Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Guillaume Pagès"'
Autor:
Guillaume Pagès
Publikováno v:
Revue de Primatologie, Vol 6 (2016)
Les nourritures dites « de recul » ou « de rabat » (fallback foods), utilisées pendant les périodes de pénurie des aliments « préférés » comme les fruits, sont la plupart du temps perçues comme étant nutritionnellement pauvres, alors qu
Externí odkaz:
https://doaj.org/article/4f5b2c2ef47942adaedda2eb29601af1
Publikováno v:
Journal of Experimental Botany
Journal of Experimental Botany, 2020, 71 (12), pp.3524-3534. ⟨10.1093/jxb/eraa122⟩
Journal of Experimental Botany, Oxford University Press (OUP), 2020, 71 (12), pp.3524-3534. ⟨10.1093/jxb/eraa122⟩
Journal of Experimental Botany, 2020, 71 (12), pp.3524-3534. ⟨10.1093/jxb/eraa122⟩
Journal of Experimental Botany, Oxford University Press (OUP), 2020, 71 (12), pp.3524-3534. ⟨10.1093/jxb/eraa122⟩
We present a simple and generic model, based on mechanistic hypotheses, to represent the longitudinal variations of the diameter of individual roots and the associated diversity of growth patterns.
In a given root system, individual roots usuall
In a given root system, individual roots usuall
Autor:
Guillaume, Pagès, Sergei, Grudinin
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2165
Symmetry is very common among proteins found in structural databases such as the Protein Data Bank (PDB). We present novel software, called AnAnaS, that finds positions and orientations of the symmetry axes in all types of symmetrical protein assembl
Autor:
Guillaume Pagès, Sergei Grudinin
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2018, 203 (3), pp.185-194. ⟨10.1016/j.jsb.2018.05.005⟩
Journal of Structural Biology, 2018, 203 (3), pp.185-194. ⟨10.1016/j.jsb.2018.05.005⟩
Journal of Structural Biology, Elsevier, 2018, 203 (3), pp.185-194. ⟨10.1016/j.jsb.2018.05.005⟩
Journal of Structural Biology, 2018, 203 (3), pp.185-194. ⟨10.1016/j.jsb.2018.05.005⟩
International audience; Protein assemblies are often symmetric, as this organization has many advantages compared to individual proteins. Complex protein structures thus very often possess high-order symmetries. Detection and analysis of these symmet
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2018, 203 (2), pp.142-148. ⟨10.1016/j.jsb.2018.04.004⟩
Journal of Structural Biology, 2018, 203 (2), pp.142-148. ⟨10.1016/j.jsb.2018.04.004⟩
Journal of Structural Biology, Elsevier, 2018, 203 (2), pp.142-148. ⟨10.1016/j.jsb.2018.04.004⟩
Journal of Structural Biology, 2018, 203 (2), pp.142-148. ⟨10.1016/j.jsb.2018.04.004⟩
International audience; Symmetry in protein, and, more generally, in macromolecular assemblies is a key point to understand their structure, stability and function. Many symmetrical assemblies are currently present in the Protein Data Bank (PDB) and
Autor:
Sergei Grudinin, Guillaume Pagès
Publikováno v:
Methods in Molecular Biology ISBN: 9781071607077
Protein Structure Prediction. Methods in Molecular Biology
Protein Structure Prediction. Methods in Molecular Biology, pp.245-257, 2020, ⟨10.1007/978-1-0716-0708-4_14⟩
Protein Structure Prediction. Methods in Molecular Biology
Protein Structure Prediction. Methods in Molecular Biology, pp.245-257, 2020, ⟨10.1007/978-1-0716-0708-4_14⟩
International audience; Symmetry is very common among proteins found in structural databases such as the PDB. We present novel software, called AnAnaS, that finds positions and orientations of the symmetry axes in all types of symmetrical protein ass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ecb666436da2063922d9ff31faa64b
https://doi.org/10.1007/978-1-0716-0708-4_14
https://doi.org/10.1007/978-1-0716-0708-4_14
Autor:
Sergei Grudinin, Guillaume Pagès
Publikováno v:
Bioinformatics
Bioinformatics, 2019, 35 (24), pp.5113-5120. ⟨10.1093/bioinformatics/btz454⟩
Bioinformatics, Oxford University Press (OUP), 2019, 35 (24), pp.5113-5120. ⟨10.1093/bioinformatics/btz454⟩
Bioinformatics, 2019, 35 (24), pp.5113-5120. ⟨10.1093/bioinformatics/btz454⟩
Bioinformatics, Oxford University Press (OUP), 2019, 35 (24), pp.5113-5120. ⟨10.1093/bioinformatics/btz454⟩
Motivation Thanks to the recent advances in structural biology, nowadays 3D structures of various proteins are solved on a routine basis. A large portion of these structures contain structural repetitions or internal symmetries. To understand the evo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32a1e154110f05e43b3305f4f4ba57bb
https://inria.hal.science/hal-01903624
https://inria.hal.science/hal-01903624
Autor:
Bohdan Monastyrskyy, Juri Rappsilber, Krzysztof Fidelis, J. Eduardo Fajardo, Mikhail Karasikov, Alexander Leitner, Agnieszka S. Karczyńska, Andras Fiser, Adam Belsom, Silvia Crivelli, Emilia A. Lubecka, Celina Sikorska, Andriy Kryshtafovych, Nelson Gil, Cezary Czaplewski, Rojan Shrestha, Esben Trabjerg, Sergei Grudinin, Guillaume Pagès, Adam Liwo, Adam K. Sieradzan
Publikováno v:
Proteins-Structure, Function and Bioinformatics
Proteins-Structure, Function and Bioinformatics, Wiley, 2019, Critical Assessment of Methods of Protein Structure Prediction (CASP) Special Issue, 87 (12), pp.1283-1297. ⟨10.1002/prot.25816⟩
Proteins
Proteins-Structure, Function and Bioinformatics, 2019, Critical Assessment of Methods of Protein Structure Prediction (CASP) Special Issue, 87 (12), pp.1283-1297. ⟨10.1002/prot.25816⟩
Fajardo, J E, Shrestha, R, Gil, N, Belsom, A, Crivelli, S N, Czaplewski, C, Fidelis, K, Grudinin, S, Karasikov, M, Karczyńska, A S, Kryshtafovych, A, Leitner, A, Liwo, A, Lubecka, E A, Monastyrskyy, B, Pagès, G, Rappsilber, J, Sieradzan, A K, Sikorska, C, Trabjerg, E & Fiser, A 2019, ' Assessment of chemical-crosslink-assisted protein structure modeling in CASP13 ', Proteins: Structure, Function, and Bioinformatics, vol. 87, no. 12, pp. 1283-1297 . https://doi.org/10.1002/prot.25816
Proteins-Structure, Function and Bioinformatics, Wiley, 2019, Critical Assessment of Methods of Protein Structure Prediction (CASP) Special Issue, 87 (12), pp.1283-1297. ⟨10.1002/prot.25816⟩
Proteins
Proteins-Structure, Function and Bioinformatics, 2019, Critical Assessment of Methods of Protein Structure Prediction (CASP) Special Issue, 87 (12), pp.1283-1297. ⟨10.1002/prot.25816⟩
Fajardo, J E, Shrestha, R, Gil, N, Belsom, A, Crivelli, S N, Czaplewski, C, Fidelis, K, Grudinin, S, Karasikov, M, Karczyńska, A S, Kryshtafovych, A, Leitner, A, Liwo, A, Lubecka, E A, Monastyrskyy, B, Pagès, G, Rappsilber, J, Sieradzan, A K, Sikorska, C, Trabjerg, E & Fiser, A 2019, ' Assessment of chemical-crosslink-assisted protein structure modeling in CASP13 ', Proteins: Structure, Function, and Bioinformatics, vol. 87, no. 12, pp. 1283-1297 . https://doi.org/10.1002/prot.25816
International audience; With the advance of experimental procedures obtaining chemical crosslinking information is becoming a fast and routine practice. Information on crosslinks can greatly enhance the accuracy of protein structure modeling. Here, w
Publikováno v:
Bioinformatics
Bioinformatics, Oxford University Press (OUP), 2019, 35 (18), pp.3313-3319. ⟨10.1093/bioinformatics/btz122⟩
Bioinformatics, 2019, 35 (18), pp.3313-3319. ⟨10.1093/bioinformatics/btz122⟩
Bioinformatics, Oxford University Press (OUP), 2019, 35 (18), pp.3313-3319. ⟨10.1093/bioinformatics/btz122⟩
Bioinformatics, 2019, 35 (18), pp.3313-3319. ⟨10.1093/bioinformatics/btz122⟩
Motivation Protein model quality assessment (QA) is a crucial and yet open problem in structural bioinformatics. The current best methods for single-model QA typically combine results from different approaches, each based on different input features
Publikováno v:
Bioinformatics
Bioinformatics, Oxford University Press (OUP), 2019, 35 (16), pp.2801-2808. ⟨10.1093/bioinformatics/bty1037⟩
Bioinformatics, 2019, 35 (16), pp.2801-2808. ⟨10.1093/bioinformatics/bty1037⟩
Bioinformatics, Oxford University Press (OUP), 2019, 35 (16), pp.2801-2808. ⟨10.1093/bioinformatics/bty1037⟩
Bioinformatics, 2019, 35 (16), pp.2801-2808. ⟨10.1093/bioinformatics/bty1037⟩
Motivation Protein quality assessment (QA) is a crucial element of protein structure prediction, a fundamental and yet open problem in structural bioinformatics. QA aims at ranking predicted protein models to select the best candidates. The assessmen