CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation - Wikidata - awgldk - TriplyDB

CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation

CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation

http://www.wikidata.org/entity/Q28650415

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Cerebral Cavernous Malformations: Review of the Genetic and Protein-Protein Interactions Resulting in Disease Pathogenesis PAK6 targets to cell-cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface PDCD10 (CCM3) regulates brain endothelial barrier integrity in cerebral cavernous malformation type 3: role of CCM3-ERK1/2-cortactin cross-talk.Cerebral cavernous malformations arise from endothelial gain of MEKK3-KLF2/4 signalling.Introduction to cerebral cavernous malformation: a brief review.MicroRNA-103 suppresses tumor cell proliferation by targeting PDCD10 in prostate cancer.The cerebral cavernous malformations proteins.Exploring Coronary Artery Disease GWAs Targets With Functional Links to Immunometabolism

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P2860

CCM2-CCM3 interaction stabilizes their protein expression and permits endothelial network formation

http://www.wikidata.org/entity/Q28650415

description

2015 nî lūn-bûn

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2015 թուականի Մարտին հրատարակուած գիտական յօդուած

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2015 թվականի մարտին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@ast

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@en

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

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type

label

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@ast

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@en

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@nl

prefLabel

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@ast

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@en

CCM2-CCM3 interaction stabiliz ...... endothelial network formation

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Journal of Cell Biology

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CCM2-CCM3 interaction stabiliz ...... endothelial network formation

@en

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David A Calderwood

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

Giulia Villari

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

Kyle M Draheim

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

Rong Zhang

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

Titus J Boggon

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

Xiaofeng Li

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

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Adaptor protein cerebral cavernous malformation 3 (CCM3) mediates phosphorylation of the cytoskeletal proteins ezrin/radixin/moesin by mammalian Ste20-4 to protect cells from oxidative stress

Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus

A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein

Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity

CCM3 interacts with CCM2 indicating common pathogenesis for cerebral cavernous malformations

Cerebral cavernous malformation protein CCM1 inhibits sprouting angiogenesis by activating DELTA-NOTCH signaling.

Mutations in a gene encoding a novel protein containing a phosphotyrosine-binding domain cause type 2 cerebral cavernous malformations.

Far3 and five interacting proteins prevent premature recovery from pheromone arrest in the budding yeast Saccharomyces cerevisiae

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

Processing of X-ray diffraction data collected in oscillation mode

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987-1001

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scholarly article

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2569995

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10.1083/JCB.201407129

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7

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208

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Oriana S Fisher

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2015-03-30T00:00:00Z

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274372257

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25825518

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