Cargando…

Posttranslational arginylation enzyme Ate1 affects DNA mutagenesis by regulating stress response

Arginyltransferase 1 (Ate1) mediates protein arginylation, a poorly understood protein posttranslational modification (PTM) in eukaryotic cells. Previous evidence suggest a potential involvement of arginylation in stress response and this PTM was traditionally considered anti-apoptotic based on the...

Descripción completa

Detalles Bibliográficos
Autores principales:	Kumar, Akhilesh, Birnbaum, Michael D, Patel, Devang M, Morgan, William M, Singh, Jayanti, Barrientos, Antoni, Zhang, Fangliang
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group 2016
Materias:	Original Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5059882/ https://www.ncbi.nlm.nih.gov/pubmed/27685622 http://dx.doi.org/10.1038/cddis.2016.284

Ejemplares similares

Posttranslational Arginylation Enzyme Arginyltransferase1 Shows Genetic Interactions With Specific Cellular Pathways in vivo
por: Wiley, David J., et al.
Publicado: (2020)

Ate1-mediated posttranslational arginylation affects substrate adhesion and cell migration in Dictyostelium discoideum
por: Batsios, Petros, et al.
Publicado: (2019)

Global Analysis of Posttranslational Protein Arginylation
por: Wong, Catherine C. L, et al.
Publicado: (2007)

Insertion/deletion-activated frame-shift fluorescence protein is a sensitive reporter for genomic DNA editing
por: Kumar, Akhilesh, et al.
Publicado: (2019)

Arginylation regulates purine nucleotide biosynthesis by enhancing the activity of phosphoribosyl pyrophosphate synthase
por: Zhang, Fangliang, et al.
Publicado: (2015)

Crystal structure of the Ate1 arginyl-tRNA-protein transferase and arginylation of N-degron substrates
por: Kim, Bong Heon, et al.
Publicado: (2022)

Posttranslational Chemical Mutagenesis Methods to Insert Posttranslational Modifications into Recombinant Proteins
por: Harel, Omer, et al.
Publicado: (2022)

Arginylation-dependent regulation of a proteolytic product of talin is essential for cell–cell adhesion
por: Zhang, Fangliang, et al.
Publicado: (2012)

Iron-sulfur clusters are involved in post-translational arginylation
por: Van, Verna, et al.
Publicado: (2023)

Arginylation-Dependent Neural Crest Cell Migration Is Essential for Mouse Development
por: Kurosaka, Satoshi, et al.
Publicado: (2010)

Global Analysis of Post-Translational Side-Chain Arginylation Using Pan-Arginylation Antibodies
por: MacTaggart, Brittany, et al.
Publicado: (2023)

Arginylation Regulates Intracellular Actin Polymer Level by Modulating Actin Properties and Binding of Capping and Severing Proteins
por: Saha, Sougata, et al.
Publicado: (2010)

Regulation of Mitochondrial Respiratory Chain Complex Levels, Organization, and Function by Arginyltransferase 1
por: Jiang, Chunhua, et al.
Publicado: (2020)

α-Synuclein arginylation in the human brain
por: Zhao, Jun, et al.
Publicado: (2022)

Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
por: White, Mark D., et al.
Publicado: (2017)

Arginyltransferase ATE1 suppresses cell tumorigenic potential and inversely correlates with metastases in human cancers
por: Rai, Reena, et al.
Publicado: (2015)

Arginylation Regulates G-protein Signaling in the Retina
por: Fina, Marie E., et al.
Publicado: (2022)

Quantification of intracellular N-terminal β-actin arginylation
por: Chen, Li, et al.
Publicado: (2019)

JMJD5 is a human arginyl C-3 hydroxylase
por: Wilkins, Sarah E., et al.
Publicado: (2018)

Amino-terminal arginylation as a degradation signal for selective autophagy
por: Cha-Molstad, Hyunjoo, et al.
Publicado: (2015)

The ZZ domain of HERC2 is a receptor of arginylated substrates
por: Tencer, Adam H., et al.
Publicado: (2022)

Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase
por: Avcilar-Kucukgoze, Irem, et al.
Publicado: (2022)

Arginine deprivation affects glioblastoma cell adhesion, invasiveness and actin cytoskeleton organization by impairment of β-actin arginylation
por: Pavlyk, Iuliia, et al.
Publicado: (2014)

Protein Arginylation Is Regulated during SARS-CoV-2 Infection
por: Macedo-da-Silva, Janaina, et al.
Publicado: (2023)

Publisher Correction: JMJD5 is a human arginyl C-3 hydroxylase
por: Wilkins, Sarah E., et al.
Publicado: (2018)

Protein arginylation regulates cellular stress response by stabilizing HSP70 and HSP40 transcripts
por: Deka, Kamalakshi, et al.
Publicado: (2016)

Posttranslational Regulation of Human DNA Polymerase ι
por: McIntyre, Justyna, et al.
Publicado: (2015)

Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein
Publicado: (1983)

Arginylation: a new regulator of mRNA stability and heat stress response
por: Deka, Kamalakshi, et al.
Publicado: (2017)

SUMOylation of Arginyl tRNA Synthetase Modulates the Drosophila Innate Immune Response
por: Nayak, Prajna, et al.
Publicado: (2021)

Availability of Arg, but Not tRNA, Is a Rate-Limiting Factor for Intracellular Arginylation
por: Avcilar-Kucukgoze, Irem, et al.
Publicado: (2021)

The structural basis of tRNA recognition by arginyl-tRNA-protein transferase
por: Abeywansha, Thilini, et al.
Publicado: (2023)

Protein arginylation targets alpha synuclein, facilitates normal brain health, and prevents neurodegeneration
por: Wang, Junling, et al.
Publicado: (2017)

Restriction enzyme-free mutagenesis via the light regulation of DNA polymerization
por: Young, Douglas D., et al.
Publicado: (2009)

Reduced Arginyltransferase 1 is a driver and a potential prognostic indicator of prostate cancer metastasis
por: Birnbaum, Michael D., et al.
Publicado: (2018)

Oxidative, Reductive, and Nitrosative Stress Effects on Epigenetics and on Posttranslational Modification of Enzymes in Cardiometabolic Diseases
por: Pérez-Torres, I., et al.
Publicado: (2020)

A Neurostimulant para-Chloroamphetamine Inhibits the Arginylation Branch of the N-end Rule Pathway
por: Jiang, Yanxialei, et al.
Publicado: (2014)

Inhibitors of both the N-methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases
por: Bonnici, Joanna, et al.
Publicado: (2018)

Co-Immobilization of RizA Variants with Acetate Kinase for the Production of Bioactive Arginyl Dipeptides
por: Bordewick, Sven, et al.
Publicado: (2022)

Posttranslational Modifications in Ferroptosis
por: Wei, Xiang, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_t76mpsdk3t5d113pfn5ngd36gr