Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions.
about
DisProt: the Database of Disordered ProteinsStructural, Functional, and Bioinformatic Studies Demonstrate the Crucial Role of an Extended Peptide Binding Site for the SH3 Domain of Yeast Abp1pThe biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic contextComparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins.The WASP homologue Las17 activates the novel actin-regulatory activity of Ysc84 to promote endocytosis in yeastESTimating plant phylogeny: lessons from partitioningPredicting physiologically relevant SH3 domain mediated protein-protein interactions in yeast.Lipid binding by the Unique and SH3 domains of c-Src suggests a new regulatory mechanism.Domain-mediated protein interaction prediction: From genome to network.The identification of short linear motif-mediated interfaces within the human interactomeMOTIPS: automated motif analysis for predicting targets of modular protein domainsLocal structural disorder imparts plasticity on linear motifs.Inferring function using patterns of native disorder in proteinsGenome-wide prediction of SH2 domain targets using structural information and the FoldX algorithm.Attributes of short linear motifs.Intrinsic disorder and functional proteomics.Gene loss rate: a probabilistic measure for the conservation of eukaryotic genes.Proteome-wide discovery of evolutionary conserved sequences in disordered regions.Protein intrinsic disorder and network connectivity. The case of 14-3-3 proteins.An omics perspective of protein disorder.Interactions via intrinsically disordered regions: what kind of motifs?Computational structural analysis of protein interactions and networks.Selection maintains signaling function of a highly diverged intrinsically disordered region.The role of disorder in interaction networks: a structural analysis.Intramolecular Fuzzy Interactions Involving Intrinsically Disordered Domains.Short linear motifs in intrinsically disordered regions modulate HOG signaling capacity.
P2860
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P2860
Comparative genomics and disorder prediction identify biologically relevant SH3 protein interactions.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Comparative genomics and disor ...... evant SH3 protein interactions
@nl
Comparative genomics and disor ...... vant SH3 protein interactions.
@ast
Comparative genomics and disor ...... vant SH3 protein interactions.
@en
type
label
Comparative genomics and disor ...... evant SH3 protein interactions
@nl
Comparative genomics and disor ...... vant SH3 protein interactions.
@ast
Comparative genomics and disor ...... vant SH3 protein interactions.
@en
prefLabel
Comparative genomics and disor ...... evant SH3 protein interactions
@nl
Comparative genomics and disor ...... vant SH3 protein interactions.
@ast
Comparative genomics and disor ...... vant SH3 protein interactions.
@en
P2860
P1476
Comparative genomics and disor ...... vant SH3 protein interactions.
@en
P2093
Luis Serrano
P2860
P356
10.1371/JOURNAL.PCBI.0010026
P407
P577
2005-08-12T00:00:00Z