For Certain, SIRT4 Activities

Surinder Kumar; David B Lombard

doi:10.1016/j.tibs.2017.05.008

Back

Journal article

Peer reviewed

For Certain, SIRT4 Activities

Surinder Kumar and David B Lombard

Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.42(7), pp.499-501

2017-07

DOI: https://doi.org/10.1016/j.tibs.2017.05.008

PMCID: PMC5518788

PMID: 28587732

Abstract

Lysine

Mitochondrial Proteins

Sirtuins

Despite the fact that SIRT4 regulates important biological processes, its primary enzymatic activity has remained ambiguous. A recent study by Anderson, Huynh et al. has uncovered deacylase activities of SIRT4 towards newly described lysine modifications derived from reactive acyl-CoAs generated in leucine catabolism.

Metrics

8 Record Views

16 Times Cited - Web of Science

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Citation topics: 1 Clinical & Life Sciences; 1.264 Longevity; 1.264.1102 Resveratrol
Web Of Science research areas: Biochemistry & Molecular Biology
ESI research areas: Biology & Biochemistry

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

Source: InCites

Details

Title: For Certain, SIRT4 Activities
Creators: Surinder Kumar - University of Michigan–Ann Arbor
David B Lombard - University of Michigan–Ann Arbor
Publication Details: Trends in biochemical sciences (Amsterdam. Regular ed.), Vol.42(7), pp.499-501
Grant note: R21 AG053561 / NIA NIH HHS R01 GM101171 / NIGMS NIH HHS R01 HL114858 / NHLBI NIH HHS
Academic Unit: Miller School of Medicine; UMMG Department of Pathology; UMMG Dept of Pathology - Comparative Pathology
Language: English
Resource Type: Journal article
PMID: 28587732
PMCID: PMC5518788
Record Identifier: 991031725480802976