Mannini, J. Habchi, S. K. R. Chia, F. S. Ruggeri, M. Perni, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
Stabilization and characterization of cytotoxic Abeta40 oligomers isolated from an aggregation reaction in the presence of zinc ions.
ACS Chem. Neurosci. 9, 2959-2971 (2018). [PDF]
C. Capitini, J. R. Patel, A. Natalello, C. D'Andrea, A. Relini, J. A. Jarvis, L. Birolo, A. Peduzzo, M. Vendruscolo, P. Matteini, C. M. Dobson, A. De Simone and F. Chiti.
Structural differences between toxic and nontoxic HypF-N oligomers.
Chem. Comm. 54, 8637-8640 (2018). [PDF]
E. Papaleo, C. Camilloni, K. Teilum, M. Vendruscolo and K. Lindorff-Larsen.
Molecular dynamics ensemble refinement of the heterogeneous native state of NCBD using chemical shifts and NOEs.
PeerJ 6, e5125 (2018). [PDF]
M. Perni, P. Flagmeier, R. Limbocker, R. Cascella, F. A. Aprile, C. Galvagnion, G. Meisl, S. W. Chen, J. R. Kumita, P. K. Challa, J. B. Kirkegaard, S. I. A. Cohen, D. Barbut, E. A. A. Nollen, C. Cecchi, N. Cremades, T. P. J. Knowles, F. Chiti, M. Zasloff, M. Vendruscolo and C. M. Dobson.
Multistep inhibition of alpha-synuclein aggregation and toxicity in vitro and in vivo by trodusquemine.
ACS Chem. Biol. 13, 2308-2319 (2018). [PDF]
S. Vahidi, Z. A. Ripstein, M. Bonomi, T. Yuwen, M. F. Mabanglo, J. B. Juravsky, K. Rizzolo, A. Velyvis, W. A. Houry, M. Vendruscolo, J. L. Rubinstein and L. E Kay.
Reversible inhibition of the ClpP protease via an N-terminal conformational switch.
Proc. Natl. Acad. Sci. USA, 115, E6447-E6456 (2018). [PDF]
M. A. Wright, F. A. Aprile, M. M. J. Bellaiche, T. C. T. Michaels, T. Muller, P. Arosio, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Cooperative assembly of Hsp70 subdomain clusters.
Biochemistry, 57, 3641-3649 (2018). [PDF]
A. Possenti, M. Vendruscolo, C. Camilloni and G. Tiana.
A method of partitioning the information contained in a protein sequence between its structure and function.
Proteins, 86, 956-964 (2018).
M. N. Bongiovanni, F. A. Aprile, P. Sormanni and M. Vendruscolo.
A rationally designed Hsp70 variant rescues the aggregation-associated toxicity of hIAPP in pancreatic islet beta-cells.
Int. J. Mol. Sci. 19, 1443 (2018). [PDF]
F. El Turk, E. De Genst, T. Guilliams, B. Fauvet, M. Hejjaoui, M. Vendruscolo, H. A. Lashuel and C. M. Dobson.
Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding.
Protein Sci. 27, 1262-1274 (2018). [PDF]
G. T. Heller, M. Bonomi and M. Vendruscolo.
Structural ensemble modulation upon small molecule binding to disordered proteins.
J. Mol. Biol. 430, 2288-2292 (2018). [PDF]
E. Liberis, P. Velickovic, P. Sormanni, M. Vendruscolo and Pietro Lio'.
Parapred: Antibody paratope prediction using convolutional and recurrent neural networks.
Bioinformatics, 34, 2944-2950 (2018). [PDF]
G. Fusco, M. Sanz-Hernandez, F. S. Ruggeri, M. Vendruscolo, C. M. Dobson and A. De Simone.
Molecular determinants of the interaction of EGCG with ordered and disordered proteins.
Biopolymers, e23117 (2018). [PDF]
M. Perni, P. K. Challa, J. B. Kirkegaard, R. Limbocker, M. Koopman, M. C. Hardenberg, P. Sormanni, T. Muller, K. L. Saar, L. Roode, J. Habchi, G. Vecchi, N. Fernando, E. A. A. Nollen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery.
J. Neurosci. Methods, 306, 57-67 (2018). [PDF]
J. Habchi, S. Chia, C. Galvagnion, T. C. T. Michaels, M. Bellaiche, F. S. Ruggeri, M. Sanguanini, I. Idini, J. R. Kumita, E. Sparr, S. Linse, C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
Cholesterol catalyses Abeta42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes.
Nat. Chem. 10, 673-683 (2018). [PDF] [Alzforum]
M. Bonomi, R. Pellarin and M. Vendruscolo.
Simultaneous determination of protein structure and dynamics using cryo-electron microscopy.
Bioph. J. 114, 1604-1613 (2018). [PDF]
S. Qamar, G. Z. Wang, S. Randle, F. S. Ruggeri, A. Miyashita, E. Phillips, J. A. Varela, J. Q. Lin, D. Williams, W. Meadows, R. Ferry, G. G. Tartaglia, L. A. Farrer, C. Holt, G. Schmitt-Ulms, D. Klenerman, T. P. J. Knowles, M. Vendruscolo, P. St George-Hyslop.
FUS phase separation Is modulated by a molecular chaperone and methylation of arginine cation-pi interactions.
Cell 173, 720-734 (2018). [PDF] [BBC News]
T. C. T. Michaels, A. Saric, J. Habchi, S. Chia, G. Meisl, M. Vendruscolo, C. M. Dobson, and T. P. J. Knowles.
Chemical kinetics for bridging molecular mechanisms and macroscopic measurements of amyloid fibril formation.
Annu. Rev. Phys. Chem. 69, 273-298 (2018). [PDF]
S. I. A. Cohen, R. Cukalevski, T. C. T. Michaels, A. Saric, M. Vendruscolo, C. M. Dobson, A. K. Buell, T. P. J. Knowles and S. Linse.
Distinct thermodynamic signature of oligomer generation in the aggregation of the amyloid-beta peptide.
Nat. Chem. 10, 523-531 (2018). [PDF]
D. Piovesan, F. Tabaro, L. Paladin, M. Necci, I. Micetic, C. Camilloni, D. Davey, Z. Dosztanyi, B. Meszaros, A. Monzon, G. Parisi, E. Schad, P. Sormanni, P. Tompa, M. Vendruscolo, W. Vranken, S, Tosatto.
MobiDB 3.0: More annotations for intrinsic disorder, conformational diversity and interactions in proteins.
Nucl. Acids Res. 46, D471-D476 (2018). [PDF]

2017

G. Fusco, S. W. Chen, P. T. Williamson, R. Cascella, M. Perni, J. A. Jarvis, C. Cecchi, M. Vendruscolo, F. Chiti, N. Cremades, L. Ying, C. M. Dobson and A. De Simone.
Structural basis of membrane disruption and cellular toxicity by alpha-synuclein oligomers.
Science 358, 1440-1443 (2017). [PDF]
N. Maritinez-Saez, S. Sun, D. Oldrini, P. Sormanni, O. Boutureira, F. Carboni, I. Companon, M. Deery, M. Vendruscolo, F. Corzana, R. Adamo, G. J. L. Bernardes.
Oxetane grafts site-selectively installed on native disulfides enhance protein stability and activity in vivo.
Angew. Chem. Intl. Ed. 56, 14963-14967 (2017). [PDF]
M. Perni, F. A. Aprile, S. Casford, B. Mannini, P. Sormanni, C. M. Dobson and M. Vendruscolo.
Delivery of native proteins into C. elegans using a transduction protocol based on lipid vesicles.
Sci. Rep. 7, 15045 (2017). [PDF]
G. Meisl, L. Rajah, S. I. A. Cohen, M. Pfammatter, A. Saric, E. Hellstrand, A. K. Buell, A. Aguzzi, S. Linse, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Reaction network connectivity governs scaling behaviour and rate-determining steps in filamentous self-assembly.assembly
Chem. Sci. 8, 7087-7097 (2017). [PDF]
G. T. Heller, F. A. Aprile, M. Bonomi, C. Camilloni, A. De Simone and M. Vendruscolo.
Sequence specificity in the entropy-driven binding of a small molecule and a disordered peptide.
J. Mol. Biol. 429, 2772-2779 (2017). [PDF]
F. A. Aprile, M. Vendruscolo, D. Ron and C. Hansen.
The molecular chaperones DNAJB6 and Hsp70 cooperate to suppress alpha-synuclein aggregation.
Sci. Rep. 7, 9039 (2017). [PDF]
P. Sormanni, L. Amery, S. Ekizoglou, M. Vendruscolo and B. Popovic.
Rapid and accurate in silico solubility screening of a monoclonal antibody library.
Sci. Rep. 7, 8200 (2017). [PDF]
M. Iljina, L. Hong, M. H. Horrocks, M. H. Ludtmann, M. L. Choi, C. D. Hughes, F. S. Ruggeri, T. Guilliams, A. K. Buell, J.-E. Lee, S. Gandhi, S. F. Lee, C. E. Bryant, M. Vendruscolo, T. P. J. Knowles, C. M. Dobson, E. De Genst, D. Klenerman.
Nanobodies raised against monomeric alpha-synuclein inhibit fibril formation and destabilize toxic oligomeric species of alpha-synuclein.
BMC Biol. 15, 57 (2017). [PDF]
S. Chia, P. Flagmeier, J. Habchi, V. Lattanzi, S. Linse, C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
Monomeric and fibrillar alpha-synuclein exert opposite effects on the catalytic cycle that promotes the proliferation of Abeta42 aggregates.
Proc. Natl. Acad. Sci. USA, 114, 8005-8010 (2017). [PDF]
R. Kundra, P. Ciryam, R. I. Morimoto, C. M. Dobson and M. Vendruscolo.
Protein homeostasis of a metastable subproteome associated with Alzheimer's disease.
Proc. Natl. Acad. Sci. USA, 114, E5703-E5711 (2017). [PDF]
A. Munke, J. Persson, T. Weiffert, E. J. J. de Genst, G. Meisl, P. Arosio, C. M Dobson, M. Vendruscolo, T. P. J. Knowles and S. Linse.
Phage display and kinetic selection of antibodies that selectively inhibit amyloid self-replication.
Proc. Natl. Acad. Sci. USA, 14, 6444-6449 (2017). [PDF]
K. Stroobants, J. R. Kumita, N. Harris, D. Y. Chirgadze, C. M. Dobson, P. J. Booth and M. Vendruscolo.
Amyloid-like fibrils from an alpha-helical transmembrane protein.
Biochemistry, 56, 3225-3233 (2017). [PDF]
F. A. Aprile, P. Sormanni, M. Perni, P. Arosio, S. Linse, T. P. J. Knowles, C. M. Dobson and Michele Vendruscolo.
Selective targeting of primary and secondary nucleation pathways in Abeta42 aggregation using a rational antibody scanning method.
Sci. Adv. 3, e1700488 (2017). [PDF]
G. T. Heller, F. A. Aprile and M. Vendruscolo.
Methods of probing the interactions between small molecules and disordered proteins.
Cell. Mol. Life Sci. 74, 3225-3243 (2017). [PDF]
P. Kukic, Y. Pustovalova, C. Camilloni, S. Gianni, D. M. Korzhnev and M. Vendruscolo.
Structural characterisation of the early events in the nucleation-condensation mechanism in a protein folding process.
J. Am. Chem. Soc. 139, 6899-6910 (2017). [PDF]
J. Kitevski-LeBlanc, A. Fradet-Turcotte, P. Kukic, G. Portella, T. Yuwen, M. D. Wilson, S. Panier, S. Duan, M. D. Canny, H. van Ingen, C. Arrowsmith, J. L. Rubinstein, M. Vendruscolo, D. Durocher and L. E. Kay.
RNF168 and RNF169 define a new class of ubiquitylated-histone reader involved in the response to DNA damage.
eLife 6, e23872 (2017). [PDF]
G. Hultqvist, E. Aberg, C. Camilloni, G. Sundell, E. Andersson, J. Dogan, M. Vendruscolo and P. Jemth.
Emergence and evolution of an interaction between intrinsically disordered proteins.
eLife 6, e16059 (2017). [PDF]
Y. Yoshimura, M. A. Holmberg, P. Kukic, C. B. Andersen, A. Mata-Cabana, M. Vendruscolo, E. A.A. Nollen and F. A.A. Mulder.
MOAG-4 promotes the aggregation of alpha-synuclein by competing with self-protective electrostatic interactions.
J. Biol. Chem. 292, 8269-8278 (2017). [PDF]
P. Ciryam, I. Lambert-Smith, D. M. Bean, R. Freer, F. Cid, G. G. Tartaglia, D. N. Saunders, M. R. Wilson, S. G. Oliver, R. I. Morimoto, C. M. Dobson, M. Vendruscolo, G. Favrin and J. J. Yerbury.
Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.
Proc. Natl. Acad. Sci. USA 114, E3935-E3943 (2017). [PDF]
F. A. Aprile, P. Arosio, G. Fusco, S. W. Chen, J. R Kumita, A. Dhulesia, P. Tortora, T. P. J. Knowles, M. Vendruscolo, C. M. Dobson and N. Cremades.
Inhibition of alpha-synuclein fibril elongation by Hsp70 is governed by a kinetic binding competition between alpha-synuclein species.
Biochemistry 56, 1177-1180, 2017. [PDF]
O. Sin, T. de Jong, A. Mata-Cabana, M. Kudron, R. Seinstra, A. Zaini, F. A. Aprile, R. Seinstra, E. Stroo, R. Willinge Prins, C. Martineau, H. H. Wang, W. Hogewerf, A. Steinhof, E. E. Wanker, M. Vendruscolo, C. F. Calkhoven, V. Reinke, V. Guryev and E. A. A. Nollen.
Identification of a small non-coding RNA Pol III-associated regulator linked with disease-associated protein aggregation.
Mol. Cell 65, 1096-1108, 2017. [PDF]
M. J. Holliday, C. Camilloni, G. S. Armstrong, M. Vendruscolo and E. Z. Eisenmesser.
Networks of dynamic allostery control enzyme function.
Structure 25, 276-286 (2017). [PDF]
P. Sormanni, D. Piovesan, G. T. Heller, M. Bonomi, P. Kukic, C. Camilloni, M. Fuxreiter, Z. Dosztanyi, R. Pappu, M. M. Babu, S. Longhi, P. Tompa, A. K. Dunker, V. N. Uversky, S. C. E. Tosatto and M. Vendruscolo.
Simultaneous quantification of order and disorder in proteins.
Nat. Chem. Biol. 13, 339-342 (2017). [PDF]
M. Bonomi, G. T. Heller, C. Camilloni and M. Vendruscolo.
Principles of protein structural ensemble determination.
Curr. Op. Struct. Biol. 42, 106-116 (2017). [PDF]
A. N. Borkar, P. Vallurupalli, C. Camilloni, L. E. Kay, and M. Vendruscolo.
Simultaneous NMR characterisation of multiple minima in the free energy landscape of an RNA UUCG tetraloop.
Phys. Chem. Chem. Phys. 19, 2797-2804 (2017). [PDF]
M. Perni, C. Galvagnion, A. S. Maltsev, G. Meisl, M. B. D. Muller, P. K. Challa, J. B. Kirkegaard, P. Flagmeier, S. I. A. Cohen, R. Cascella, S. W. Chen, R. Limbocker, P. Sormanni, G. T. Heller, F. A. Aprile, N. Cremades, C. Cecchi, F. Chiti, E. A. A. Nollen, T. P. J. Knowles, M. Vendruscolo, A. Bax, M. Zasloff, C. M. Dobson
A natural product inhibits the initiation of alpha-synuclein aggregation by displacing it from lipid membranes and suppresses its toxicity.
Proc. Natl. Acad. Sci. USA 114, E1009-E1017 (2017). [PDF]
J. Habchi, S. Chia, R. Limbocker, B. Mannini, M. Ahn, M. Perni, O. Hansson, P. Arosio, J. R. Kumita, P. K. Challa, S. I. A. Cohen, S. Linse, C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
Systematic development of small molecules to inhibit specific microscopic steps of Abeta42 aggregation in Alzheimer's disease.
Proc. Natl. Acad. Sci. USA 114, E200-E208 (2017). [PDF]

2016

J. W. P. Brown, A. K. Buell, T. C. T. Michaels, G. Meisl, J. Carozza, P. Flagmeier, M. Vendruscolo, T. P. J. Knowles, Christopher M. Dobson, C. Galvagnion.
beta-synuclein suppresses both the initiation and amplification steps of alpha-synuclein aggregation via competitive binding to surfaces.
Sci. Rep. 6, 36010 (2016). [PDF]
P. Flagmeier, G. Meisl, M. Vendruscolo, T. P. J. Knowles, C. M. Dobson, A. K. Buell and C. Galvagnion.
Mutations associated with familial Parkinson's disease alter the initiation and amplification steps of alpha-synuclein aggregation.
Proc. Natl. Acad. Sci. USA, 113, 10328-10333 (2016). [PDF]
G. Fusco, T. Pape, P. Mahou, P. Arosio, A. Rita Costa, G. Kaminski-Schierle, M. Vendruscolo, G. Veglia, C. M. Dobson and A. De Simone.
Structural basis of synaptic vesicle assembly promoted by alpha-synuclein.
Nat. Comm. 7, 12563 (2016). [PDF]
R. Freer, P. Sormanni, G. Vecchi, P. Ciryam, C. M. Dobson and M. Vendruscolo.
A protein homeostasis signature in healthy brains recapitulates tissue vulnerability to Alzheimer's disease.
Sci. Adv. 2, e1600947 (2016). [PDF] [The Guardian]
M. Bonomi, C. Camilloni and M. Vendruscolo.
Metadynamic metainference: Enhanced sampling of the metainference ensemble using metadynamics.
Sci. Rep. 6, 31232 (2016). [PDF]
C. Galvagnion, J. Brown, M. M. Ouberai, P. Flagmeier, M. Vendruscolo, A. K. Buell, E. Sparr and C. M. Dobson.
Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of alpha-synuclein.
Proc. Natl. Acad. Sci. USA, 113, 7065-7070 (2016). [PDF]
G. Fusco, A. De Simone, P. Arosio, M. Vendruscolo, G. Veglia, C. M. Dobson.
Structural ensembles of the membrane-bound alpha-synuclein reveal the molecular determinants of synaptic vesicle affinity.
Sci. Rep. 6, 27125 (2016). [PDF]
C. Camilloni, D. Bonetti, A. Morrone, R. Giri, C. M. Dobson, M. Brunori, S. Gianni and M. Vendruscolo.
Towards a structural biology of the hydrophobic effect in protein folding.
Sci. Rep. 6, 28285, (2016). [PDF]
A. N. Borkar, M. F. Bardaro, C. Camilloni, F. A. Aprile, G. Varani and M. Vendruscolo.
Structure of a low-population binding intermediate in protein-RNA recognition.
Proc. Natl. Acad. Sci. USA, 113, 7171-7176 (2016). [PDF]
F. El-Turk, F. Newby, E. J. de Genst, T. Guilliams, T. Sprules, A. Mittermaier, C. M. Dobson and M. Vendruscolo.
Structural effects of two camelid nanobodies directed to distinct C-terminal epitopes on alpha-synuclein.
Biochemistry, 55, 3116-3122 (2016). [PDF]
C. Camilloni, B. M. Sala, P. Sormanni, R. Porcari, A. Corazza, M. De Rosa, S. Zanini, A. Barbiroli, G. Esposito, M. Bolognesi, V. Bellotti, M. Vendruscolo and S. Ricagno.
Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability.
Sci. Rep. 6, 25559 (2016). [PDF]
T. Muller, P. Arosio, L. Rajah, S. I. A. Cohen, E. V. Yates, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Particle-based Monte-Carlo simulations of steady-state mass transport at intermediate Peclet numbers.
Int. J. Nonlinear Sci. Numer. Simul. 17, 175-183 (2016). [PDF]
D. Bonetti, C. Camilloni, L. Visconti, S. Longhi, M. Brunori, M. Vendruscolo and S. Gianni.
Identification and structural characterization of an intermediate in the folding of the measles virus X domain.
J. Biol. Chem. 291, 10886-10892 (2016). [PDF]
P. Ciryam, R. Kundra, R. Freer, R. I. Morimoto, C. M. Dobson and M. Vendruscolo.
A transcriptional signature of Alzheimer's disease is associated with a metastable subproteome at risk of aggregation.
Proc. Natl. Acad. Sci. USA, 113, 4753-4758 (2016). [PDF]
A. Deckert, C. A. Waudby, T. Wlodarski, A. S. Wentink, X. Wang, J. F. S. Paton, C. Camilloni, P. Kukic, C. M. Dobson, M. Vendruscolo, L. D. Cabrita and J. Christodoulou.
Structural characterization of the interaction of alpha-synuclein nascent chains with the ribosomal surface and trigger factor.
Proc. Natl. Acad. Sci. USA, 113, 5012-5017 (2016). [PDF]
P. Joshi, S. Chia, J. Habchi, T. P. J. Knowles, C. M. Dobson and M. Vendruscolo.
A fragment-based method of generating small molecule libraries to target the aggregation of intrinsically disordered proteins.
ACS Comb. Sci. 18, 144-153 (2016). [PDF] [Cover]
P. Arosio, T. C. T. Michaels, S. Linse, C. Mansson, C. Emanuelsson, J. Presto, J. Johansson, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation.
Nat. Comm. 7, 10948 (2016). [PDF]
A. Toto, C. Camilloni, R. Giri, M. Brunori, M. Vendruscolo and S. Gianni.
Molecular recognition by templated folding of an intrinsically disordered protein.
Sci. Rep. 6, 21994 (2016). [PDF]
J. Habchi, P. Arosio, M. Perni, A. R. Costa, M. Yagi-Utsumi, P. Joshi, S. Chia, S. I. A. Cohen, M. B. D. Muller, S. Linse, E. A. A. Nollen, C. M. Dobson, T. P. J. Knowles and M. Vendruscolo.
An anti-cancer drug suppresses the primary nucleation reaction that initiates the formation of toxic Abeta aggregates linked with Alzheimer's disease.
Sci. Adv. 2, e1501244 (2016). [PDF] [BBC News]
L. D. Cabrita, A. M.E. Cassaignau, H. M.M. Launay, C. A. Waudby, C. Camilloni, A. L. Robertson, X. Wang, T. Wlodarski, A. S. Wentink, C. A. Woolhead, M. Vendruscolo, C. M. Dobson and J. Christodoulou.
A structural ensemble of a ribosome-nascent chain complex during in vivo co-translational protein folding.
Nat. Struct. Mol. Biol. 23, 278-285 (2016). [PDF]
P. Arosio, T. Muller, L. Rajah, E. V. Yates, F. A. Aprile, Y. Zhang, S. I. A. Cohen, D. A. White, T. Herling, E. De Genst, S. Linse, M. Vendruscolo, C. M. Dobson, and Tuomas P. J. Knowles.
Microfluidic diffusion analysis of sizes and interactions of protein solutions under native conditions.
ACS Nano, 10, 333-341 (2016). [PDF]
P. Kukic, P. Lundstrom, C. Camilloni, J. Evenas, M. Akke and M. Vendruscolo.
Structural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Biochemistry, 55, 19-28 (2016). [PDF]
M. Bonomi, C. Camilloni, A. Cavalli and M. Vendruscolo.
Metainference: A Bayesian inference method for heterogeneous systems.
Sci. Adv. 2, e1501177 (2016). [PDF]
T. C. T. Michaels, S. I. A. Cohen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Hamiltonian dynamics of protein filament formation.
Phys. Rev. Lett. 116, 038101 (2016). [PDF]
G. Meisl, J. B. Kirkegaard, M. Vendruscolo, C. M. Dobson, S. Linse and T. P. J. Knowles.
Molecular mechanisms of protein aggregation from global fitting of kinetic models.
Nat. Protoc. 11, 252-272 (2016). [PDF]
I. Ivani, P. D. Dans, A. Noy, A. Perez, I. Faustino, A. Hospital, J. Walther, P. Andrio, R. Goni, A. Balaceanu, G. Portella, F. Battistini, J. L. Gelpi, C. Gonzalez, M. Vendruscolo, C. A. Laughton, S. A. Harris, D. A. Case and M. Orozco.
PARMBSC1: A refined force field for DNA simulations.
Nat. Methods 13, 55-58 (2016) [PDF]

2015

C. Camilloni and M. Vendruscolo.
Using pseudocontact shifts and residual dipolar couplings as exact NMR restraints for the determination of protein structural ensembles.
Biochemistry, 54, 7470-7476 (2015). [PDF]
F. Newby, A. De Simone, M. Yagi-Utsumi, X. Salvatella, C. M. Dobson and M. Vendruscolo.
Structure-free validation of RDC and PRE measurements of disordered proteins.
Biochemistry, 54, 6876-6886 (2015). [PDF]
T. Murakami, S. Qamar, J. Q. Lin, G. S. Kaminski Schierle, E. Rees, A. Miyashita, A. R. Costa, R. B. Dodd, F. T. S. Chan, Claire H. Michel, D. Kronenberg-Versteeg, Y. Li, S.-P.Yang, Y. Wakutani, W. Meadows, R. R. Ferry, L. Dong, G. G. Tartaglia, G. Favrin, W.-L. Lin, D. W. Dickson, M. Zhen, D. Ron, G. Schmitt-Ulms, P. E. Fraser, N. A. Shneider, C. Holt, M. Vendruscolo, C. F. Kaminski and P. St George-Hyslop.
ALS/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function.
Neuron, 88, 678-690 (2015). [PDF]
E. V. Yates, T. Muller, L. Rajah, E. J. De Genst, P. Arosio, S. Linse, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles.
Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.
Nat. Chem. 7, 802-809 (2015). [PDF]
M. A. Wright, F. A. Aprile, P. Arosio, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
Chem. Comm. 51, 14425-14234 (2015). [PDF]
F. A. Aprile, P. Sormanni and M. Vendruscolo.
A rational design strategy for the selective activity enhancement of a molecular chaperone towards a target substrate.
Biochemistry, 54, 5103-5112 (2015). [PDF]
P. Sormanni, F. A. Aprile and M. Vendruscolo.
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins.
Proc. Natl. Acad. Sci. USA, 112, 9902-9907 (2015). [PDF]
R. Collepardo-Guevara, G. Portella, M. Vendruscolo, D. Frenkel, T. Schlick, M. Orozco.
Chromatin unfolding by epigenetic modifications explained by dramatic impairment of internucleosome interactions: a multiscale computational study.
J. Am. Chem. Soc. 137, 10205-10215 (2015). [PDF]
G. T. Heller, P. Sormanni and M. Vendruscolo.
Targeting disordered proteins with small molecules using entropy.
Trends Bioch. Sci. 40, 491-496 (2015). [PDF]
P. Kukic, A. Kannan, M. J. J. Dijkstra, S. Abeln, C. Camilloni and M. Vendruscolo.
Mapping the protein fold universe using the CamTube force field in molecular dynamics simulations.
PLoS Comp. Biol. 11, e1004435 (2015). [PDF]
Y. Pustovalova, P. Kukic, M. Vendruscolo and D. M. Korzhnev.
Probing the residual structure of the low populated denatured state of ADA2h under folding conditions by relaxation dispersion NMR spectroscopy.
Biochemistry, 54, 4611-4622 (2015). [PDF]
M. Pickhardt, T. Neumann, D. Schwizer, K. Callaway, M. Vendruscolo, D. Schenk, P. St George-Hyslop, E.-M. Mandelkow, C. M. Dobson, L. McConlogue, E. Mandelkow and G. Toth.
Identification of small molecule inhibitors of Tau aggregation by targeting monomeric Tau as a potential therapeutic approach for Tauopathies.
Curr. Alzheimer Res. 12, 814-828 (2015). [PDF]
D. Granata, F. Baftizadeh, J. Habchi, C. Galvagnion, A. De Simone, C. Camilloni, A. Laio and M. Vendruscolo.
The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments.
Sci. Rep. 5, 15449 (2015). [PDF]
C. Camilloni and M. Vendruscolo.
Reply to Comment on 'A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings'.
J. Phys. Chem. B, 119, 8225-8226 (2015). [PDF]
M. J. Holliday, C. Camilloni, G. Armstrong, N. G. Isern, F. Zhang, M. Vendruscolo and E. Eisenmesser.
Structure and dynamics of GeoCyp: A thermophilic cyclophilin with a novel substrate binding mechanism that functions efficiently at low temperatures.
Biochemistry, 54, 3207-3217 (2015). [PDF]
K. Brewer, T. Bacaj, A. Cavalli, C. Camilloni, N. Barlow, A. Zhou, P. Cao, J. Xu, A. B. Seven, E. A. Prinslow, R. Voleti, D. Haussinger, A. Bonvin, J. Liu, D. R. Tomchick, M. Vendruscolo, B. Graham, T. C. Sudhof, J. Rizo.
Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution
Nat. Struct. Mol. Biol. 22, 555-564 (2015). [PDF]
D. M. Walther, P. Kasturi, M. Zheng, S. Pinkert, G. Vecchi, P. Ciryam, R. I. Morimoto, C. M. Dobson, M. Vendruscolo, M. Mann and F.-U. Hartl.
Widespread proteome remodeling and aggregation in aging C. elegans.
Cell 161, 919-932 (2015). [PDF]
A. Cavalli and M. Vendruscolo.
Analysis of the performance of the CHESHIRE and YAPP methods at CASD-NMR round 3.
J. Biomol. NMR, 62, 503-509 (2015). [PDF]
T. P. J. Knowles, M. Vendruscolo and C. M. Dobson.
The physical basis of protein misfolding disorders.
Physics Today 68, 36-41 (2015). [PDF]
A. De Simone, F. A. Aprile, A. Dhulesia, C. M. Dobson and M. Vendruscolo.
Structure of a low-population intermediate state in the release of an enzyme product.
eLife 4, e02777 (2015). [PDF] [Podcast]
S. I. A. Cohen, P. Arosio, J. Presto, F. R. Kurudenkandy, H. Biverstal, L. Dolfe, C. Dunning, X. Yang, B. Frohm, M. Vendruscolo, J. Johansonn, C. M. Dobson, A. Fisahn, T. P. J. Knowles and S. Linse.
A molecular chaperone breaks the catalytic cycle that generates toxic Abeta oligomers.
Nat. Struct. Mol. Biol. 22, 207-213 (2015). [PDF] [N&V] [Press]
C. Galvagnion, A. K. Buell, G. Meisl, T. C. T. Michaels, M. Vendruscolo, T. P. J. Knowles and C. M. Dobson.
Lipid vesicles trigger alpha-synuclein aggregation by stimulating primary nucleation.
Nat. Chem. Biol. 11, 229-234 (2015). [PDF] [N&V] [Press]
P. Sormanni, C. Camilloni, P. Fariselli and M. Vendruscolo.
The s2D method: Simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins.
J. Mol. Biol. 427, 982-996 (2015). [PDF] [s2D web server]
P. Ciryam, R. Kundra, R. I. Morimoto, C. M. Dobson and M. Vendruscolo.
Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases.
Trends Pharmacol. Sci. 36, 72-77 (2015). [PDF]
R. Porcari, C. Proukakis, C. A. Waudby, B. Bolognesi, P. P. Mangione, J. F. S. Paton, S. Mullin, L. D. Cabrita, A. Penco, A. Relini, G. Verona, M. Vendruscolo, M. Stoppini, G. G. Tartaglia, C. Camilloni, J. Christodoulou, A. H. V. Schapira and V. Bellotti.
The H50Q mutation induces a tenfold decrease in the solubility of alpha-synuclein.
J. Biol. Chem. 290, 2395-2404 (2015). [PDF]
P. Kukic, H. T. K. Leung, F. Bemporad, F. A. Aprile, J. R. Kumita, A. De Simone, C. Camilloni, M. Vendruscolo.
The structure and dynamics of the integrin LFA-1 I-domain in the inactive state underlie its inside-out/outside-in signalling and allosteric mechanism.
Structure, 23, 745-753 (2015). [PDF]
S. Kumar, M. Vendruscolo, A. Singh, D. Kumar and A. Samal.
Analysis of the hierarchical structure of the B. subtilis transcriptional regulatory network.
Mol. BioSys. 11, 930-941 (2015). [PDF]
H. Takahashi, N. Adachi, T. Shirafuji, S. Danno, T. Ueyama, M. Vendruscolo, A. N. Shuvaev, T. Sugimoto, T. Seki, D. Hamada, K. Irie, H. Hirai, N. Sakai and N. Saito.
Identification and characterization of PKCgamma, a kinase implicated in SCA14, as an amyloidogenic protein.
Hum. Mol. Gen. 24, 525-539 (2015). [PDF]
P. Sormanni, F. A. Aprile and M. Vendruscolo.
The CamSol method of rational design of protein mutants with enhanced solubility.
J. Mol. Biol. 427, 478-490 (2015). [PDF] [CamSol web server (academic)] [CamSol web server (non-academic)]
C. Camilloni and M. Vendruscolo.
A tensor-free method for the structural and dynamical refinement of proteins using residual dipolar couplings.
J. Phys. Chem. B 19, 653-661 (2015). [PDF]

2014

D. Sanfelice, A. De Simone, A. Cavalli, S. Faggiano, M. Vendruscolo, A. Pastore.
Characterisation of the conformational fluctuations in the Josephin domain of ataxin-3.
Bioph. J. 107, 2923-2931 (2014). [PDF]
J. R. Allison, R. C. Rivers, J. C. Christodoulou, M. Vendruscolo and C. M. Dobson.
A relationship between the transient structure in the monomeric state and the aggregation propensities of alpha-synuclein and beta-synuclein.
Biochemistry, 53, 7170-7183 (2014). [PDF]
H. T. K. Leung, P. Kukic, C. Camilloni, F. Bemporad, A. De Simone, F. A. Aprile, J. Kumita and M. Vendruscolo.
NMR characterisation of the conformational fluctuations of the human lymphocyte function associated antigen-1 I domain.
Protein Sci. 23, 1596-1606 (2014) [PDF]
S. Gianni, C. Camilloni, R. Giri, A. Toto, D. Bonetti, A. Morrone, P. Sormanni, M. Brunori and M. Vendruscolo
Understanding the frustration arising from the competition between function, misfolding and aggregation in a globular protein.
Proc. Natl. Acad. Sci. USA 111, 14141-14146 (2014). [PDF]
W. Boomsma, P. Tian, J. Frellsen, J. Ferkinghoff-Borg, T. Hamelryck, K. Lindorff-Larsen and M. Vendruscolo.
Equilibrium simulations of proteins using molecular fragment replacement and NMR chemical shifts.
Proc. Natl. Acad. Sci. USA 111, 13852-13857 (2014). [PDF]
C. Camilloni, A. B. Sahakyan, M. Holliday, N. G. Isern, F. Zhang, E. Z. Eisenmesser and M. Vendruscolo.
Cyclophilin A catalyses proline isomerization by an electrostatic handle mechanism.
Proc. Natl. Acad. Sci. USA 111, 10203-10208 (2014). [PDF]
C. Camilloni and M. Vendruscolo.
Statistical mechanics of the denatured state of a protein using replica-averaged metadynamics.
J. Am. Chem. Soc. 136, 8982-8991 (2014). [PDF]
F. Blombach, H. Launay, A. P. Snijders, V. Zorraquino-Salvo, H. Wu, B. de Koning, S. J. Brouns, T. Ettema, C. Camilloni, A. Cavalli, M. Vendruscolo, M. J. Dickman, L. D. Cabrita, A. La Teana, D. Benelli, P. Londei, J. Christodoulou, J. van der Oost.
Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain.
Biochem. J. 462, 373-384 (2014). [PDF]
T. P. J. Knowles, M. Vendruscolo and C. M. Dobson.
The amyloid state and its association with protein misfolding diseases.
Nat. Rev. Mol. Cell Biol. 15, 384-396 (2014). [PDF]
P. Ciryam, M. Vendruscolo, C. M. Dobson and E. P. O'Brien.
Understanding the influence of codon translation rates on cotranslational protein folding.
Acc. Chem. Res. 47, 1536-1544 (2014). [PDF]
A. K. Buell, C. Galvagnion, R. Gaspar, E. Sparr, M. Vendruscolo, T. P. J. Knowles, S. Linse and C. M. Dobson.
Solution conditions determine the relative importance of nucleation and growth processes in alpha-synuclein aggregation.
Proc. Natl. Acad. Sci. USA, 111, 7671-7676 (2014). [PDF]
G. Fusco, A. De Simone, G. Tata, V. Vostrikov, M. Vendruscolo, C. M. Dobson, G. Veglia.
Direct observation of the three regions in alpha-synuclein that determine its membrane-bound behaviour.
Nat. Comm. 5, 3827 (2014). [PDF]
B. Fu, A. B. Sahakyan, C. Camilloni, G. G. Tartaglia, E. Paci, A. Caflisch, M. Vendruscolo and A. Cavalli.
ALMOST: An all atom molecular simulation toolkit for protein structure determination.
J. Comp. Chem. 35, 1101-1105 (2014). [PDF]
P. Kukic, C. Camilloni, A. Cavalli and M. Vendruscolo.
Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
J. Mol. Biol. 426, 1826-1838 (2014). [PDF]
A. A. Kendrick, M. J. Holliday, N. G. Isern, F. Zhang, C. Camilloni, C. Huynh, M. Vendruscolo, G. Armstrong and E. Z. Eisenmesser.
The dynamics of interleukin-8 and its interaction with human CXC receptor I peptide.
Protein Sci. 23, 464-480 (2014). [PDF]
R. W. Montalvao, C. Camilloni, A. De Simone and M. Vendruscolo.
New opportunities for tensor-free calculations of residual dipolar couplings for the study of protein dynamics.
J. Biolmol. NMR, 58, 233-238 (2014). [PDF]
A. Kannan, C. Camilloni, A. B. Sahakyan, A. Cavalli and M. Vendruscolo.
A conformational ensemble derived using NMR methyl chemical shifts reveals a mechanical clamping transition that gates the binding of the HU protein to DNA.
J. Am. Chem. Soc. 136, 2204-2207 (2014). [PDF]
P. Arosio, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Chemical kinetics for drug discovery against protein aggregation.
Trends Pharmacol. Sci. 35, 127-135 (2014). [PDF]
S. I. A. Cohen, L. Rajah, C. Yoon, A. K. Buell, D. A. White, R. A. Sperling, M. Vendruscolo, E. M. Terentjev, C. M. Dobson, D. A. Weitz and T. P. J. Knowles.
Spatial propagation of protein polymerisation.
Phys. Rev. Lett. 112, 098101 (2014). [PDF]
G. Toth, S. Gardai, W. Zago, C. W. Bertoncini, N. Cremades, S. L. Roy, M. A. Tambe, J.-C. Rochet, C. Galvaignon, G. Skibinski, S. Finkbeiner, M. Bova, K. Regnstrom, S. Chiou, J. Johnston, K. Callaway, J. P. Anderson, M. F. Jobling, A. K. Buell, T. A. Yednock, T. P. J. Knowles, M. Vendruscolo, J. Christodoulou, C. M. Dobson, D. Schenk, L. McConlogue.
Targeting the intrinsically disordered structural ensemble of alpha-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease.
PLoS One, 9, e87133 (2014). [PDF]
E. P. O'Brien, M. Vendruscolo and C. M. Dobson.
Kinetic modeling indicates fast translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates.
Nat. Comm. 5, 2988 (2014). [PDF]
S. Abeln, M. Vendruscolo, C. M. Dobson, D. Frenkel.
A simple lattice model that captures protein folding, aggregation and amyloid formation.
PLoS One, 9, e85185 (2014). [PDF]
M. Varadi, S. Kosol, P. Lebrun, E. Valentini, M. Blackledge, A. K. Dunker, I. C. Felli, J. D. Forman-Kay, R. W. Kriwacki, J. Sussman, D. I. Svergun, V. N. Uversky, M. Vendruscolo, D. Wishart, P. E. Wright, P. Tompa.
pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins.
Nucl. Acids Res. 42, D326-D335 (2014). [PDF]

2013

G. T. Debelouchina, M. J. Bayro, A. W. Fitzpatrick, V. Ladizhansky, M. T. Colvin, M. A. Caporini, C. P. Jaroniec, V. S. Bajaj, M. Rosay, C. E. MacPhee, M. Vendruscolo, W. E. Maas, C. M. Dobson, R. G. Griffin.
Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.
J. Am. Chem. Soc. 135, 19237-19247 (2013). [PDF]
L. Volpatti, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
A clear view of polymorphism, twist and chirality in amyloid fibril formation.
ACS Nano, 7, 10443-10448 (2013). [PDF]
C. Camilloni, A. Cavalli and M. Vendruscolo.
Replica-averaged metadynamics.
J. Chem. Theor. Comput. 9, 5610-5617 (2013). [PDF]
P. Ciryam, G. G. Tartaglia, R. I. Morimoto, C. M. Dobson and M. Vendruscolo.
Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins.
Cell Rep. 5, 781-790 (2013). [PDF]
F. Biedermann, M. Vendruscolo, O. A. Scherman, A. De Simone, W. M. Nau.
Cucurbit[8]uril and blue-box: High-energy water release overwhelms electrostatic interactions.
J. Am. Chem. Soc. 135, 14879-14888 (2013). [PDF]
A. De Simone, M. Gustavsson, R. W. Montalvao, L. Shi, G. Veglia and M. Vendruscolo.
Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.
Biochemistry, 52, 6684-6694 (2013). [PDF]
A. De Simone, R. W. Montalvao, C. M. Dobson and M. Vendruscolo.
Characterisation of the interdomain motions in hen lysozyme using residual dipolar couplings as replica-averaged structural restraints in molecular dynamics simulations.
Biochemistry, 52, 6480-6486 (2013). [PDF]
C. Camilloni and M. Vendruscolo.
A relationship between the aggregation rates of alpha-synuclein variants and the beta-sheet populations in their monomeric forms.
J. Phys. Chem. B, 117, 10737-10741 (2013). [PDF]
M. Tsytlonok, P. Sormanni, P. J. E. Rowling, M. Vendruscolo and L. S. Itzhaki.
Subdomain architecture and stability of a giant repeat protein.
J. Phys. Chem. B, 117, 13029-13037 (2013). [PDF]
C. A. Waudby, C. Camilloni, A. W. P. Fitzpatrick, L. Cabrita, C. M. Dobson, M. Vendruscolo and J. Christodoulou.
In-cell NMR characterization of the secondary structure populations of a disordered conformation of alpha-synuclein within E. coli cells.
PLoS One, 8, e72286 (2013). [PDF]
M. H. Horrocks, L. Rajah, P. Jonsson, M. Kjaergaard, M. Vendruscolo, T. P. J. Knowles and D. Klenerman.
Single-molecule measurements of transient biomolecular complexes through microfluidic dilution.
Anal. Chem. 85, 6855-6859 (2013). [PDF]
R. Suardiaz, A. B. Sahakyan and M. Vendruscolo.
A geometrical parametrisation of C1'- C5' RNA ribose chemical shifts calculated by density functional theory.
J. Chem. Phys. 139, 034101 (2013). [PDF]
M. Zhu, A. De Simone, D. Schenk, G. Toth, C. M. Dobson and M. Vendruscolo.
Identification of small-molecule binding pockets in the soluble monomeric form of the Abeta42 peptide.
J. Chem. Phys. 139, 035101 (2013). [PDF]
A. Borkar, A. De Simone, R. W. Montalvao and M. Vendruscolo.
A method of determining RNA conformational ensembles using structure-based calculations of residual dipolar couplings.
J. Chem. Phys. 138, 215103 (2013). [PDF]
T. W. Herling, T. M. Muller, L. Rajah, J. N. Skepper, M. Vendruscolo, and T. P. J. Knowles.
Integration and characterization of solid wall electrodes in microfluidic devices fabricated in a single photolithography step.
App. Phys. Lett. 102, 184102 (2013). [PDF]
S. I. A. Cohen, S. Linse, L. M. Luheshi, E. Hellstrand, D. A. White, L. Rajah, D. E. Otzen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Proliferation of amyloid-beta42 aggregates occurs through a secondary nucleation mechanism.
Proc. Natl. Acad. Sci. USA, 110, 9758-9763 (2013). [PDF]
L. Caniparoli, M. Marsili and M. Vendruscolo.
The Codon Information Index: A quantitative measure of the information provided by the codon bias.
J. Stat. Mech. P04031 (2013). [PDF]
D. Granata, C. Camilloni, M. Vendruscolo and A. Laio.
Characterization of the free energy landscapes of proteins by NMR-guided metadynamics.
Proc. Natl. Acad. Sci. USA, 110, 6817-6822 (2013). [PDF]
A. W. P. Fitzpatrick, G. T. Debelouchina, M. J. Bayro, D. K. Clare, M. A. Caporini, V. S. Bajaj, C. P. Jaroniec, L. Wang, V. Ladizhansky, S. A. Muller, C. E. MacPhee, C. A. Waudby, H. R. Mott, A. De Simone, T. P. J. Knowles, H. R. Saibil, M. Vendruscolo, E. Orlova, R. G. Griffin and C. M. Dobson.
Atomic structure and hierarchical self-assembly of a cross-beta amyloid fibril.
Proc. Natl. Acad. Sci. USA, 110, 5468-5473 (2013). [PDF]
T. Guilliams, F. El-Turk, A. K. Buell, E. M. O'Day, F. A. Aprile, E. K. Esbjorner, M. Vendruscolo, N. Cremades, E. Pardon, W. Lode, M. E. Welland, J. Steyaert, J. Christodoulou, C. M. Dobson and E. De Genst.
Nanobodies raised against monomeric alpha-synuclein distinguish between fibrils at different maturation stages.
J. Mol. Biol. 425, 2397-2411 (2013). [PDF]
M. Vendruscolo and C. M. Dobson
Protein self-assembly intermediates.
Nat. Chem. Biol. 9, 216-217 (2013). [PDF]
A. Cavalli, C. Camilloni and M. Vendruscolo.
Molecular dynamics simulations with replica-averaged structural restraints generate structural ensembles according to the maximum entropy principle.
J. Chem. Phys. 138, 094112 (2013) [PDF]
A. B. Sahakyan and M. Vendruscolo.
Analysis of ring current and electric field effects on the chemical shifts of RNA bases.
J. Phys. Chem. B, 117, 1989-1998 (2013). [PDF]
C. Camilloni, A. Cavalli and M. Vendruscolo.
Assessment of the use chemical shifts as replica-averaged structural restraints in molecular dynamics simulations to characterise the dynamics of proteins.
J. Phys. Chem. B, 117, 1838-1843 (2013). [PDF]
P. Ciryam, R. I. Morimoto, M. Vendruscolo, C. M. Dobson and E. P. O'Brien.
In vivo translation rates can substantially delay the co-translational folding of the Escherichia coli cytosolic proteome.
Proc. Natl. Acad. Sci. USA, 110, E132-E140 (2013). [PDF]

2012

C. Roodveldt, A. Andersson, E. J. De Genst, A. Labrador-Garrido, A. K. Buell, C. M. Dobson, G. G. Tartaglia and M. Vendruscolo.
A rationally-designed six-residue swap generates comparability in the aggregation behaviour of alpha-synuclein and beta-synuclein.
Biochemistry, 51, 8771-8778 (2012). [PDF]
T. P. Knowles, A. De Simone, A. W. Fitzpatrick, A. Baldwin, S. Meehan, L. Rajah, M. Vendruscolo, M. E. Welland, C. M. Dobson, E. M. Terentjev.
Twisting transition between crystalline and fibrillar phases of aggregated peptides.
Phys. Rev. Lett. 109, 158101 (2012). [PDF]
R. W. Montalvao, A. De Simone and M. Vendruscolo.
Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.
J. Biomol. NMR, 53, 281-292 (2012). [PDF]
J. E. Chambers, K. Petrova, G. Tomba, M. Vendruscolo and D. Ron.
ADP ribosylation adapts an endoplasmic reticulum chaperone response to short-term fluctuations in unfolded protein load.
J. Cell Biol. 198, 371-385 (2012). [PDF]
E. P. O'Brien, M. Vendruscolo and C. M. Dobson.
Prediction of variable translation rate effects on cotranslational protein folding.
Nat. Comm. 3, 868 (2012). [PDF]
A. B. Sahakyan, A. Cavalli, W. F. Vranken and M. Vendruscolo.
Protein structure validation using side-chain chemical shifts.
J. Phys. Chem. B, 116, 4754-4759 (2012). [PDF]
E. P. O'Brien, J. Christodoulou, M. Vendruscolo and C. M. Dobson.
Trigger factor slows co-translational folding through kinetic trapping while sterically protecting the nascent chain from aberrant cytosolic interactions.
J. Am. Chem. Soc. 134, 10920-10932 (2012). [PDF]
J. Chen, H. Yagi, P. Sormanni, M. Vendruscolo, K. Makabe, T. Nakamura, Y. Goto, K. Kuwajima.
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone.
FEBS Lett. 586, 1120-1127 (2012). [PDF]
C. Camilloni, A. De Simone, W. F. Vranken and M. Vendruscolo.
Determination of secondary structure populations in disordered states of proteins using NMR chemical shifts.
Biochemistry, 51, 2224-2231 (2012). [PDF] [d2D web server]
S. I. A. Cohen, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles.
From macroscopic measurements to microscopic mechanisms of protein aggregation.
J. Mol. Biol. 421, 160-171 (2012). [PDF]
P. Neudecker, P. Robustelli, A. Cavalli, P. Walsh, P. Lundstrom, A. Zarrine-Afsar, S. Sharpe, M. Vendruscolo, L. E. Kay.
Structure of an intermediate state in protein folding and aggregation.
Science, 336, 362-366 (2012). [PDF]
C. Camilloni, P. Robustelli, A. De Simone, A. Cavalli and M. Vendruscolo.
Characterisation of the conformational equilibrium between the two major substates of RNase A using NMR chemical shifts.
J. Am. Chem. Soc. 134, 3968-3971 (2012). [PDF]
H. T. A. Leung, B. Ochoa Montano, T. L. Blundell, M. Vendruscolo and R. W. Montalvao.
Arabesque: A tool for protein structural comparison using differential geometry and knot theory.
Wor. Res. J. Pep. Prot. 1, 33-40 (2012). [PDF]
M. Vendruscolo.
Proteome folding and aggregation.
Curr. Op. Struct. Biol. 22, 138-143 (2012). [PDF]
F. Agostini, M. Vendruscolo, G. G. Tartaglia.
Sequence-based prediction of protein solubility.
J. Mol. Biol. 421, 237-241 (2012). [PDF]
G. Fusco, A. De Simone, S.-T. D. Hsu, F. Bemporad, M. Vendruscolo, F. Chiti, C. M. Dobson.
1H, 13C and 15N resonance assignments of human muscle acylphosphatase.
Biomol. NMR. Assign. 6, 27-29 (2012). [PDF]
A. Rosato, J. Aramini, C. Arrowsmith, A. Bagaria, D. Baker, A. Cavalli, J. F. Doreleijers, A. Eletsky, A. Giachetti, P. Guerry, A. Gutmanas, P. Guntert, Y.-F. He, T. Herrmann, Y. J. Huang, V. Jaravine, H. R.A. Jonker, M. A. Kennedy, O. F. Lange, G. Liu, T. E. Malliavin, R. Mani, B. Mao, G. T. Montelione, M. Nilges, P. Rossi, G. van der Schot, H. Schwalbe, T. Szyperski, M. Vendruscolo, R. Vernon, W. F. Vranken, S. de Vries, G. W. Vuister, B. Wu, Y. Yang and A. M.J.J. Bonvin.
Blind testing of routine, fully automated determination of protein structures from NMR data.
Structure, 20, 227-236 (2012). [PDF]
T. Murakami, S.-P. Yang, L. Xie, T. Kawano, D. Fu, A. Mukai, C. Bohm, F. Chen, J. Robertson, H. Suzuki, G. G. Tartaglia, M. Vendruscolo, G. S. Schierle, F. T. Chan, A. Moloney, D. C. Crowther, C. F. Kaminski, M. Zhen and P. St George-Hyslop.
ALS mutations in FUS causes neuronal dysfunction and death in C. elegans by a dominant gain-of-function mechanism.
Hum. Mol. Gen. 21, 1-9 (2012). [PDF]

2011

A. De Simone, A. Dhulesia, G. Soldi, M. Vendruscolo, S.-T. D. Hsu, F. Chiti and C. M. Dobson.
Experimental energy surfaces reveal the mechanisms of maintenance of protein solubility
Proc. Natl. Acad. Sci. USA, 108, 21057-21062 (2011). [PDF]
M. Vendruscolo, T. P. J. Knowles and C. M. Dobson.
Protein solubility and protein homeostasis: A generic view of protein misfolding disorders.
Cold Spring Harb Perspect. Biol. 3, a010454 (2011). [PDF]
K. Wolff, M. Vendruscolo and M. Porto.
A coarse-grained model for protein folding based on structural profiles.
Phys. Rev. E, 84, 041934 (2011). [PDF]
A. De Simone, R. W. Montalvao and M. Vendruscolo.
Determination of dynamic equilibria in proteins using residual dipolar couplings.
J. Chem. Theor. Comp. 7, 4189-4195 (2011). [PDF]
S. I. A. Cohen, M. Vendruscolo, C. M. Dobson, T. P. J. Knowles.
Nucleated polymerisation in the presence of pre-formed seed filaments.
Int. J. Mol. Sci. 12, 5844-5852 (2011). [PDF]
M. Vendruscolo.
Excited-state control of protein activity.
J. Mol. Biol. 412, 153-154 (2011). [PDF]
A. W. Fitzpatrick, T. P. J. Knowles, C. A. Waudby, M. Vendruscolo and C. M. Dobson.
Inversion of the balance of hydrophobicity and hydrogen bonding between protein folding and aggregation.
PLoS Comp. Biol. 7, e1002169 (2011). [PDF]
L. Kang, K.-P. Wu, M. Vendruscolo and J. Baum.
The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse alpha-synuclein.
J. Am. Chem. Soc. 133, 13465-13470 (2011). [PDF]
A. B. Sahakyan, W. F. Vranken, A. Cavalli and M. Vendruscolo.
Using side-chain aromatic proton chemical shifts for a quantitative analysis of protein structures.
Angew. Chem. Intl. Ed. 50, 9620-9623 (2011). [PDF] [ArShift web server]
S. I. A. Cohen, M. Vendruscolo, M. E. Welland, C. M. Dobson, E. M. Terentjev and T. P. J. Knowles.
Nucleated polymerization with secondary pathways I. Time evolution of the principal moments.
J. Chem. Phys. 135, 065105 (2011). [PDF]
S. I. A. Cohen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Nucleated polymerization with secondary pathways II. Determination of self-consistent solutions to growth processes described by non-linear master equations.
J. Chem. Phys. 135, 065106 (2011). [PDF]
S. I. A. Cohen, M. Vendruscolo, C. M. Dobson and T. P. J. Knowles.
Nucleated polymerization with secondary pathways III. Equilibrium behavior, filament length distribution and oligomer populations.
J. Chem. Phys. 135, 065107 (2011). [PDF]
A. J. Baldwin, T. P. J. Knowles, G. G. Tartaglia, A. W. Fitzpatrick, G. L. Devlin, S. Shammas, C. A. Waudby, M. F. Mossuto, S. Meehan, S. L. Gras, J. Christodoulou, S. J. Anthony-Cahill, P. D. Barker, M. Vendruscolo, C. M. Dobson.
Metastability of native proteins and the phenomenon of amyloid formation.
J. Am. Chem. Soc. 133, 14160-14163 (2011). [PDF]
A. Cavalli, R. W. Montalvao and M. Vendruscolo.
Using chemical shifts to determine structural changes in proteins upon complex formation.
J. Phys. Chem. B, 115, 9491-9494 (2011). [PDF]
M. Vendruscolo.
Protein regulation: The statitical theory of allostery.
Nat. Chem. Biol. 7, 411-412 (2011). [PDF]
A. B. Sahakyan, W. F. Vranken, A. Cavalli and M. Vendruscolo.
Structure-based prediction of methyl chemical shifts in proteins.
J. Biomol. NMR, 50, 331-346 (2011). [PDF] [CH3Shift web server]
K. Wolff, M. Vendruscolo and M. Porto.
Asymmetric folding pathways and transient misfolding in a coarse-grained model of proteins.
Europhys. Lett. 94, 48005 (2011). [PDF]
T. R. Jahn, K. J. Kohlhoff, M. Scott, G. G. Tartaglia, D. A. Lomas, C. M. Dobson, M. Vendruscolo and D. C. Crowther.
Detection of early locomotor abnormalities in a Drosophila model of Alzheimer's disease by a three-dimensional tracking system.
J. Neurosci. Meth. 197, 186-189 (2011). [PDF]
K. J. Kohlhoff, T. R. Jahn, D. A. Lomas, C. M. Dobsom, C. D. Crowther and M. Vendruscolo.
The iFly tracking system for an automated locomotor and behavioural analysis of Drosophila melanogaster.
Integrative Biology, 3, 755-760 (2011). [PDF]
S. Raimondi, F. Guglielmi, S. Giorgetti, S. Di Gaetano, A. Arciello, D. M. Monti, A. Relini, D. Nichino, S. M. Doglia, A. Natalello, P. Pucci, P. Mangione, L. Obici, G. Merlini, M. Stoppini, P. Robustelli, G. G. Tartaglia, M. Vendruscolo, C. M. Dobson, R. Piccoli, V. Bellotti.
Effects of the known pathogenic mutations on the aggregation pathways of the amyloidogenic peptide of human apolipoprotein A-I.
J. Mol. Biol. 407, 465-476 (2011). [PDF]
E. O'Brien, J. Christodoulou, M. Vendruscolo, C. M. Dobson.
New scenarios of protein folding can occur on the ribosome.
J. Am. Chem. Soc. 132, 16928-16937 (2011). [PDF]
O. Szczepankiewicz, C. Cabaleiro-Lago, G. G. Tartaglia, M. Vendruscolo, T. Hunter, G. J. Hunter, H. Nilsson, E. Thulin and S. Linse.
Interactions in the native state of monellin, which play a protective role against aggregation.
Mol. BioSys. 7, 521-532 (2011). [PDF]
L. Masino, G. Nicastro, L. Calder, M. Vendruscolo and A. Pastore.
Functional interactions as a survival strategy against abnormal aggregation.
FEBS J. 25, 45-54 (2011). [PDF]
M. Vendruscolo and C. M. Dobson.
Protein dynamics: Moore's law in molecular biology.
Current Biology, 21, R68-R70 (2011). [PDF]
H. Olzscha, S. M. Schermann, A. C. Worner, S. Pinkert, M. H. Hecht, G. G. Tartaglia, M. Vendruscolo, M. Hayer-Hartl, F. U. Hartl and R. M. Vabulas.
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions.
Cell, 144, 67-78 (2011). [PDF]

2010

S. Gianni, Y. Ivarsson, A. De Simone, C. Travaglini-Allocatelli, M. Brunori and M. Vendruscolo.
Characterization of the structure of a misfolded intermediate populated during the folding process of a PDZ domain.
Nat. Struct. Mol. Biol. 17, 1431-1437 (2010). [PDF]
M. Vendruscolo.
Enzymatic activity in disordered states of proteins.
Curr. Op. Chem. Biol. 14, 671-675 (2010). [PDF]
E. P. O'Brien, S. -T. D Hsu, J. Christodoulou, M. Vendruscolo, and C. M. Dobson.
Transient tertiary structure formation within the ribosome exit port.
J. Am. Chem. Soc. 132, 16928-16937 (2010). [PDF]
M. A. Caporini, V. S. Bajaj, M. Veshtort, A. Fitzpatrick, C. E. MacPhee, M. Vendruscolo, C. M. Dobson, and R. G. Griffin.
Accurate determination of interstrand distances and alignment in amyloid fibrils by magic angle spinning NMR.
J. Phys. Chem. B, 114, 13555-13561 (2010). [PDF]
S. Pechmann and M. Vendruscolo.
Derivation of a solubility condition for proteins from an analysis of the competition between folding and aggregation.
Mol. BioSys. 6, 2490-2497 (2010). [PDF]
G. G. Tartaglia and M. Vendruscolo.
Proteome-level relationship between folding and aggregation propensities of proteins.
J. Mol. Biol. 402, 919-928 (2010). [PDF]
Y. Lee, T. Zhou, G. G. Tartaglia, M. Vendruscolo and C. O. Wilke.
Translationally optimal codons associate with aggregation-prone sites in proteins.
Proteomics, 10, 4163-4171 (2010). [PDF]
P. Robustelli, K. J. Kohlhoff, A. Cavalli and M. Vendruscolo.
Using NMR chemical shifts as structural restraints in molecular dynamics simulations of proteins.
Structure, 18, 923-933 (2010). [PDF]
G. G. Tartaglia, C. M. Dobson, F. U. Hartl and M. Vendruscolo.
Physico-chemical determinants of chaperone requirements.
J. Mol. Biol. 400, 579-588 (2010). [PDF]
I. De Gortari, G. Portella, X. Salvatella, V. S. Bajaj, P. van der Wel, J. R. Yates, M. D. Segall, C. J. Pickard, M. C. Payne and M. Vendruscolo.
Time averaging of NMR chemical shifts in the MLF peptide in the solid state.
J. Am. Chem. Soc. 132, 5993-6000, 2010. [PDF]
A.-C. Brorsson, B. Bolognesi, G. G. Tartaglia, S. L. Shammas, G. Favrin, I. Watson, D. A. Lomas, F. Chiti, M. Vendruscolo, C. M. Dobson, D. C. Crowther and L. M. Luheshi.
Intrinsic determinants of neurotoxic aggregate formation by the amyloid beta peptide.
Bioph. J. 98, 1677-1684, 2010. [PDF]
K. Wolff, M. Vendruscolo and M. Porto.
Efficient identification of near-native conformations in ab initio protein structure prediction using structural profiles.
Proteins, 78, 249-258 (2010). [PDF]