Evidence map›Paper›PMID 22902405›Full record

ArticleCell reports2012

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

Alicia Lundby, Kasper Lage, Brian T Weinert, Dorte B Bekker-Jensen, Anna Secher, Tine Skovgaard, Christian D Kelstrup, Anatoliy Dmytriyev, Chunaram Choudhary, Carsten Lundby and 1 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 329 papers.

0numbers the graph read from it
0cells of the map it votes in
329citing papers in PubMed
22.4field-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

329 citing papers in PubMed, 539 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. CLASPP: A unified model for predicting post-translational modifications.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  12. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. NADMetabolites · 2025
    Article
  18. Article
  19. Review
  20. Article

269 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

11 authors at 5 institutions in 3 countries.

Alicia LundbyNovo Nordisk Foundation Center for Protein Research, Department for Proteomics, Faculty of Health Sciences, University of Copenhagen, Denmark.
Kasper Lage
Brian T Weinert
Dorte B Bekker-Jensen
Anna Secher
Tine Skovgaard
Christian D Kelstrup
Anatoliy Dmytriyev
Chunaram Choudhary
Carsten Lundby
Jesper V Olsen
University of Copenhagen · DKNovo Nordisk Foundation · DKBroad Institute · USMassachusetts General Hospital · USUniversity of Zurich · CH

Funding

THE DROSOPHILA GENETICS AND RNAI CORE (THE FLY CORE)P01HD068250 · NICHD · MASSACHUSETTS GENERAL HOSPITAL · PI CHUNG, WENDY K, DONAHOE, PATRICIA K · 2011 to 2022
$17.1M
NICHD NIH HHS P01 HD068250
6 · The paper itself

Abstract

Lysine acetylation is a major posttranslational modification involved in a broad array of physiological functions. Here, we provide an organ-wide map of lysine acetylation sites from 16 rat tissues analyzed by high-resolution tandem mass spectrometry. We quantify 15,474 modification sites on 4,541 proteins and provide the data set as a web-based database. We demonstrate that lysine acetylation displays site-specific sequence motifs that diverge between cellular compartments, with a significant fraction of nuclear sites conforming to the consensus motifs G-AcK and AcK-P. Our data set reveals that the subcellular acetylation distribution is tissue-type dependent and that acetylation targets tissue-specific pathways involved in fundamental physiological processes. We compare lysine acetylation patterns for rat as well as human skeletal muscle biopsies and demonstrate its general involvement in muscle contraction. Furthermore, we illustrate that acetylation of fructose-bisphosphate aldolase and glycerol-3-phosphate dehydrogenase serves as a cellular mechanism to switch off enzymatic activity.

Indexed as

AcetylationAmino Acid MotifsAnimalsHumansLysineOrgan SpecificityProtein Processing, Post-TranslationalProteomeProteomicsRatsRats, Sprague-DawleyLysineProteome

Identifiers

PMID22902405
PMCPMC4103158
OpenAlexW2101065953

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.