Multi-Scaled Explorations of Binding-Induced Folding of Intrinsically Disordered Protein Inhibitor IA3 to its Target Enzyme

Autor: Wei Han, Yong Wang, Xiakun Chu, Stephen J. Hagen, Jin Wang, Erkang Wang

Publikováno v: PLoS Computational Biology
PLoS Computational Biology, Vol 7, Iss 4, p e1001118 (2011)

Biomolecular function is realized by recognition, and increasing evidence shows that recognition is determined not only by structure but also by flexibility and dynamics. We explored a biomolecular recognition process that involves a major conformati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c06205a98e592b3d1fca890903ae078
http://europepmc.org/articles/PMC3072359

The dynamics of Ca2+ ions within the solvation shell of calbindin D9k

Autor: Esther Nachliel, Elad, Menachem Gutman

Publikováno v: PLoS ONE, Vol 6, Iss 2, p e14718 (2011)
PLoS ONE

The encounter of a Ca(2+) ion with a protein and its subsequent binding to specific binding sites is an intricate process that cannot be fully elucidated from experimental observations. We have applied Molecular Dynamics to study this process with at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9233b0665b8841bbf141d7f5c546d793
http://europepmc.org/articles/PMC3043054?pdf=render

Modelling Vesicular Release at Hippocampal Synapses

Autor: Herbert Levine, Thomas M. Bartol, Suhita Nadkarni, Terrence J. Sejnowski

Publikováno v: PLoS Computational Biology
PLoS Computational Biology, Vol 6, Iss 11, p e1000983 (2010)

We study local calcium dynamics leading to a vesicle fusion in a stochastic, and spatially explicit, biophysical model of the CA3-CA1 presynaptic bouton. The kinetic model for vesicle release has two calcium sensors, a sensor for fast synchronous rel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e74412b23174a0ab8038e74354aff73
http://europepmc.org/articles/PMC2978677

Networks of high mutual information define the structural proximity of catalytic sites: implications for catalytic residue identification

Autor: Morten Nielsen, José M. Delfino, Elin Teppa, Cristina Marino Buslje, Tomás Di Domenico

Publikováno v: PLoS Computational Biology, Vol 6, Iss 11, p e1000978 (2010)
PLoS Computational Biology
Buslje, C M, Teppa, E, Di Doménico, T, Delfino, J M & Nielsen, M 2010, ' Networks of High Mutual Information Define the Structural Proximity of Catalytic Sites: Implications for Catalytic Residue Identification ', P L o S Computational Biology (Online), vol. 6, no. 11 . https://doi.org/10.1371/journal.pcbi.1000978
Scopus-Elsevier

Identification of catalytic residues (CR) is essential for the characterization of enzyme function. CR are, in general, conserved and located in the functional site of a protein in order to attain their function. However, many non-catalytic residues

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3259373c836d5c8f01d79c0bf53d16e
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21079665/?tool=EBI

Additional serine/threonine phosphorylation reduces binding affinity but preserves interface topography of substrate proteins to the c-Cbl TKB domain

Autor: Qingxiang Sun, Graeme R. Guy, J. Sivaraman, Cherlyn Ng, Rebecca A. Jackson

Publikováno v: PLoS ONE, Vol 5, Iss 9, p e12819 (2010)
PLoS ONE

The E3-ubiquitin ligase, c-Cbl, is a multi-functional scaffolding protein that plays a pivotal role in controlling cell phenotype. As part of the ubiquitination and downregulation process, c-Cbl recognizes targets, such as tyrosine kinases and the Sp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44b862f86efa6ed802cd0e5040394a9d
http://europepmc.org/articles/PMC2943896?pdf=render