Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
about
The N-end rule pathwayNuclear reprogramming: kinetics of cell cycle and metabolic progression as determinants of successSmall molecule inhibitors of arginyltransferase regulate arginylation-dependent protein degradation, cell motility, and angiogenesisArginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivoPlant arginyltransferases (ATEs).The N-end rule pathway and regulation by proteolysisCardioproteomics: advancing the discovery of signaling mechanisms involved in cardiovascular diseasesDegradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway.Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress responseIdentification of Targets and Interaction Partners of Arginyl-tRNA Protein Transferase in the Moss Physcomitrella patens.Loss of ATE1-mediated arginylation leads to impaired platelet myosin phosphorylation, clot retraction, and in vivo thrombosis formation.Posttranslational arginylation as a global biological regulator.Post-translational protein arginylation in the normal nervous system and in neurodegeneration.Arginylation and methylation double up to regulate nuclear proteins and nuclear architecture in vivo.Arginylation regulates myofibrils to maintain heart function and prevent dilated cardiomyopathy.Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegenerationProtein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts.Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.Arginyltransferase ATE1 is targeted to the neuronal growth cones and regulates neurite outgrowth during brain development.Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation.Arginyltransferase suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers.Post-translational arginylation as a novel regulator of platelet functionRapid and dynamic arginylation of the leading edge β- actin is required for cell migration.Spatio-temporal patterning of arginyl-tRNA protein transferase (ATE) contributes to gametophytic development in a moss.Target site specificity and in vivo complexity of the mammalian arginylome
P2860
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P2860
Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@ast
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@en
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@nl
type
label
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@ast
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@en
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@nl
prefLabel
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@ast
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@en
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@nl
P2093
P2860
P1476
Arginyltransferase is an ATP-i ...... functional complexes in vivo.
@en
P2093
Alexey Wolfson
Anna Kashina
Fangliang Zhang
John R Yates
Junling Wang
Sougata Saha
Xuemei Han
P2860
P304
P356
10.1016/J.CHEMBIOL.2010.10.016
P50
P577
2011-01-01T00:00:00Z