Evidence map›Paper›PMID 21151122›Full record

ArticleNature chemical biology2011

Identification of lysine succinylation as a new post-translational modification.

Zhihong Zhang, Minjia Tan, Zhongyu Xie, Lunzhi Dai, Yue Chen, Yingming Zhao

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 559 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
559citing papers in PubMed, 1 pooled it
9.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

559 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,021 citations in OpenAlex.

  1. Pooled it
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  3. Review
  4. Review
  5. Article
  6. Aspirin-Derived Salicyl-CoA Drives Histone Lysine Salicylation Regulated by CBP and SIRT2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  7. Review
  8. Article
  9. Article
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  12. Article
  13. Article
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  18. Stage-Specific H3K14 and H3K23 Succinylation Orchestrates Insect Metamorphosis and Oogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  19. Review
  20. Article

499 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Zhihong ZhangBen May Department for Cancer Research, The University of Chicago, Chicago, Illinois, USA.
Minjia Tan
Zhongyu Xie
Lunzhi Dai
Yue Chen
Yingming Zhao
University of Chicago · US

Funding

Global characterization of lysine acetylation in cancer by a proteomics approachR01CA126832 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI ZHAO, YINGMING · 2008 to 2012
$1.6M
NCI NIH HHS R01 CA126832
6 · The paper itself

Abstract

Of the 20 ribosomally coded amino acid residues, lysine is the most frequently post-translationally modified, which has important functional and regulatory consequences. Here we report the identification and verification of a previously unreported form of protein post-translational modification (PTM): lysine succinylation. The succinyllysine residue was initially identified by mass spectrometry and protein sequence alignment. The identified succinyllysine peptides derived from in vivo proteins were verified by western blot analysis, in vivo labeling with isotopic succinate, MS/MS and HPLC coelution of their synthetic counterparts. We further show that lysine succinylation is evolutionarily conserved and that this PTM responds to different physiological conditions. Our study also implies that succinyl-CoA might be a cofactor for lysine succinylation. Given the apparent high abundance of lysine succinylation and the significant structural changes induced by this PTM, it is expected that lysine succinylation has important cellular functions.

Indexed as

Protein Processing, Post-TranslationalAcyl Coenzyme AAmino Acid SequenceBlotting, WesternChromatography, High Pressure LiquidEscherichia coli ProteinsLysineMass SpectrometryMolecular Sequence DataPeptidesSequence AlignmentSuccinic AcidAcyl Coenzyme AEscherichia coli ProteinsLysinePeptidesSuccinic Acidsuccinyl-coenzyme A

Identifiers

PMID21151122
PMCPMC3065206
OpenAlexW1969899640

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.