Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis - Test2 - elhamkhani - TriplyDB

Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis

Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis

http://www.wikidata.org/entity/Q30505748

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Inhibition of arginyltransferase 1 induces transcriptional activity of myocardin-related transcription factor A (MRTF-A) and promotes directional migration.Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation.Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.Control of Pim2 kinase stability and expression in transformed human haematopoietic cells Loss of ATE1-mediated arginylation leads to impaired platelet myosin phosphorylation, clot retraction, and in vivo thrombosis formation.Post-translational protein arginylation in the normal nervous system and in neurodegeneration.Regulating the regulators: Epigenetic, transcriptional, and post-translational regulation of RGS proteins.

P2860

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P2860

Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesis

http://www.wikidata.org/entity/Q30505748

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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name

Small molecule inhibitors of a ...... ell motility, and angiogenesis

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Small molecule inhibitors of a ...... ell motility, and angiogenesis

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J.BCP.2012.01.012

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Biochemical Pharmacology

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Small molecule inhibitors of a ...... ell motility, and angiogenesis

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P2093

Anna Kashina

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Brenda Lilly

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Brian Buckley

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Junling Wang

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Mikhail Chernov

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Qingqing Wang

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Sougata Saha

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P2860

Arginylation-dependent neural crest cell migration is essential for mouse development

In vivo half-life of a protein is a function of its amino-terminal residue

Global analysis of posttranslational protein arginylation.

Identification of mammalian arginyltransferases that modify a specific subset of protein substrates

Purification and characterization of arginyl-tRNA-protein transferase from rabbit reticulocytes. Its involvement in post-translational modification and degradation of acidic NH2 termini substrates of the ubiquitin pathway.

Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.

Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations.

Identification and characterization of regulator of G protein signaling 4 (RGS4) as a novel inhibitor of tubulogenesis: RGS4 inhibits mitogen-activated protein kinases and vascular endothelial growth factor signaling.

RGS4 and RGS5 are in vivo substrates of the N-end rule pathway

Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity

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866-873

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10.1016/J.BCP.2012.01.012

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7

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83

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221780671

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22280815

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3288401

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