المؤلفون: Maria-Evangelia Karyadi, Julian M. Schmidt-Engler, Carlo Camilloni, Sammy H. S. Chan, Anaïs M. E. Cassaignau, Michele Vendruscolo, Lisa D. Cabrita, Anne S. Wentink, Christopher A. Waudby, John Christodoulou, Tomasz Wlodarski

المصدر: Proceedings of the National Academy of Sciences of the United States of America

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Protein Folding, Magnetic Resonance Spectroscopy, Filamins, Isomerase, Filamin, Ribosome, Domain (software engineering), 03 medical and health sciences, chemistry.chemical_compound, Biosynthesis, Protein biosynthesis, Humans, protein misfolding, Proteostasis Deficiencies, Multidisciplinary, molecular dynamics simulations, Biological Sciences, Folding (chemistry), Biophysics and Computational Biology, nuclear magnetic resonance, Kinetics, 030104 developmental biology, chemistry, Tandem Repeat Sequences, tandem repeat protein, Biophysics, Thermodynamics, cotranslational folding, Protein folding, Ribosomes, Protein Modification, Translational

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f78ba1add2d83a3e2d60f4afc439352e
https://doi.org/10.1073/pnas.1716252115

المؤلفون: Guido Tiana, Carlo Camilloni, Michele Vendruscolo, Andrea Possenti

المساهمون: Tiana, Guido [0000-0001-9868-1809], Apollo - University of Cambridge Repository

المصدر: Proteins: Structure, Function, and Bioinformatics. 86:956-964

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Protein Folding, Protein Conformation, Computer science, Computational biology, Information theory, Intrinsically disordered proteins, information content, Biochemistry, 03 medical and health sciences, Protein structure, Protein sequencing, Structural Biology, Amino Acid Sequence, Molecular Biology, Peptide sequence, Sequence (medicine), designed proteins, 030102 biochemistry & molecular biology, protein folding/function, Computational Biology, Proteins, Biomolecules (q-bio.BM), Genetic code, structure prediction, 030104 developmental biology, Quantitative Biology - Biomolecules, FOS: Biological sciences, Thermodynamics, Protein folding, intrinsically disordered proteins

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5219086cbc8a0086c8a08542b2eeffa
https://doi.org/10.1002/prot.25527

المؤلفون: Alessandra Pesce, Marco Orlando, Stefania Brocca, Marina Lotti, Sandra Pucciarelli, Marco Nardini, Michela Lapi, Alberto Barbiroli, Carlo Camilloni, Marco Mangiagalli, Serena Maione

المساهمون: Mangiagalli, M, Lapi, M, Maione, S, Orlando, M, Brocca, S, Pesce, A, Barbiroli, A, Camilloni, C, Pucciarelli, S, Lotti, M, Nardini, M

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, Protein Conformation, alpha-Helical, cooperativity, Gene Expression, Crystallography, X-Ray, Biochemistry, Substrate Specificity, 0302 clinical medicine, psychrophilic enzyme, Enzyme Stability, glycoside hydrolase, Cloning, Molecular, Psychrophile, Marinomonas, Phylogeny, chemistry.chemical_classification, computer.file_format, Recombinant Proteins, Cold Temperature, enzyme kinetic, 030220 oncology & carcinogenesis, Thermodynamics, Mesophile, Protein Binding, Genetic Vectors, Antarctic Regions, 03 medical and health sciences, Bacterial Proteins, Escherichia coli, Protein Interaction Domains and Motifs, Amino Acid Sequence, Thermolabile, Protein Structure, Quaternary, Molecular Biology, Binding Sites, Sequence Homology, Amino Acid, Thermophile, Substrate (chemistry), Galactose, Cell Biology, Protein Data Bank, beta-Galactosidase, Protein Structure, Tertiary, Kinetics, 030104 developmental biology, Enzyme, chemistry, cold adaptation, Biophysics, Protein quaternary structure, Protein Conformation, beta-Strand, Protein Multimerization, computer, Sequence Alignment

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::377881be43c22122ddeaef1692e1af46
http://hdl.handle.net/10281/276684

المؤلفون: 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

المساهمون: The Royal Society, Département de Biologie structurale et Chimie - Department of Structural Biology and Chemistry, Institut Pasteur [Paris] (IP), Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Scuola Internazionale Superiore di Studi Avanzati / International School for Advanced Studies (SISSA / ISAS), Università degli Studi di Milano = University of Milan (UNIMI), Queen's University [Belfast] (QUB), Centre de Biochimie Structurale [Montpellier] (CBS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Institut de recherche pour le développement [IRD] : UR206-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Unité de Catalyse et Chimie du Solide - UMR 8181 (UCCS), Université d'Artois (UA)-Centrale Lille-Institut de Chimie du CNRS (INC)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre Blaise Pascal (CBP), École normale supérieure de Lyon (ENS de Lyon), University of Rochester [USA], 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. M., 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., Institut Pasteur [Paris], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano [Milano] (UNIMI), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Centrale Lille Institut (CLIL)-Université d'Artois (UA)-Centrale Lille-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Lille, École normale supérieure - Lyon (ENS Lyon), Simulation of Biomolecular Systems (HIMS, FNWI), Molecular Simulations (HIMS, FNWI), Massimiliano Bonomi, Giovanni Bussi, Carlo Camilloni, Gareth A. Tribello, Pavel Banáš, 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, Vojtěch Spiwok, Jiří Šponer, David W. H. Swenson, Pratyush Tiwary, Omar Valsson, Michele Vendruscolo, Gregory A. Voth & Andrew White

المصدر: 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

مصطلحات موضوعية: Models, Molecular, DYNAMICS, enhanced-sampling, free-energy calculations, molecular dynamics simulations, transparency, reproducibility, dissemination, Biochemistry & Molecular Biology, Computer science, Molecular Conformation, Molecular Dynamics Simulation, Biochemistry, Biochemical Research Methods, Settore FIS/03 - Fisica della Materia, 03 medical and health sciences, 10 Technology, Humans, ddc:610, reproducibility, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 11 Medical and Health Sciences, 030304 developmental biology, 0303 health sciences, Reproducibility, Science & Technology, PLUMED consortium, Reproducibility of Results, Cell Biology, 06 Biological Sciences, simulation, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Transparency (graphic), Systems engineering, Life Sciences & Biomedicine, Software, Biotechnology, Developmental Biology

وصف الملف: application/pdf; ELETTRONICO

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3927d802200cff3bcbe25d3464ffedbf
http://hdl.handle.net/20.500.11767/100676

المؤلفون: Thomas, Löhr, Carlo, Camilloni, Massimiliano, Bonomi, Michele, Vendruscolo

المصدر: Methods in molecular biology (Clifton, N.J.). 2022

مصطلحات موضوعية: Models, Molecular, Protein Conformation, Bayes Theorem, Molecular Dynamics Simulation, Peptides, Nuclear Magnetic Resonance, Biomolecular, Algorithms

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::e86134f4ec1476acba932110a78e9422
https://pubmed.ncbi.nlm.nih.gov/31396909

المؤلفون: Michele Vendruscolo, Carlo Camilloni, Samuel Reghim Silva, Rinaldo W. Montalvao, Antonio Marinho da Silva Neto

المصدر: Proteins: Structure, Function, and Bioinformatics.

مصطلحات موضوعية: Models, Molecular, Protein Conformation, Curvature, Biochemistry, Proto-Oncogene Proteins c-myb, 03 medical and health sciences, Superposition principle, Software, Structural Biology, Animals, Cluster Analysis, Humans, Statistical physics, Cluster analysis, Molecular Biology, Conformational ensembles, 030304 developmental biology, Mathematics, Principal Component Analysis, 0303 health sciences, Ubiquitin, business.industry, 030302 biochemistry & molecular biology, Proteins, Metric space, Differential geometry, Torsion (algebra), business

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa36007fd0ba04e8c19622eed0509917
https://doi.org/10.1002/prot.25652

المؤلفون: Eva Schad, Silvio C. E. Tosatto, Alexander Miguel Monzon, Zsuzsanna Dosztányi, Ivan Mičetić, Damiano Piovesan, Pietro Sormanni, Lisanna Paladin, Francesco Tabaro, Bálint Mészáros, Gustavo Parisi, Michele Vendruscolo, Carlo Camilloni, Peter Tompa, Marco Necci, Wim F. Vranken, Norman E. Davey

المساهمون: Lääketieteen ja biotieteiden tiedekunta - Faculty of Medicine and Life Sciences, University of Tampere, Structural Biology Brussels, Department of Bio-engineering Sciences, Informatics and Applied Informatics, Chemistry, Basic (bio-) Medical Sciences

المصدر: Nucleic acids research, 46 (D1
Nucleic Acids Research
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Protein Folding, DATABASE, Protein Data Bank (RCSB PDB), Datasets as Topic, Information layer, Roentgen rays, Computational biology, Biology, Indirect evidence, Biokemia, solu- ja molekyylibiologia - Biochemistry, cell and molecular biology, purl.org/becyt/ford/1 [https], 03 medical and health sciences, Annotation, Journal Article, Genetics, Database Issue, Humans, Protein Interaction Domains and Motifs, Amino Acid Sequence, Databases, Protein, Protein secondary structure, Search function, Internet, Binding Sites, PROTEIN DISORDER, Molecular Sequence Annotation, purl.org/becyt/ford/1.2 [https], Intrinsically Disordered Proteins, Gene Ontology, 030104 developmental biology, Ciencias de la Computación e Información, INTRINSIC DISORDER, UniProt, Sequence Alignment, Biologie, Ciencias de la Información y Bioinformática, Software, CIENCIAS NATURALES Y EXACTAS, Protein Binding

وصف الملف: application/pdf; fulltext; D471-D476; 1 full-text file(s): application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a173b8e499eafa1f22f66340d235ae
https://academic.oup.com/nar/article/46/D1/D471/4612964

المؤلفون: Johannes Buchner, Manuel Hora, Carlo Camilloni, Pamina Kazman, Christoph Göbl, Bernd Reif, Benedikt Weber

المصدر: J. Mol. Biol. 430, 4925-4940 (2018)

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Amyloid, Protein Conformation, Proteolysis, Arginine, Immunoglobulin light chain, Fibril, Antibody Folding, Protein Stability, Light Chain Linker, Intramolecular Interactions, Protein Aggregation, Pathological, 03 medical and health sciences, Residue (chemistry), Amyloid disease, Protein Domains, Structural Biology, medicine, Humans, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Binding Sites, 030102 biochemistry & molecular biology, medicine.diagnostic_test, Chemistry, 030104 developmental biology, Residual dipolar coupling, Mutation, Biophysics, Immunoglobulin Light Chains, Linker

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8a266856d366d146ff587a41c6b5124
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=54713

المؤلفون: Carlo Camilloni, Massimiliano Bonomi

المساهمون: Università degli Studi di Milano [Milano] (UNIMI)

المصدر: Bioinformatics
Bioinformatics, Oxford University Press (OUP), 2017, 33 (24), pp.3999-4000. ⟨10.1093/bioinformatics/btx529⟩

مصطلحات موضوعية: 0301 basic medicine, Statistics and Probability, Models, Molecular, Molecular Conformation, Computational biology, 010402 general chemistry, 01 natural sciences, Biochemistry, 03 medical and health sciences, Molecular Biology, ComputingMilieux_MISCELLANEOUS, Structure (mathematical logic), Supplementary data, Experimental data, Bayes Theorem, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], ISDB, 0104 chemical sciences, Computer Science Applications, Variety (cybernetics), Computational Mathematics, 030104 developmental biology, Computational Theory and Mathematics, A priori and a posteriori, Bayesian framework, Noise (video), Biological system, Software

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2e2a883e7a9581e7d4e4a57b950cd47
https://hal.archives-ouvertes.fr/hal-03136441

المؤلفون: Carlo Camilloni, Gabriella T. Heller, Michele Vendruscolo, Massimiliano Bonomi

المساهمون: University of Cambridge [UK] (CAM), Università degli Studi di Milano [Milano] (UNIMI), Bonomi, Massimilano [0000-0002-7321-0004], Heller, Gabrielle [0000-0002-5672-0467], Vendruscolo, Michele [0000-0002-3616-1610], Apollo - University of Cambridge Repository

المصدر: Current Opinion in Structural Biology
Current Opinion in Structural Biology, Elsevier, 2017, 42, pp.106-116. ⟨10.1016/j.sbi.2016.12.004⟩

مصطلحات موضوعية: 0301 basic medicine, Models, Molecular, 010304 chemical physics, Protein molecules, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Entropy, Proteins, Nanotechnology, Computational biology, 01 natural sciences, [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM], Visualization, 03 medical and health sciences, 030104 developmental biology, Protein structure, Structural Biology, 0103 physical sciences, Human proteome project, Humans, Molecular Biology

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce3cf4626f44535e13d0061e1fe2badb
https://hal.archives-ouvertes.fr/hal-03136490