Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation - Wikidata - awgldk - TriplyDB

Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation

Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation

http://www.wikidata.org/entity/Q27695708

about

Genetic profiling of intrahepatic cholangiocarcinoma and its clinical implication in targeted therapy p38γ and p38δ Mitogen Activated Protein Kinases (MAPKs), New Stars in the MAPK Galaxy Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ.

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P2860

Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation

http://www.wikidata.org/entity/Q27695708

description

2014 nî lūn-bûn

@nan

2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Reciprocal allosteric regulati ...... in-modulated complex formation

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Reciprocal allosteric regulati ...... in-modulated complex formation

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Reciprocal allosteric regulati ...... in-modulated complex formation

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type

label

Reciprocal allosteric regulati ...... in-modulated complex formation

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Reciprocal allosteric regulati ...... in-modulated complex formation

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Reciprocal allosteric regulati ...... in-modulated complex formation

@nl

prefLabel

Reciprocal allosteric regulati ...... in-modulated complex formation

@ast

Reciprocal allosteric regulati ...... in-modulated complex formation

@en

Reciprocal allosteric regulati ...... in-modulated complex formation

@nl

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SCISIGNAL.2005722

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Science Signaling

P1476

Reciprocal allosteric regulati ...... in-modulated complex formation

@en

P2093

Chia-Cheng Chou

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

Mei-Ju Wu

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

Meng-Ru Ho

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

Shu-Yu Lin

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

Tzu-Ching Meng

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

P2860

Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin. A mechanism for specific substrate recognition

The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation

Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains

Large-scale structural analysis of the classical human protein tyrosine phosphatome

Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases

PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif.

Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing

PTPH1 dephosphorylates and cooperates with p38gamma MAPK to increase ras oncogenesis through PDZ-mediated interaction

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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ra98

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scholarly article

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2302277

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10.1126/SCISIGNAL.2005722

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347

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7

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Andrew H.-J. Wang

Abirami Santhanam

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2014-10-14T00:00:00Z

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266945339

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25314968

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