Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution. - Test2 - elhamkhani - TriplyDB

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

http://www.wikidata.org/entity/Q34162330

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Motif co-regulation and co-operativity are common mechanisms in transcriptional, post-transcriptional and post-translational regulation Short linear motifs - ex nihilo evolution of protein regulation Coiled-coil proteins facilitated the functional expansion of the centrosome Alp/Enigma family proteins cooperate in Z-disc formation and myofibril assembly Stereochemical Determinants of C-terminal Specificity in PDZ Peptide-binding Domains: A NOVEL CONTRIBUTION OF THE CARBOXYLATE-BINDING LOOP Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1 Stereochemical Preferences Modulate Affinity and Selectivity among Five PDZ Domains that Bind CFTR: Comparative Structural and Sequence Analyses Large-scale interaction profiling of PDZ domains through proteomic peptide-phage display using human and viral phage peptidomes Discovery and confirmation of ligand binding specificities of the Schistosoma japonicum polarity protein Scribble K-shell Analysis Reveals Distinct Functional Parts in an Electron Transfer Network and Its Implications for Extracellular Electron Transfer DoReMi: context-based prioritization of linear motif matches SH3 interactome conserves general function over specific form.Linear motif-mediated interactions have contributed to the evolution of modularity in complex protein interaction networks Molecular characterization and ligand binding specificity of the PDZ domain-containing protein GIPC3 from Schistosoma japonicum.Pre-metazoan origins and evolution of the cadherin adhesome.High-throughput methods for identification of protein-protein interactions involving short linear motifs.PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-β3 (PLC-β3)-specific activation of somatostatin by forming a ternary complex with PLC-β3 and somatostatin receptors Zeta Inhibitory Peptide Disrupts Electrostatic Interactions That Maintain Atypical Protein Kinase C in Its Active Conformation on the Scaffold p62.Secondary PDZ domain-binding site on class B plexins enhances the affinity for PDZ-RhoGEF Network rewiring is an important mechanism of gene essentiality change Metazoans evolved by taking domains from soluble proteins to expand intercellular communication network.modPDZpep: a web resource for structure based analysis of human PDZ-mediated interaction networks Plasticity of PDZ domains in ligand recognition and signaling.Uncovering new aspects of protein interactions through analysis of specificity landscapes in peptide recognition domains.Claudins reign: The claudin/EMP/PMP22/γ channel protein family in C. elegans Exploring Short Linear Motifs Using the ELM Database and Tools.Algorithms for modeling global and context-specific functional relationship networks.Modeling dynamic functional relationship networks and application to ex vivo human erythroid differentiation Proteomic analysis reveals novel ligands and substrates for LNX1 E3 ubiquitin ligase.Peptide-binding domains: are limp handshakes safest?The Human SLC1A5 (ASCT2) Amino Acid Transporter: From Function to Structure and Role in Cell Biology

P2860

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P2860

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

http://www.wikidata.org/entity/Q34162330

description

2012 nî lūn-bûn

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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

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Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

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Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

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type

label

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

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Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@en

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@nl

prefLabel

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@ast

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@en

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@nl

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Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution.

@en

P2093

Inhae Kim

http://www.w3.org/2001/XMLSchema#string

Jihye Hwang

http://www.w3.org/2001/XMLSchema#string

Jinho Kim

http://www.w3.org/2001/XMLSchema#string

Yoon Sup Choi

http://www.w3.org/2001/XMLSchema#string

Young-Eun Shin

http://www.w3.org/2001/XMLSchema#string

P2860

Antagonism of LIN-17/Frizzled and LIN-18/Ryk in nematode vulva induction reveals evolutionary alterations in core developmental pathways

Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species

Neuroligins 3 and 4X interact with syntrophin-gamma2, and the interactions are affected by autism-related mutations

Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are associated with autism

CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95

X-linked mental retardation and autism are associated with a mutation in the NLGN4 gene, a member of the neuroligin family

Online Mendelian Inheritance in Man (OMIM), a knowledgebase of human genes and genetic disorders

Scaffold proteins: hubs for controlling the flow of cellular information

Identifying protein-binding sites from unaligned DNA fragments

PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor

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