Literature DB >> 26285874

Protein Arginylation: Over 50 Years of Discovery.

Anna S Kashina1.   

Abstract

Posttranslational modifications have emerged in recent years as the major biological regulators responsible for the orders of magnitude increase in complexity of protein functions. These "molecular switches" affect nearly every protein in vivo by modulating their protein structure, activity, molecular interactions, and homeostasis. While over 350 protein modifications have been described, only a handful of them have been characterized. Until recently, protein arginylation has belonged to the list of obscure, poorly understood posttranslational modifications, before the recent explosion of studies has put arginylation on the map of intracellular metabolic pathways and biological processes. This chapter contains an overview of all the major milestones in the protein arginylation field, from its original discovery in 1963 to this day.

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Year:  2015        PMID: 26285874     DOI: 10.1007/978-1-4939-2935-1_1

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  3 in total

1.  tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

Authors:  Irem Avcilar-Kucukgoze; Howard Gamper; Christine Polte; Zoya Ignatova; Ralph Kraetzner; Michael Shtutman; Ya-Ming Hou; Dawei W Dong; Anna Kashina
Journal:  Cell Chem Biol       Date:  2020-06-16       Impact factor: 8.116

Review 2.  Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.

Authors:  Dilson E Rassier; Anna Kashina
Journal:  Am J Physiol Cell Physiol       Date:  2019-02-21       Impact factor: 4.249

3.  α-Synuclein arginylation in the human brain.

Authors:  Jun Zhao; Buyan Pan; Marie Fina; Yun Huang; Marie Shimogawa; Kelvin C Luk; Elizabeth Rhoades; E James Petersson; Dawei W Dong; Anna Kashina
Journal:  Transl Neurodegener       Date:  2022-04-08       Impact factor: 8.014

  3 in total

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