RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
about
The N-end rule pathwayMouse Dfa is a repressor of TATA-box promoters and interacts with the Abt1 activator of basal transcriptionDiscovery of cellular regulation by protein degradationGalphao/i-stimulated proteosomal degradation of RGS20: a mechanism for temporal integration of Gs and Gi pathwaysDiversity of degradation signals in the ubiquitin-proteasome systemSynthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathwayN-Terminal Acetylation-Targeted N-End Rule Proteolytic System: The Ac/N-End Rule PathwayPerspectives and Insights into the Competition for Aminoacyl-tRNAs between the Translational Machinery and for tRNA Dependent Non-Ribosomal Peptide Bond FormationWaterproofing crops: effective flooding survival strategiesArginylation-dependent neural crest cell migration is essential for mouse developmentRegulators of G-protein signaling in the heart and their potential as therapeutic targets.Amino acids induce peptide uptake via accelerated degradation of CUP9, the transcriptional repressor of the PTR2 peptide transporter.Global analysis of posttranslational protein arginylation.The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule pathway, stabilizes Tex19.1 during spermatogenesisLiat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeatsBiochemical and genetic studies of UBR3, a ubiquitin ligase with a function in olfactory and other sensory systemsUBR2 mediates transcriptional silencing during spermatogenesis via histone ubiquitinationFBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends on a Cullin 4B/DDB1 Complex.Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.Generation of Artificial N-end Rule Substrate Proteins In Vivo and In Vitro.An improved workflow for quantitative N-terminal charge-based fractional diagonal chromatography (ChaFRADIC) to study proteolytic events in Arabidopsis thaliana.The evolution of regulators of G protein signalling proteins as drug targets - 20 years in the making: IUPHAR Review 21.Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.The substrate recognition domains of the N-end rule pathway.Arginyltransferase regulates alpha cardiac actin function, myofibril formation and contractility during heart development.Small molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesisRab family proteins regulate the endosomal trafficking and function of RGS4.Ablation of arginylation in the mouse N-end rule pathway: loss of fat, higher metabolic rate, damaged spermatogenesis, and neurological perturbations.The anti-apoptotic form of tyrosine kinase Lyn that is generated by proteolysis is degraded by the N-end rule pathway.Upregulation of RGS4 and downregulation of CPI-17 mediate inhibition of colonic muscle contraction by interleukin-1beta.Variations in Gnai2 and Rgs1 expression affect chemokine receptor signaling and the organization of secondary lymphoid organs.Ubiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndromeProtein arginylation, a global biological regulator that targets actin cytoskeleton and the muscleA neurostimulant para-chloroamphetamine inhibits the arginylation branch of the N-end rule pathway.The N-end rule pathway and regulation by proteolysisMEKK1-MKK4-JNK-AP1 pathway negatively regulates Rgs4 expression in colonic smooth muscle cellsUBR2 of the N-end rule pathway is required for chromosome stability via histone ubiquitylation in spermatocytes and somatic cells.Thinking outside of the "RGS box": new approaches to therapeutic targeting of regulators of G protein signaling.DHHC protein-dependent palmitoylation protects regulator of G-protein signaling 4 from proteasome degradation.Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity
P2860
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P2860
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
description
2005 nî lūn-bûn
@nan
2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@ast
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@en
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@nl
type
label
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@ast
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@en
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@nl
prefLabel
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@ast
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@en
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@nl
P2093
P2860
P356
P1476
RGS4 and RGS5 are in vivo substrates of the N-end rule pathway
@en
P2093
Ilia V Davydov
Jee Young An
Kayoko Moroi
Min Jae Lee
Takafumi Tasaki
Yong Tae Kwon
P2860
P304
15030-15035
P356
10.1073/PNAS.0507533102
P407
P50
P577
2005-10-10T00:00:00Z