Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network.
about
An intrinsically disordered region of the acetyltransferase p300 with similarity to prion-like domains plays a role in aggregationA Structural Basis for the Assembly and Functions of a Viral Polymer that Inactivates Multiple Tumor SuppressorsNew tricks for "old" domains: how novel architectures and promiscuous hubs contributed to the organization and evolution of the ECMMapping small molecule binding data to structural domainsSimulated evolution of protein-protein interaction networks with realistic topology.Evaluation of sequence features from intrinsically disordered regions for the estimation of protein function.Transient protein-protein interface prediction: datasets, features, algorithms, and the RAD-T predictor.Multiple-Localization and Hub Proteins.Content of intrinsic disorder influences the outcome of cell-free protein synthesis.Virtual interactomics of proteins from biochemical standpoint.Evolutionary Model Selection and Parameter Estimation for Protein-Protein Interaction Network Based on Differential Evolution Algorithm.Hub promiscuity in protein-protein interaction networks.The PP1 binding code: a molecular-lego strategy that governs specificity.Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes.Biological messiness vs. biological genius: Mechanistic aspects and roles of protein promiscuity.How do disordered regions achieve comparable functions to structured domains?Molecular recognition features (MoRFs) in three domains of life.At the Interface of Three Nucleic Acids: The Role of RNA-Binding Proteins and Poly(ADP-ribose) in DNA Repair.Exploring the binding diversity of intrinsically disordered proteins involved in one-to-many binding.Extreme multifunctional proteins identified from a human protein interaction network.The role of structural disorder in the rewiring of protein interactions through evolution.A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes.Deciphering the cause of evolutionary variance within intrinsically disordered regions in human proteins.Long disordered regions of the C-terminal domain of Abelson tyrosine kinase have specific and additive functions in regulation and axon localization.pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Tat peptide-calmodulin binding studies and bioinformatics of HIV-1 protein-calmodulin interactions.Structural flexibility of intrinsically disordered proteins induces stepwise target recognition.
P2860
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P2860
Domain distribution and intrinsic disorder in hubs in the human protein-protein interaction network.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Domain distribution and intrin ...... n-protein interaction network.
@en
Domain distribution and intrin ...... n-protein interaction network.
@nl
type
label
Domain distribution and intrin ...... n-protein interaction network.
@en
Domain distribution and intrin ...... n-protein interaction network.
@nl
prefLabel
Domain distribution and intrin ...... n-protein interaction network.
@en
Domain distribution and intrin ...... n-protein interaction network.
@nl
P2860
P356
P1433
P1476
Domain distribution and intrin ...... n-protein interaction network.
@en
P2093
Ashwini Patil
Kengo Kinoshita
P2860
P304
P356
10.1002/PRO.425
P577
2010-08-01T00:00:00Z