Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Marta E. Hallak"'
Publikováno v:
Cell Communication and Signaling, Vol 22, Iss 1, Pp 1-17 (2024)
Abstract Background Arginyltransferase (Ate1) orchestrates posttranslational protein arginylation, a pivotal regulator of cellular proteolytic processes. In eukaryotic cells, two interconnected systems—the ubiquitin proteasome system (UPS) and macr
Externí odkaz:
https://doaj.org/article/80774d2b7ef044ca81148c1ba202484a
Publikováno v:
GliaREFERENCES. 70(2)
Addition of arginine (Arg) from tRNA can cause major alterations of structure and function of protein substrates. This post-translational modification, termed protein arginylation, is mediated by the enzyme arginyl-tRNA-protein transferase 1 (Ate1).
Publikováno v:
Molecular Neurobiology. 56:1653-1664
After retrotranslocation from the endoplasmic reticulum to the cytoplasm, calreticulin is modified by the enzyme arginyltransferase-1 (ATE1). Cellular levels of arginylated calreticulin (R-CRT) are regulated in part by the proteasomal system. Under v
Publikováno v:
Journal of Neurochemistry. 138:506-517
Post-translational arginylation of proteins is an important regulator of many physiological pathways in cells. This modification was originally noted in protein degradation during neurodegenerative processes, with an apparently different physiologica
Autor:
Guillermo G. Montich, María Belén Decca, Graciela A. Borioli, Marta E. Hallak, Alejandro Moreschi, Edith Sandra Durand
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1867(3)
Calreticulin (CRT) is a calcium-binding protein that participates in several cellular processes including the control of protein folding and homeostasis of Ca2+. Its folding, stability and functions are strongly controlled by the presence of Ca2+. Th
Publikováno v:
Journal of Biological Chemistry. 287:22043-22054
Post-translational modifications of proteins are important for the regulation of cell fate and functions; one of these post-translational modifications is arginylation. We have previously established that calreticulin (CRT), an endoplasmic reticulum
Autor:
Mauricio R, Galiano, Marta E, Hallak
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1337
To evaluate the posttranslational arginylation of proteins in vivo, we describe a protocol for studying the (14)C-Arg incorporation into proteins of cells in culture. The conditions determined for this particular modification contemplate both the bio
Autor:
Mauricio R. Galiano, Marta E. Hallak
Publikováno v:
Methods in Molecular Biology ISBN: 9781493929344
Methods in Molecular Biology ISBN: 9781071629413
Methods in Molecular Biology ISBN: 9781071629413
To evaluate the posttranslational arginylation of proteins in vivo, we describe a protocol for studying the (14)C-Arg incorporation into proteins of cells in culture. The conditions determined for this particular modification contemplate both the bio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c43c2ac94698fb9b7537588ccb4e6d8
https://doi.org/10.1007/978-1-4939-2935-1_7
https://doi.org/10.1007/978-1-4939-2935-1_7
Calreticulin and Arginylated Calreticulin Have Different Susceptibilities to Proteasomal Degradation
Autor:
Victor Goitea, Marta E. Hallak
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Post-translational arginylation has been suggested to target proteins for proteasomal degradation. The degradation mechanism for arginylated calreticulin (R-CRT) localized in the cytoplasm is unknown. To evaluate the effect of arginylation on CRT sta
Autor:
Didier Job, Annie Schweitzer, Mauricio R. Galiano, Marta E. Hallak, Annie Andrieux, Christophe Bosc
Publikováno v:
Journal of Neuroscience Research. 78:329-337
Many cell types contain subpopulations of microtubules that resist depolymerizing conditions, such as exposure to cold or to the drug nocodazole. This stabilization is due mainly to polymer association with STOP proteins. In mouse, neurons express tw