Optimization of specificity in a cellular protein interaction network by negative selection.
about
The conservation pattern of short linear motifs is highly correlated with the function of interacting protein domainsTwo-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysisSRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactomeEfficient T-cell receptor signaling requires a high-affinity interaction between the Gads C-SH3 domain and the SLP-76 RxxK motifThe BAR domain proteins: molding membranes in fission, fusion, and phagyThe development and application of a quantitative peptide microarray based approach to protein interaction domain specificity spaceStructural mechanism for the specific assembly and activation of the extracellular signal regulated kinase 5 (ERK5) moduleInferring protein domain interactions from databases of interacting proteins.Prokaryotic 2-component systems and the OmpR/PhoB superfamilyShort linear motifs - ex nihilo evolution of protein regulationHydrophobicity and charge shape cellular metabolite concentrationsSynthetic biology: lessons from engineering yeast MAPK signalling pathwaysStructural, Functional, and Bioinformatic Studies Demonstrate the Crucial Role of an Extended Peptide Binding Site for the SH3 Domain of Yeast Abp1pDistinct Peptide Binding Specificities of Src Homology 3 (SH3) Protein Domains Can Be Determined by Modulation of Local Energetics across the Binding InterfaceSuperbinder SH2 domains act as antagonists of cell signalingTransmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway.Interaction with the SH3 domain protein Bem1 regulates signaling by the Saccharomyces cerevisiae p21-activated kinase Ste20Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins.Identifying cognate binding pairs among a large set of paralogs: the case of PE/PPE proteins of Mycobacterium tuberculosisNovel peptide-mediated interactions derived from high-resolution 3-dimensional structuresDifferential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysisInterface-resolved network of protein-protein interactionsEvolution of domain-peptide interactions to coadapt specificity and affinity to functional diversityAn inter-species protein-protein interaction network across vast evolutionary distanceQuantification of the transferability of a designed protein specificity switch reveals extensive epistasis in molecular recognitionAmino-acid site variability among natural and designed proteinsDesign of multi-specificity in protein interfacesSH2 Domains Recognize Contextual Peptide Sequence Information to Determine SelectivitySite-selective Characterization of Src Homology 3 Domain Molecular Recognition with Cyanophenylalanine Infrared Probes.Yeast osmosensors Hkr1 and Msb2 activate the Hog1 MAPK cascade by different mechanisms.Engineering of weak helper interactions for high-efficiency FRET probes.SH3 interactome conserves general function over specific form.Domain-mediated protein interaction prediction: From genome to network.Transient protein-protein interaction of the SH3-peptide complex via closely located multiple binding sites.Arginine mimetics using α-guanidino acids: introduction of functional groups and stereochemistry adjacent to recognition guanidiniums in peptidesSpecificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transductionA Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.MOTIPS: automated motif analysis for predicting targets of modular protein domainsQuantitative relation between intermolecular and intramolecular binding of pro-rich peptides to SH3 domains.Optimizing scoring function of protein-nucleic acid interactions with both affinity and specificity.
P2860
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P2860
Optimization of specificity in a cellular protein interaction network by negative selection.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Optimization of specificity in ...... network by negative selection.
@ast
Optimization of specificity in ...... network by negative selection.
@en
Optimization of specificity in ...... network by negative selection.
@nl
type
label
Optimization of specificity in ...... network by negative selection.
@ast
Optimization of specificity in ...... network by negative selection.
@en
Optimization of specificity in ...... network by negative selection.
@nl
prefLabel
Optimization of specificity in ...... network by negative selection.
@ast
Optimization of specificity in ...... network by negative selection.
@en
Optimization of specificity in ...... network by negative selection.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Optimization of specificity in ...... network by negative selection.
@en
P2093
Ali Zarrinpar
Sang-Hyun Park
Wendell A Lim
P2860
P2888
P304
P3181
P356
10.1038/NATURE02178
P407
P577
2003-12-11T00:00:00Z
P5875
P6179
1039601295