Quantitative Acetylomics Reveals Substrates of Lysine Acetyltransferase GCN5 in Adult and Aging <i>Drosophila</i>-Reference-Cited by-同舟云学术

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Quantitative Acetylomics Reveals Substrates of Lysine Acetyltransferase GCN5 in Adult and Aging Drosophila

Published:2023-08-07 Issue:9 Volume:22 Page:2909-2924
ISSN:1535-3893
Container-title:Journal of Proteome Research
language:en
Short-container-title:J. Proteome Res.

Author:

Li Jingshu¹²^ORCID,Cao Ye¹²,Yang Yun¹²,Ma Huanhuan¹²,Zhao Jing¹²,Zhang Yaoyang¹³^ORCID,Liu Nan¹³^ORCID

Affiliation:

1. Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 100 Hai Ke Rd., Pudong, Shanghai 201210, China

2. University of Chinese Academy of Sciences, Beijing 100049, China

3. Shanghai Key Laboratory of Aging Studies, 100 Hai Ke Rd., Pudong, Shanghai 201210, China

Funder

Natural Science Foundation of Shanghai

National Natural Science Foundation of China

Shanghai Municipal Science and Technology Major Project

Shanghai Key Laboratory of Aging Studies, Chinese Academy of Sciences

Publisher

American Chemical Society (ACS)

Subject

General Chemistry,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jproteome.3c00247

Reference90 articles.

1. Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance

2. An acetylation switch controls TDP-43 function and aggregation propensity

3. Uric acid and evolution

4. Histone acetylation: a switch between repressive and permissive chromatin

5. Combinatorial patterns of histone acetylations and methylations in the human genome

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