Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Lysine succinylation and lysine malonylation in histones.

Molecular & cellular proteomics : MCP - 1 May 2012

Xie Zhongyu, Dai Junbiao, Dai Lunzhi, Tan Minjia, Cheng Zhongyi, Wu Yeming, Boeke Jef D, Zhao Yingming

Abstract excerpt

Histone protein post-translational modifications (PTMs) are significant for gene expression and DNA repair. Here we report the identification and validation of a new type of PTM in histones, lysine succinylation. The identified lysine succinylated histone peptides were verified by MS/MS of synthe...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Conserved Sequence
Share to Drosophila
Share to Histones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lysine

Share to Peptide Fragments

Share to Protein Processing, Post-Translational

Share to Succinates

Share to Tandem Mass Spectrometry

Source

Open in PubMed Open full text

Identifiers

PMID: 22389435
DOI: 10.1074/mcp.M111.015875
PMCID: PMC3418837

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22389435-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Lysine succinylation and lysine malonylation in histones.PMID 22389435Read ↗

Lysine succinylation, the metabolic bridge between cancer and immunitySemantic proximity Read ↗

Protein post-translational modification by lysine succinylation: Biochemistry, biological implications, and therapeutic opportunitiesSemantic proximity Read ↗

Proteomic Quantification of Lysine Acetylation and Succinylation Profile Alterations in Lung Adenocarcinomas of Non-Smoking FemalesSemantic proximity Read ↗

Succinylation and redox status in cancer cellsSemantic proximity Read ↗

Dysregulation of protein succinylation and disease developmentSemantic proximity Read ↗

Function and mechanism of histone β-hydroxybutyrylation in health and diseaseSemantic proximity Read ↗

Post-translational lysine ac(et)ylation in health, ageing and diseaseSemantic proximity Read ↗

Global proteomic analyses of lysine acetylation, malonylation, succinylation, and crotonylation in human sperm reveal their involvement in male fertilitySemantic proximity Read ↗

Identification of Lysine Succinylation Substrates and the Succinylation Regulatory Enzyme CobB in Escherichia coliSemantic proximity Read ↗

Function and mechanism of lysine crotonylation in health and diseaseSemantic proximity Read ↗

Biotinylation is a natural, albeit rare, modification of human histonesSemantic proximity Read ↗

Live-Cell Epigenome Manipulation by Synthetic Histone Acylation Catalyst SystemSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.