Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation (Q64064307)

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27 April 2020

title

Analysis of human acetylation stoichiometry defines mechanistic constraints on protein regulation (English)

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27 April 2020

1

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27 April 2020

Rajat Gupta

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27 April 2020

David Lyon

4

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27 April 2020

Takeo Narita

5

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27 April 2020

Chunaram Choudhary

7

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27 April 2020

author name string

Linda Baldus

3

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27 April 2020

Michael Lammers

6

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27 April 2020

Brian T Weinert

8

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27 April 2020

language of work or name

English

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publication date

5 March 2019

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27 April 2020

published in

Nature Communications

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27 April 2020

volume

10

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27 April 2020

issue

1

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27 April 2020

page(s)

1055

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Creative Commons Attribution 4.0 International

27 April 2020

copyright license

start time

5 March 2019

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

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Substrate and functional diversity of lysine acetylation revealed by a proteomics survey

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Lysine acetylation targets protein complexes and co-regulates major cellular functions

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Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns

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Widespread and enzyme-independent Nε-acetylation and Nε-succinylation of proteins in the chemical conditions of the mitochondrial matrix

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Acetylation dynamics and stoichiometry in Saccharomyces cerevisiae

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7 January 2021

Analysis of acetylation stoichiometry suggests that SIRT3 repairs nonenzymatic acetylation lesions

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7 January 2021

Accurate Quantification of Site-specific Acetylation Stoichiometry Reveals the Impact of Sirtuin Deacetylase CobB on the E. coli Acetylome

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Temporal Regulation of the Bacillus subtilis Acetylome and Evidence for a Role of MreB Acetylation in Cell Wall Growth.

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Avoiding abundance bias in the functional annotation of posttranslationally modified proteins

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Deep, Quantitative Coverage of the Lysine Acetylome Using Novel Anti-acetyl-lysine Antibodies and an Optimized Proteomic Workflow

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Time-Resolved Analysis Reveals Rapid Dynamics and Broad Scope of the CBP/p300 Acetylome

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An Optimized Shotgun Strategy for the Rapid Generation of Comprehensive Human Proteomes

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A subcellular map of the human proteome

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Improved visualization of protein consensus sequences by iceLogo

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Proximal Cysteines that Enhance Lysine N-Acetylation of Cytosolic Proteins in Mice Are Less Conserved in Longer-Living Species

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7 January 2021

Discovery of protein acetylation patterns by deconvolution of peptide isomer mass spectra

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7 January 2021

Global and specific responses of the histone acetylome to systematic perturbation

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7 January 2021

Site-Specific Identification of Lysine Acetylation Stoichiometries in Mammalian Cells

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Measurement of acetylation turnover at distinct lysines in human histones identifies long-lived acetylation sites.

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7 January 2021

Acetylation site specificities of lysine deacetylase inhibitors in human cells

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7 January 2021

Protein lysine acetylation by p300/CBP

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Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A)

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7 January 2021

DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylation-driven ubiquitination

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Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex

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7 January 2021

Insulin and mTOR Pathway Regulate HDAC3-Mediated Deacetylation and Activation of PGK1

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The transcriptional co-activator PCAF regulates cdk2 activity

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EB1 acetylation by P300/CBP-associated factor (PCAF) ensures accurate kinetochore-microtubule interactions in mitosis.

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A Proteomic Approach to Analyze the Aspirin-mediated Lysine Acetylome

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Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress

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PubMed

https://pubmed.ncbi.nlm.nih.gov/30837475

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1038/S41467-019-09024-0

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30837475%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

27 April 2020

ADS bibcode

2019NatCo..10.1055H

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0 references

1 reference

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27 April 2020

PubMed publication ID

30837475

1 reference