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Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of...

Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_1302961110

Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways

About this item

Full title

Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2013-04, Vol.110 (16), p.6601-6606

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Large-scale proteomic approaches have identified numerous mitochondrial acetylated proteins; however in most cases, their regulation by acetyltransferases and deacetylases remains unclear. Sirtuin 3 (SIRT3) is an NAD ⁺-dependent mitochondrial protein deacetylase that has been shown to regulate a limited number of enzymes in key metabolic pathways....

Alternative Titles

Full title

Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_primary_10_1073_pnas_1302961110

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_1302961110

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1302961110

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