Evidence map›Paper›PMID 23908237›Full record

ArticleScience (New York, N.Y.)2013

Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.

Raymond E Moellering, Benjamin F Cravatt

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.

0numbers the graph read from it
0cells of the map it votes in
127citing papers in PubMed
9.7field-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

127 citing papers in PubMed, 203 citations in OpenAlex.

  1. Article
  2. Reversible formation ofRSC chemical biology · 2026
    Article
  3. Article
  4. Review
  5. Expanding the Genetic Code with Lysine Aminoacylation.Journal of the American Chemical Society · 2026
    Article
  6. Article
  7. Acetate enhances neuronal plasticity and reduces ischemic brain injury by promoting tau protein lactylation.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2026
    Article
  8. The plant epigenome governed by nutrients and metabolism.Current opinion in plant biology · 2025
    Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. The chemical language of protein glycation.Nature chemical biology · 2025
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Immunometabolic Maladaptations to the Tumor Microenvironment.Cold Spring Harbor perspectives in medicine · 2024
    Review

67 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

2 authors at 1 institution in 1 country.

Raymond E MoelleringThe Skaggs Institute for Chemical Biology and Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA. rmoeller@scripps.edu
Benjamin F Cravatt
Scripps Research Institute · US

Funding

Chemical Approaches for Activity-Based ProteomicsR37CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2009 to 2018
$3.1M
CHEMICAL APPROACHES FOR ACTIVITY BASED PROTEOMICSR01CA087660 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F · 2000 to 2008
$2.8M
NCI NIH HHS CA087660NCI NIH HHS R01 CA087660NCI NIH HHS R37 CA087660
6 · The paper itself

Abstract

The posttranslational modification of proteins and their regulation by metabolites represent conserved mechanisms in biology. At the confluence of these two processes, we report that the primary glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) reacts with select lysine residues in proteins to form 3-phosphoglyceryl-lysine (pgK). This reaction, which does not require enzyme catalysis, but rather exploits the electrophilicity of 1,3-BPG, was found by proteomic profiling to be enriched on diverse classes of proteins and prominently in or around the active sites of glycolytic enzymes. pgK modifications inhibit glycolytic enzymes and, in cells exposed to high glucose, accumulate on these enzymes to create a potential feedback mechanism that contributes to the buildup and redirection of glycolytic intermediates to alternate biosynthetic pathways.

Indexed as

GlycolysisProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsBiomarkers, TumorCatalysisCell LineDiphosphoglyceric AcidsDNA-Binding ProteinsGlucoseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycerophosphatesHumansLysineMiceMolecular Sequence DataBiomarkers, TumorDiphosphoglyceric AcidsDNA-Binding ProteinsENO1 protein, humanGlucoseGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)glycerate 1,3-biphosphateGlycerophosphatesLysinePhosphopyruvate HydrataseProteinsTumor Suppressor Proteins

Identifiers

PMID23908237
PMCPMC4005992
OpenAlexW2022760167

What OpenQuestion holds

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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.