Global analysis of posttranslational protein arginylation. - Wikidata - wikimedia - TriplyDB

Global analysis of posttranslational protein arginylation.

Global analysis of posttranslational protein arginylation.

http://www.wikidata.org/entity/Q28469307

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Factors controlling cardiac neural crest cell migration Diversity of degradation signals in the ubiquitin-proteasome system Conditional Tek promoter-driven deletion of arginyltransferase in the germ line causes defects in gametogenesis and early embryonic lethality in mice Arginylation-dependent neural crest cell migration is essential for mouse development Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.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 angiogenesis Arginyltransferase ATE1 catalyzes midchain arginylation of proteins at side chain carboxylates in vivo Plant arginyltransferases (ATEs).Arginylation of myosin heavy chain regulates skeletal muscle strength Protein arginylation, a global biological regulator that targets actin cytoskeleton and the muscle The tubulin code: molecular components, readout mechanisms, and functions Differential arginylation of actin isoforms is regulated by coding sequence-dependent degradation.Post-translational modifications of microtubules.The N-end rule pathway and regulation by proteolysis Arginyltransferase is an ATP-independent self-regulating enzyme that forms distinct functional complexes in vivo.Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation.Chemical biology of protein arginine modifications in epigenetic regulation Arginylation regulates purine nucleotide biosynthesis by enhancing the activity of phosphoribosyl pyrophosphate synthase Arginylation-dependent regulation of a proteolytic product of talin is essential for cell-cell adhesion.Characterization of arginylation branch of N-end rule pathway in G-protein-mediated proliferation and signaling of cardiomyocytes Quantitative proteomics analysis of the Arg/N-end rule pathway of targeted degradation in Arabidopsis roots Reduced passive force in skeletal muscles lacking protein arginylation.Post-translational modification and regulation of actin.Multivalency-assisted control of intracellular signaling pathways: application for ubiquitin- dependent N-end rule pathway.Cell biology of embryonic migration.Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response Identification 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.The arginylation-dependent association of calreticulin with stress granules is regulated by calcium.Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts.The N-end rule pathway regulates pathogen responses in plants.Analyzing N-terminal Arginylation through the Use of Peptide Arrays and Degradation Assays.

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P2860

Global analysis of posttranslational protein arginylation.

http://www.wikidata.org/entity/Q28469307

description

2007 nî lūn-bûn

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2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Global analysis of posttranslational protein arginylation

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Global analysis of posttranslational protein arginylation.

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Global analysis of posttranslational protein arginylation.

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type

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Global analysis of posttranslational protein arginylation

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Global analysis of posttranslational protein arginylation.

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Global analysis of posttranslational protein arginylation.

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Global analysis of posttranslational protein arginylation

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Global analysis of posttranslational protein arginylation

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Global analysis of posttranslational protein arginylation.

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Global analysis of posttranslational protein arginylation.

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Global analysis of posttranslational protein arginylation.

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Aaron O Bailey

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Anna Kashina

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

Catherine C L Wong

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Henry Zebroski

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

John R Yates

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

Reena Rai

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

Tao Xu

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P2860

Aminopeptidase B (EC 3.4.11.6)

High resolution two-dimensional electrophoresis of proteins

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Cloning and functional analysis of the arginyl-tRNA-protein transferase gene ATE1 of Saccharomyces cerevisiae.

Transglutaminase 2: an enigmatic enzyme with diverse functions

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

DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics

A novel form of neurotensin post-translationally modified by arginylation.

Protein arginylation in rat brain cytosol: a proteomic analysis.

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

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