Small-molecule binding to an intrinsically disordered protein revealed by experimental NMR19F transverse spin-relaxation

Autor: Gabriella T. Heller, Vaibhav Kumar Shukla, Angelo M. Figueiredo, D. Flemming Hansen

Intrinsically disordered proteins are highly dynamic biomolecules that rapidly interconvert between many structural conformations. Traditionally, these proteins have been considered un-druggable because of their lack of classical long-lived binding p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1982aea8fb432acf2290e8736ee6eb74
https://doi.org/10.1101/2023.05.03.539297

Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors

Autor: Paolo Arosio, Sara Linse, Gabriella T. Heller, Andela Saric, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles, Thomas C. T. Michaels, Samo Curk, Georg Meisl

Publikováno v: Proc Natl Acad Sci U S A

Understanding the mechanism of action of compounds capable of inhibiting amyloid-fibril formation is critical to the development of potential therapeutics against protein-misfolding diseases. A fundamental challenge for progress is the range of possi

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https://doi.org/10.1073/pnas.2006684117

Promoting transparency and reproducibility in enhanced molecular simulations

Autor: B. Pavel, L. Vittorio, C. Michele, F. Marta, W. Andrew, G. Federico, V. Michele, Š. Jiří, Davide Provasi, M. Layla, K. Evgeny, S. Matteo, V. Omar, Riccardo Capelli, M. Carla, David W.H. Swenson, Kim E. Jelfs, G. Piero, D. Davide, M. Angelos, P. Jim, Gareth A. Tribello, M. Fabrizio, C. Francesco, P. Michele, E. Bernd, Cristina Paissoni, M. Matteo, F. Haohao, L. Kresten, P. Pablo, T. Pratyush, L. Alessandro, Marco De La Pierre, B. Mattia, J. Alexander, M. Tetsuya, B. Sandro, Andrew L. Ferguson, Gabriella T. Heller, Francesco Luigi Gervasio, B. Davide, R. Paolo, D. Viktor, Massimiliano Bonomi, I. Michele, Peter G. Bolhuis, P. GiovanniMaria, Carlo Camilloni, C. Andrea, P. Elena, S. Vojtěch, James S. Fraser, L. Thomas, C. Haochuan, C. Paolo, N. Marco, B. Alessandro, P. Fabio, B. Giovanni, I. Marcella, G. Alejandro, C. Wei, Glen M. Hocky, G. Toni, P. Adriana, Gabriele C. Sosso, Q. David, P. Silvio, Gregory A. Voth, M. Ralf, R. Stefano, D. Sandip, R. Jakub

Publikováno v: Nature Methods
Nature Methods, 2019, 16 (8), pp.670-673. ⟨10.1038/s41592-019-0506-8⟩
The PLUMED consortium 2019, ' Promoting transparency and reproducibility in enhanced molecular simulations ', Nature Methods, vol. 16, no. 8, pp. 670-673 . https://doi.org/10.1038/s41592-019-0506-8
Nature methods 16(8), 670-673 (2019). doi:10.1038/s41592-019-0506-8
Nature Methods, Nature Publishing Group, 2019, 16 (8), pp.670-673. ⟨10.1038/s41592-019-0506-8⟩
Bonomi, M, Bussi, G, Camilloni, C, Tribello, G A, Banas, P, Barducci, A, Bernetti, M, Bolhuis, P G, Bottaro, S, Branduardi, D, Capelli, R, Carloni, P, Ceriotti, M, Cesari, A, Chen, H, Chen, W, Colizzi, F, De, S, De La Pierre, M, Donadio, D, Drobot, V, Ensing, B, Ferguson, A L, Filizola, M, Fraser, J S, Fu, H, Gasparotto, P, Gervasio, F L, Giberti, F, Gil-Ley, A, Giorgino, T, Heller, G T, Hocky, G M, Iannuzzi, M, Invernizzi, M, Jelfs, K E, Jussupow, A, Kirilin, E, Laio, A, Limongelli, V, Lindorff-Larsen, K, Lohr, T, Marinelli, F, Martin-Samos, L, Masetti, M, Meyer, R, Michaelides, A, Molteni, C, Morishita, T, Nava, M, Paissoni, C, Papaleo, E, Parrinello, M, Pfaendtner, J, Piaggi, P, Piccini, G, Pietropaolo, A, Pietrucci, F, Pipolo, S, Provasi, D, Quigley, D, Raiteri, P, Raniolo, S, Rydzewski, J, Salvalaglio, M, Sosso, G C, Spiwok, V, Sponer, J, Swenson, D W H, Tiwary, P, Valsson, O, Vendruscolo, M, Voth, G A & White, A 2019, ' Promoting transparency and reproducibility in enhanced molecular simulations ', Nature Methods, vol. 16, no. 8, pp. 670-673 . https://doi.org/10.1038/s41592-019-0506-8
Nature Methods, 16(8), 670-673. Nature Publishing Group
Nature methods (Online) 16 (2019): 670. doi:10.1038/s41592-019-0506-8
info:cnr-pdr/source/autori:Massimiliano Bonomi, Giovanni Bussi, Carlo Camilloni, Gareth A. Tribello, Pavel Baná?, Alessandro Barducci, Mattia Bernetti, Peter G. Bolhuis, Sandro Bottaro, Davide Branduardi, Riccardo Capelli, Paolo Carloni, Michele Ceriotti, Andrea Cesari, Haochuan Chen, Wei Chen, Francesco Colizzi, Sandip De, Marco De La Pierre, Davide Donadio, Viktor Drobot, Bernd Ensing, Andrew L. Ferguson, Marta Filizola, James S. Fraser, Haohao Fu, Piero Gasparotto, Francesco Luigi Gervasio, Federico Giberti, Alejandro Gil-Ley, Toni Giorgino, Gabriella T. Heller, Glen M. Hocky, Marcella Iannuzzi, Michele Invernizzi, Kim E. Jelfs, Alexander Jussupow, Evgeny Kirilin, Alessandro Laio, Vittorio Limongelli, Kresten Lindorff-Larsen, Thomas Löhr, Fabrizio Marinelli, Layla Martin-Samos, Matteo Masetti, Ralf Meyer, Angelos Michaelides, Carla Molteni, Tetsuya Morishita, Marco Nava, Cristina Paissoni, Elena Papaleo, Michele Parrinello, Jim Pfaendtner, Pablo Piaggi, GiovanniMaria Piccini, Adriana Pietropaolo, Fabio Pietrucci, Silvio Pipolo, Davide Provasi, David Quigley, Paolo Raiteri, Stefano Raniolo, Jakub Rydzewski, Matteo Salvalaglio, Gabriele Cesare Sosso, Vojt?ch Spiwok, Ji?í ?poner, David W. H. Swenson, Pratyush Tiwary, Omar Valsson, Michele Vendruscolo, Gregory A. Voth, Andrew White/titolo:Promoting transparency and reproducibility in enhanced molecular simulations/doi:10.1038%2Fs41592-019-0506-8/rivista:Nature methods (Online)/anno:2019/pagina_da:670/pagina_a:/intervallo_pagine:670/volume:16

The PLUMED consortium unifies developers and contributors to PLUMED, an open-source library for enhanced-sampling, free-energy calculations and the analysis of molecular dynamics simulations. Here, we outline our efforts to promote transparency and r

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http://hdl.handle.net/20.500.11767/100676

Rational design of a conformation-specific antibody for the quantification of Aβ oligomers

Autor: Ryan Limbocker, Tom Scheidt, Francesco A. Aprile, Michele Vendruscolo, Patricia C. Salinas, Pietro Sormanni, Michele Perni, Tuomas P. J. Knowles, Johnny Habchi, Christopher M. Dobson, Tomas Sneideris, Shianne Chhangur, Gabriella T. Heller, Francesco Simone Ruggeri, Steven F. Lee, Marina Podpolny, Lisa-Maria Needham, Benedetta Mannini

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, 117(24), 13509-13518
Proceedings of the National Academy of Sciences of the United States of America 117 (2020) 24

Significance The accurate quantification of the amounts of small oligomeric assemblies formed by the amyloid β (Aβ) peptide represents a major challenge in the Alzheimer’s field. There is therefore great interest in the development of methods to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec4f5eeca510afd76ac631c5b0205b5e
https://pubmed.ncbi.nlm.nih.gov/32493749

Small-molecule sequestration of amyloid-β as a drug discovery strategy for Alzheimer's disease

Autor: Benedetta Mannini, Roberta Pierattelli, Thomas Löhr, Massimiliano Bonomi, Carlo Camilloni, Thomas C. T. Michaels, Francesco Simone Ruggeri, Gabriella T. Heller, Alfonso De Simone, Michele Vendruscolo, Francesco A. Aprile, Christopher M. Dobson, Ryan Limbocker, Michele Perni, Isabella C. Felli, Tuomas P. J. Knowles

Publikováno v: Science Advances 6 (2020) 45
Science Advances
Science Advances, 2020, 6 (45), pp.eabb5924. ⟨10.1126/sciadv.abb5924⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2020, 6 (45), pp.eabb5924. ⟨10.1126/sciadv.abb5924⟩
Science Advances, 6(45)

A small molecule binds to a disordered protein in its monomeric form, preventing its aggregation linked to Alzheimer’s disease.
Disordered proteins are challenging therapeutic targets, and no drug is currently in clinical use that modifies the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b3641cfe696a5f6d6e115e314da75d9