Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Francois Stricher"'
Autor:
Ignacio E Sánchez, Pedro Beltrao, Francois Stricher, Joost Schymkowitz, Jesper Ferkinghoff-Borg, Frederic Rousseau, Luis Serrano
Publikováno v:
PLoS Computational Biology, Vol 4, Iss 4, p e1000052 (2008)
Current experiments likely cover only a fraction of all protein-protein interactions. Here, we developed a method to predict SH2-mediated protein-protein interactions using the structure of SH2-phosphopeptide complexes and the FoldX algorithm. We sho
Externí odkaz:
https://doaj.org/article/75a9b60eec3d46479dadde2f9585e58e
Publikováno v:
PLoS Computational Biology, Vol 4, Iss 2, p e1000002 (2008)
Numerous studies have noted that the evolution of new enzymatic specificities is accompanied by loss of the protein's thermodynamic stability (DeltaDeltaG), thus suggesting a tradeoff between the acquisition of new enzymatic functions and stability.
Externí odkaz:
https://doaj.org/article/b59573cef58247f2b3fb62b0d97320f0
Autor:
Julia V. Burnier, Luis Serrano, Francois Stricher, Almer M. van der Sloot, Raquel Garcia-Olivas, Raik Grünberg, Arrate Mallabiabarrena, Xavier Sanjuan, Tony Ferrar, Violeta Beltran-Sastre, Timo Zimmermann
Publikováno v:
Nature Methods. 10:1021-1027
Fluorescence resonance energy transfer (FRET)-based detection of protein interactions is limited by the very narrow range of FRET-permitting distances. We show two different strategies for the rational design of weak helper interactions that co-recru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6caf1c6cb9048434b16b96e71c4e454
https://doi.org/10.1038/nmeth.2625
https://doi.org/10.1038/nmeth.2625
Autor:
Lies Baeten, Joost Schymkowitz, Peter Vanhee, Luis Serrano, Erik Verschueren, Frederic Rousseau, Francois Stricher
Publikováno v:
Nucleic Acids Research
High-resolution structures of proteins remain the most valuable source for understanding their function in the cell and provide leads for drug design. Since the availability of sufficient protein structures to tackle complex problems such as modeling
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12b2ef8466fc351d30091da49245bc5a
https://doi.org/10.1093/nar/gkq972
https://doi.org/10.1093/nar/gkq972
Publikováno v:
Journal of Molecular Biology. 400:605-617
This study addresses the relation between structural and functional similarity in proteins. We introduce a novel method named tree based on root mean square deviation (T-RMSD), which uses distance RMSD (dRMSD) variations to build fine-grained structu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a390d0673a0703f236941c24606395e1
https://doi.org/10.1016/j.jmb.2010.05.012
https://doi.org/10.1016/j.jmb.2010.05.012
Autor:
Lies L. Baeten, Frederic Rousseau, Luis Serrano, Peter Vanhee, Joost Schymkowitz, Erik Verschueren, Francois Stricher, Tom Lenaerts
Publikováno v:
Structure. 17:1128-1136
We compared the modes of interaction between protein-peptide interfaces and those observed within monomeric proteins and found surprisingly few differences. Over 65% of 731 protein-peptide interfaces could be reconstructed within 1 angstrom RMSD usin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe8c40c2c3478c14d5d5593ed27c763a
https://doi.org/10.1016/j.str.2009.06.013
https://doi.org/10.1016/j.str.2009.06.013
Autor:
Ignacio E. Sánchez, G. Fernandez-Ballester, José Antonio Encinar, Francois Stricher, E. Hurtado-Gomez, Pedro Beltrao, Luis Serrano
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Motivation: Most of the structures and functions of proteome globular domains are yet unknown. We can use high-resolution structures from different modular domains in combination with automatic protein design algorithms to predict genome-wide potenti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82b4cc0f33bce9e6e3bf783d67f81077
https://doi.org/10.1093/bioinformatics/btp424
https://doi.org/10.1093/bioinformatics/btp424
Publikováno v:
Nucleic Acids Research
Meganucleases cut long (>12 bp) unique sequences in genomes and can be used to induce targeted genome engineering by homologous recombination in the vicinity of their cleavage site. However, the use of natural meganucleases is limited by the repertoi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0276f56a92b4a89eea19f5df3edcefa6
https://doi.org/10.1093/nar/gkn059
https://doi.org/10.1093/nar/gkn059
Publikováno v:
The American Journal of Human Genetics. 81(5):1006-1024
Phenylketonuria (PKU) is a genetic disease caused by mutations in human phenylalanine hydroxylase (PAH). Most missense mutations result in misfolding of PAH, increased protein turnover, and a loss of enzymatic function. We studied the prediction of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24889e4aed2a2cefe492283ff284fb18
Autor:
Jerónimo Bravo, Christophe Perez, Guillermo Montoya, Francois Stricher, Luis Serrano, Francisco J. Blanco, Sandra Rolland, Amélie Patin, Anne-Sophie Petit, Sylvain Arnould, Emmanuel Lacroix, Aymeric Duclert, Sophie Guillier, Jesús Prieto, Jean-Charles Epinat, Patrick Chames, Frédéric Pâques, Philippe Duchateau
Publikováno v:
Journal of Molecular Biology. 355:443-458
The last decade has seen the emergence of a universal method for precise and efficient genome engineering. This method relies on the use of sequence-specific endonucleases such as homing endonucleases. The structures of several of these proteins are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ddb06c8d7fd709a2ee5c267fe63aaee
https://doi.org/10.1016/j.jmb.2005.10.065
https://doi.org/10.1016/j.jmb.2005.10.065