Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Tadeo E. Saldaño"'
Autor:
Alexander Miguel Monzon, Diego Javier Zea, María Silvina Fornasari, Tadeo E Saldaño, Sebastian Fernandez-Alberti, Silvio C E Tosatto, Gustavo Parisi
Publikováno v:
PLoS Computational Biology, Vol 13, Iss 2, p e1005398 (2017)
Protein motions are a key feature to understand biological function. Recently, a large-scale analysis of protein conformational diversity showed a positively skewed distribution with a peak at 0.5 Å C-alpha root-mean-square-deviation (RMSD). To unde
Externí odkaz:
https://doaj.org/article/53bc9cf9c23447c4a5a7d78b8fc09bcf
Autor:
Giuseppe Zanotti, Francesca Vallese, Alberto Ferrari, Ilaria Menozzi, Tadeo E Saldaño, Paola Berto, Sebastian Fernandez-Alberti, Rodolfo Berni
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0187716 (2017)
The molecular symmetry of multimeric proteins is generally determined by using X-ray diffraction techniques, so that the basic question as to whether this symmetry is perfectly preserved for the same protein in solution remains open. In this work, hu
Externí odkaz:
https://doaj.org/article/3f9ac5d9b8c4459e972eaa58fb122ed9
Publikováno v:
PLoS ONE, Vol 12, Iss 7, p e0181019 (2017)
Native transthyretin (TTR) homotetramer dissociation is the first step of the fibrils formation process in amyloid disease. A large number of specific point mutations that destabilize TTR quaternary structure have shown pro-amyloidogenic effects. Bes
Externí odkaz:
https://doaj.org/article/d2f3519581ec4c3e85272999f0addc31
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 3, p e1004775 (2016)
Conformational diversity of the native state plays a central role in modulating protein function. The selection paradigm sustains that different ligands shift the conformational equilibrium through their binding to highest-affinity conformers. Intram
Externí odkaz:
https://doaj.org/article/619536de96874296b51cdf8eb970b9bb
Publikováno v:
Journal of computational chemistryREFERENCES. 43(6)
Dynamics of protein cavities associated with protein fluctuations and conformational plasticity is essential for their biological function. NMR ensembles, Molecular Dynamics (MD) simulations combined with Principal Component Analysis (PCA), and Norma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45acf1e8854fd8f37e873e4aef256bfd
https://pubmed.ncbi.nlm.nih.gov/34962296
https://pubmed.ncbi.nlm.nih.gov/34962296
Autor:
María Silvina Fornasari, Nahuel Escobedo, Agustina García Melani, Sebastian Fernandez Alberti, Tomás Peters, Gustavo Parisi, Nicolás Demitroff, Ana Julia Velez Rueda, Juan Mac Donagh, Eduardo Gonik, Nicolas Palopoli, Diego Javier Zea, Julieta Novomisky Nechcoff, Tadeo E. Saldaño, Julia Marchetti, Martín N. Salas
Publikováno v:
Bioinformatics (Oxford, England).
Motivation After the outstanding breakthrough of AlphaFold in predicting protein 3D models, new questions appeared and remain unanswered. The ensemble nature of proteins, for example, challenges the structural prediction methods because the models sh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e0b3b82b7d01354361bccb8a5eeb2ce
https://pubmed.ncbi.nlm.nih.gov/35380621
https://pubmed.ncbi.nlm.nih.gov/35380621
Autor:
Kiersten M. Ruff, Tamas Lazar, Claudiu C. Gradinaru, María Silvina Fornasari, Silvio C. E. Tosatto, Javier Iserte, Marie Skepö, Julia Marchetti, Sonia Longhi, Teresa Head-Gordon, Toby J. Gibson, Nicolás A. Méndez, Gregory-Neal W. Gomes, Malene Ringkjøbing Jensen, Nicolás A. Garrone, Pau Bernadó, Martin Blackledge, Alexander Miguel Monzon, Dmitri I. Svergun, András Hatos, Julie D. Forman-Kay, Cristina Marino-Buslje, Edward A. Lemke, Eric Fagerberg, Ana Julia Velez Rueda, Sylvain D. Vallet, Elizabeth Martínez-Pérez, Sylvie Ricard-Blum, Tiago N. Cordeiro, Federica Quaglia, Tadeo E. Saldaño, Damiano Piovesan, Peter Tompa, Tanja Mittag, Gustavo Parisi, Mihaly Varadi, Rohit V. Pappu, Lucía B. Chemes, Giovanni Minervini, Edoardo Salladini
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic acids research, vol 49, iss D1
Nucleic Acids Research, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic acids research, vol 49, iss D1
Nucleic Acids Research, 2021, 49 (D1), pp.D404-D411. ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, Oxford University Press, In press, ⟨10.1093/nar/gkaa1021⟩
Nucleic Acids Research, In press, ⟨10.1093/nar/gkaa1021⟩
The Protein Ensemble Database (PED) (https://proteinensemble.org), which holds structural ensembles of intrinsically disordered proteins (IDPs), has been significantly updated and upgraded since its last release in 2016. The new version, PED 4.0, has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d62579a66daeda9d1cb3ef52f41885bf
https://hal.univ-grenoble-alpes.fr/hal-03433964/document
https://hal.univ-grenoble-alpes.fr/hal-03433964/document
Publikováno v:
Nucleic Acids Research
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=r3c4b2081b22::d62579a66daeda9d1cb3ef52f41885bf
Autor:
Sebastian Fernandez-Alberti, Silvio C. E. Tosatto, Victor M. Freixas, Gustavo Parisi, Tadeo E. Saldaño
Proteins in their native states can be represented as ensembles of conformers in dynamical equilibrium. Thermal fluctuations are responsible for transitions between these conformers. Normal-modes analysis (NMA) using elastic network models (ENMs) pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec9000e7fb11cda1c10733a2e9d7ab90
http://hdl.handle.net/11577/3352751
http://hdl.handle.net/11577/3352751
Publikováno v:
European biophysics journal : EBJ. 48(6)
According to the generalized conformational selection model, ligand binding involves the co-existence of at least two conformers with different ligand-affinities in a dynamical equilibrium. Conformational transitions between them should be guaranteed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60cf008ee181d5c8a636e7c9c9dfcc9a
https://pubmed.ncbi.nlm.nih.gov/31273390
https://pubmed.ncbi.nlm.nih.gov/31273390