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: Sarita Puri, Iren Wang, Carlo Camilloni, Cristina Paissoni, Shang-Te Danny Hsu, Szu-Yu Chen

المصدر: Biophys J

مصطلحات موضوعية: Physics, 0303 health sciences, Protein Folding, biology, Protein Conformation, Biophysics, Methanocaldococcus jannaschii, Proteins, Articles, biology.organism_classification, Reaction coordinate, Folding (chemistry), 03 medical and health sciences, Kinetics, 0302 clinical medicine, Chemical physics, Helix, Methanocaldococcus, Thermodynamics, Protein folding, Threading (protein sequence), Protein secondary structure, 030217 neurology & neurosurgery, 030304 developmental biology, Knot (mathematics)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60546f82ced38df97e6f337d53e57a46
https://pubmed.ncbi.nlm.nih.gov/33812848

المؤلفون: Andrea Bernardini, Carlo Camilloni, Andrea Saponaro, Marco Nardini, Michela Lapi, Valentina Nardone, Diletta Dolfini, Sebastiano Pasqualato, Nerina Gnesutta, Cristina Airoldi, Antonio Chaves-Sanjuan, Roberto Mantovani

المساهمون: Nardone, V, Chaves-Sanjuan, A, Lapi, M, Airoldi, C, Saponaro, A, Pasqualato, S, Dolfini, D, Camilloni, C, Bernardini, A, Gnesutta, N, Mantovani, R, Nardini, M

المصدر: Cells
Volume 9
Issue 11
Cells, Vol 9, Iss 2370, p 2370 (2020)
'Cells ', vol: 9, pages: 2370-1-2370-21 (2020)

مصطلحات موضوعية: histone fold, Magnetic Resonance Spectroscopy, Suramin, CAAT box, Molecular Dynamics Simulation, CCAAT box, Biophysical Phenomena, Article, Structure-Activity Relationship, medicine, Humans, Amino Acid Sequence, Transcription factor, lcsh:QH301-705.5, transcription factor, suramin, Chemistry, Rational design, Isothermal titration calorimetry, Promoter, General Medicine, DNA, inhibition, Cell biology, lcsh:Biology (General), CCAAT-Binding Factor, Docking (molecular), Histone fold, Protein Multimerization, NF-Y, medicine.drug, Transcription Factors

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f4a5fb3638c456480778a438e5723dc
https://pubmed.ncbi.nlm.nih.gov/33138093

المؤلفون: Elin, Karlsson, Cristina, Paissoni, Amanda M, Erkelens, Zeinab A, Tehranizadeh, Frieda A, Sorgenfrei, Eva, Andersson, Weihua, Ye, Carlo, Camilloni, Per, Jemth

المصدر: The Journal of Biological Chemistry

مصطلحات موضوعية: Protein Conformation, alpha-Helical, Protein Folding, coupled binding and folding, Static Electricity, IDP, protein binding, Molecular Dynamics Simulation, Evolution, Molecular, Nuclear Receptor Coactivator 3, Protein Domains, Animals, Humans, Amino Acid Sequence, protein evolution, Phylogeny, pre-steady-state kinetics, phi value analysis, protein complex, transition state, CREB-Binding Protein, Recombinant Proteins, Protein Structure, Tertiary, Intrinsically Disordered Proteins, Kinetics, Protein Structure and Folding, Mutagenesis, Site-Directed, Hydrophobic and Hydrophilic Interactions, Sequence Alignment

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid________::013a44288db4dba52420dcee6a102365
https://pubmed.ncbi.nlm.nih.gov/33454008

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: Kai Kohlhoff, Thomas Löhr, Carlo Camilloni, Gabriella T. Heller, Michele Vendruscolo

مصطلحات موضوعية: Physics, Quantitative Biology::Biomolecules, Markov chain, Artificial neural network, Computer Networks and Communications, Stochastic process, Aβ peptide, Probabilistic logic, Markov model, Kinetic energy, Computer Science Applications, Microsecond, Molecular dynamics, Computer Science (miscellaneous), Human proteome project, Statistical physics

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18ff5f09a23d447bcc4a0dba778656a6
https://doi.org/10.1101/2020.05.07.082818

المؤلفون: Carlo Camilloni, Benedetta Maria Sala, Antonino Natalello, T. Le Marchand, G. Pintacuda, Stefano Ricagno

مصطلحات موضوعية: Molecular dynamics, Materials science, Chemical physics, Chemical shift, Native state, Crystal structure, Fourier transform infrared spectroscopy, Spectroscopy, Protein secondary structure, Macromolecule

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a9db7cb274ed54e28d97947dc3f0864

المؤلفون: Michael Sattler, Sara Marie Øie Solbak, Ralf Stehle, Anders Bach, Ana C. Messias, Arie Geerlof, Carlo Camilloni, Alexander Jussupow

مصطلحات موضوعية: 0303 health sciences, 010304 chemical physics, Characteristic length, Context (language use), Observable, 01 natural sciences, 03 medical and health sciences, Ubiquitins, Molecular recognition, Structural biology, 0103 physical sciences, Molecule, Biological system, Conformational ensembles, 030304 developmental biology

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2fa307af2d765e9499aa09eb9242daeb
https://doi.org/10.1101/2020.04.14.041327

المؤلفون: Frieda A. Sorgenfrei, Cristina Paissoni, Amanda M. Erkelens, Per Jemth, Carlo Camilloni, Elin Karlsson, Zeinab Amiri Tehranizadeh, Weihua Ye, Eva Andersson

مصطلحات موضوعية: Folding (chemistry), Transition (genetics), Chemistry, Mechanism (biology), Biophysics, Contact formation

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b13d5a70549539e904dc751a5bf2726

المؤلفون: 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

المساهمون: Heller, Gabriella T [0000-0002-5672-0467], Aprile, Francesco A [0000-0002-5040-4420], Perni, Michele [0000-0001-7593-8376], Ruggeri, Francesco Simone [0000-0002-1232-1907], Mannini, Benedetta [0000-0001-6812-7348], Löhr, Thomas [0000-0003-2969-810X], Bonomi, Massimiliano [0000-0002-7321-0004], Camilloni, Carlo [0000-0002-9923-8590], De Simone, Alfonso [0000-0001-8789-9546], Felli, Isabella C [0000-0002-6018-9090], Pierattelli, Roberta [0000-0001-7755-0885], Knowles, Tuomas PJ [0000-0002-7879-0140], Dobson, Christopher M [0000-0002-5445-680X], Vendruscolo, Michele [0000-0002-3616-1610], Apollo - University of Cambridge Repository, Heller, G. T., Aprile, F. A., Michaels, T. C. T., Limbocker, R., Perni, M., Ruggeri, F. S., Mannini, B., Lohr, T., Bonomi, M., Camilloni, C., de Simone, A., Felli, I. C., Pierattelli, R., Knowles, T. P. J., Dobson, C. M., Vendruscolo, M., University of Cambridge [UK] (CAM), Imperial College London, Harvard University, Bioinformatique structurale - Structural Bioinformatics, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano = University of Milan (UNIMI), University of Naples Federico II = Università degli studi di Napoli Federico II, Università degli Studi di Firenze = University of Florence (UniFI), Funding: G.T.H. is supported by the Gates Cambridge Trust and the Rosalind Franklin Research Fellowship at Newnham College, Cambridge, F.A.A. is supported by UK Research and Innovation (Future Leaders Fellowship MR/S033947/1) and the Alzheimer’s Society, UK (317, 511), R.L. is supported by the Gates Cambridge Trust, TCTM by Peterhouse, Cambridge and the Swiss National Science Foundation, and F.S.R. is supported by Darwin College and the Swiss National Foundation (grant numbers P300P2_171219 and P2ELP2_162116, respectively). We acknowledge ARCHER UK National Supercomputing Service under ARCHER Leadership project (grant number e510) and PRACE for awarding us access to MareNostrum at Barcelona Supercomputing Center (BSC), Spain for metadynamic metainference simulations. Parameterization of 10074-G5 was performed using resources provided by the Cambridge Service for Data Driven Discovery (CSD3) operated by the University of Cambridge Research Computing Service (www.csd3.cam.ac.uk), provided by Dell EMC and Intel using Tier-2 funding from the Engineering and Physical Sciences Research Council (capital grant EP/P020259/1), and DiRAC funding from the Science and Technology Facilities Council (www.dirac.ac.uk). MALDI mass spectrometry measurements were performed by L. Packman at the Protein and Nucleic Acid Chemistry Facility (PNAC) at the Department of Biochemistry, University of Cambridge. The NMR measurements were supported by the iNEXT H2020 Programme (EC contract no. 653706). OW450 C. elegans were donated by E. Nollen. BLI measurements were performed in the Biophysics facility at the Department of Biochemistry, University of Cambridge. The work was also supported by the Centre for Misfolding Diseases and the INCEPTION project ANR-16-CONV-0005., ANR-16-CONV-0005,INCEPTION,Institut Convergences pour l'étude de l'Emergence des Pathologies au Travers des Individus et des populatiONs(2016), Harvard University [Cambridge], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Milano [Milano] (UNIMI), University of Naples Federico II, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI)

المصدر: 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)

مصطلحات موضوعية: Amyloid beta, In silico, Biophysics, Intrinsically disordered proteins, 03 medical and health sciences, 0302 clinical medicine, Alzheimer Disease, Drug Discovery, medicine, Humans, Life Science, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, Research Articles, 030304 developmental biology, 0303 health sciences, Multidisciplinary, Amyloid beta-Peptides, biology, Drug discovery, Chemistry, SciAdv r-articles, Conformational entropy, Small molecule, Peptide Fragments, 3. Good health, Mechanism of action, biology.protein, Small molecule binding, medicine.symptom, Hydrophobic and Hydrophilic Interactions, 030217 neurology & neurosurgery, Research Article

وصف الملف: text/html; application/pdf; application/octet-stream

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