Literature DB >> 29167150

The dawn of succinylation: a posttranslational modification.

Matthew Alleyn1, Mason Breitzig1, Richard Lockey1, Narasaiah Kolliputi1.   

Abstract

Posttranslational modifications affect almost all proteins and are critical to a well-functioning and diverse proteome; however, many modifications remain relatively unknown and unstudied. This paper will give a perspective on the rapidly developing, novel posttranslational modification called succinylation. This modification may be implicated in numerous diseases, such as hepatic, cardiac, and pulmonary diseases. Although the influences of this modification still remain poorly understood, we are confident that further research into succinylation will provide an enhanced understanding of the complex machinery within the mitochondria, as well as the imposing consequences associated with its dysfunction.

Entities:  

Keywords:  metabolism; mitochondria; modification; posttranslational; sirtuin 5; succinylation

Mesh:

Substances:

Year:  2017        PMID: 29167150      PMCID: PMC5866436          DOI: 10.1152/ajpcell.00148.2017

Source DB:  PubMed          Journal:  Am J Physiol Cell Physiol        ISSN: 0363-6143            Impact factor:   4.249


  34 in total

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2.  Probing the active site of homoserine trans-succinylase.

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Journal:  FEBS Lett       Date:  2004-11-19       Impact factor: 4.124

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4.  Regulation of cellular metabolism by protein lysine acetylation.

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Journal:  Science       Date:  2010-02-19       Impact factor: 47.728

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7.  IL-6 cytoprotection in hyperoxic acute lung injury occurs via PI3K/Akt-mediated Bax phosphorylation.

Authors:  Narasaiah Kolliputi; Aaron B Waxman
Journal:  Am J Physiol Lung Cell Mol Physiol       Date:  2009-04-17       Impact factor: 5.464

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Authors:  Jintang Du; Yeyun Zhou; Xiaoyang Su; Jiu Jiu Yu; Saba Khan; Hong Jiang; Jungwoo Kim; Jimin Woo; Jun Huyn Kim; Brian Hyun Choi; Bin He; Wei Chen; Sheng Zhang; Richard A Cerione; Johan Auwerx; Quan Hao; Hening Lin
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10.  NADP(+)-IDH Mutations Promote Hypersuccinylation that Impairs Mitochondria Respiration and Induces Apoptosis Resistance.

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Journal:  Mol Cell       Date:  2015-11-12       Impact factor: 19.328

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  23 in total

1.  SIRT5 impairs aggregation and activation of the signaling adaptor MAVS through catalyzing lysine desuccinylation.

Authors:  Xing Liu; Chunchun Zhu; Huangyuan Zha; Jinhua Tang; Fangjing Rong; Xiaoyun Chen; Sijia Fan; Chenxi Xu; Juan Du; Junji Zhu; Jing Wang; Gang Ouyang; Guangqing Yu; Xiaolian Cai; Zhu Chen; Wuhan Xiao
Journal:  EMBO J       Date:  2020-04-17       Impact factor: 11.598

2.  Dietary succinate supplementation to maternal mice improves fetal brown adipose tissue development and thermogenesis of female offspring.

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Journal:  J Nutr Biochem       Date:  2021-11-18       Impact factor: 6.048

3.  Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage.

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Journal:  Appl Environ Microbiol       Date:  2020-11-24       Impact factor: 4.792

5.  Defining decreased protein succinylation of failing human cardiac myofibrils in ischemic cardiomyopathy.

Authors:  Hadi R Ali; Cole R Michel; Ying H Lin; Timothy A McKinsey; Mark Y Jeong; Amrut V Ambardekar; Joseph C Cleveland; Richard Reisdorph; Nichole Reisdorph; Kathleen C Woulfe; Kristofer S Fritz
Journal:  J Mol Cell Cardiol       Date:  2019-12-10       Impact factor: 5.000

Review 6.  Addressing the Possibility of a Histone-Like Code in Bacteria.

Authors:  Valerie J Carabetta
Journal:  J Proteome Res       Date:  2020-10-02       Impact factor: 4.466

Review 7.  The Mystery of Extramitochondrial Proteins Lysine Succinylation.

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Review 8.  Metabolic reprogramming and epigenetic modifications on the path to cancer.

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Journal:  Protein Cell       Date:  2021-05-29       Impact factor: 15.328

Review 9.  Large-Scale Assessment of Bioinformatics Tools for Lysine Succinylation Sites.

Authors:  Md Mehedi Hasan; Mst Shamima Khatun; Hiroyuki Kurata
Journal:  Cells       Date:  2019-01-28       Impact factor: 6.600

10.  Structure, Biosynthesis, and Biological Activity of Succinylated Forms of Bacteriocin BacSp222.

Authors:  Justyna Śmiałek; Michał Nowakowski; Monika Bzowska; Oliwia Bocheńska; Agnieszka Wlizło; Andrzej Kozik; Grzegorz Dubin; Paweł Mak
Journal:  Int J Mol Sci       Date:  2021-06-10       Impact factor: 5.923

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