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Cited by 317

The DOI matches its Crossref record; 99 of the 99 references it cites were found in a registry or an index.

Mechanisms and Dynamics of Protein Acetylation in Mitochondria

Open access
Baeza, Josue, Smallegan, Michael J., Denu, John M.·2016·Trends in Biochemical Sciences

Abstract

Reversible protein acetylation is a major regulatory mechanism for controlling protein function. Through genetic manipulations, dietary perturbations, and new proteomic technologies, the diverse functions of protein acetylation are coming into focus. Protein acetylation in mitochondria has taken center stage, revealing that 63% of mitochondrially localized proteins contain lysine acetylation sites. Here we summarize the field, and discuss salient topics that cover spurious versus targeted acetylation, the role of SIRT3 deacetylation, nonenzymatic acetylation, and molecular models for regulatory acetylations that display high and low stoichiometry.

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Crossref · 10.1016/j.tibs.2015.12.006

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Metadata

Authors
Baeza, J., Smallegan, M. J., & Denu, J. M.
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2016-03
Volume
41
Issue
3
Pages
231-244
ISSN
0968-0004 (ISSN-L)
OpenAlex
W2250423544
Cited by
317
References
99
FWCI
3.11
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Mechanisms and Dynamics of Protein Acetylation in Mitochondria. https://app.cochat.ai/papers/10.1016/j.tibs.2015.12.006
The paper
Baeza, J., Smallegan, M. J., & Denu, J. M. (2016). Mechanisms and Dynamics of Protein Acetylation in Mitochondria. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2015.12.006

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.