Evidence map›Paper›PMID 33798408›Full record

ReviewMolecular cell2021

Discovering the landscape of protein modifications.

E Keith Keenan, Derek K Zachman, Matthew D Hirschey

Abstract readReview
In one paragraph

Review in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
–field-weighted citation impact
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

86 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. A RAC1 SUMOylation switch governs breast cancer metastasis.Signal transduction and targeted therapy · 2026
    Article
  6. Review
  7. Article
  8. Review
  9. Reductive Methylation: An Alternative to Lysine → Arginine Mutagenesis.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Post-Translational Regulation of CD8Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  18. UnderstandingJournal of the American Society for Mass Spectrometry · 2026
    Article
  19. Article
  20. Review

26 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

3 authors.

E Keith KeenanDuke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Pharmacology & Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.
Derek K ZachmanDuke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA.
Matthew D HirscheyDuke Molecular Physiology Institute and Sarah W. Stedman Nutrition and Metabolism Center, Duke University Medical Center, Durham, NC 27701, USA; Department of Pharmacology & Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA; Division of Endocrinology, Metabolism, & Nutrition, Department of Medicine, Duke University Medical Center, Durham, NC 27710, USA. Electronic address: matthew.hirschey@duke.edu.

Funding

Studies on the Mechanisms by which SIRT5 Regulates Aging and DiseaseR01AG045351 · NIA · DUKE UNIVERSITY · PI HIRSCHEY, MATTHEW D · 2014 to 2023
$4.4M
Stimulating Access to Research in Residency (StARR) - NIAIDR38AI140297 · NIAID · DUKE UNIVERSITY · PI Rachel G Greenberg, David H. Harpole · 2018 to 2026
$2.4M
Post-Translational and Epigenetic Control of Branched-Chain Amino Acid MetabolismR01DK115568 · NIDDK · DUKE UNIVERSITY · PI HIRSCHEY, MATTHEW D · 2018 to 2021
$1.9M
Studies on the impact of acetyl-cysteine on metabolismR21AG080334 · NIA · DUKE UNIVERSITY · PI HIRSCHEY, MATTHEW D · 2023 to 2024
$429k
NIAID NIH HHS R38 AI140297NIA NIH HHS R01 AG045351NIA NIH HHS R21 AG080334NIDDK NIH HHS R01 DK115568
6 · The paper itself

Abstract

Protein modifications modulate nearly every aspect of cell biology in organisms, ranging from Archaea to Eukaryotes. The earliest evidence of covalent protein modifications was found in the early 20th century by studying the amino acid composition of proteins by chemical hydrolysis. These discoveries challenged what defined a canonical amino acid. The advent and rapid adoption of mass-spectrometry-based proteomics in the latter part of the 20th century enabled a veritable explosion in the number of known protein modifications, with more than 500 discrete modifications counted today. Now, new computational tools in data science, machine learning, and artificial intelligence are poised to allow researchers to make significant progress in discovering new protein modifications and determining their function. In this review, we take an opportunity to revisit the historical discovery of key post-translational modifications, quantify the current landscape of covalent protein adducts, and assess the role that new computational tools will play in the future of this field.

Indexed as

Protein Processing, Post-TranslationalAnimalsArtificial IntelligenceComputational BiologyDatabases, ProteinHumansProtein ConformationProteinsProteomicsStructure-Activity RelationshipProteinsamino acidmetabolismpost-translational modificationsprotein acylationprotein modifications

Identifiers

PMID33798408
PMCPMC8106652

What OpenQuestion holds

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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.