Evidence map›Paper›PMID 38942948›Full record

ReviewNature chemical biology2025

The chemical language of protein glycation.

Meghan S Martin, Jeremiah W Jacob-Dolan, Vo Tri Tin Pham, Nicole M Sjoblom, Rebecca A Scheck

Abstract readReview
In one paragraph

Review in Nature chemical biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Non-Enzymatic MGO-Glycation of SRSF2 Drives RNA Mis-Splicing.Journal of the American Chemical Society · 2026
    Article
  11. Article
  12. Article
  13. Discovery of Glycation-Derived Cross-links at Arginine.Journal of the American Chemical Society · 2026
    Article
  14. Review
  15. Article
  16. Review
  17. A Chemical Mechanistic Path Leads the Way to Cellular Argpyrimidine.Journal of the American Chemical Society · 2025
    Article
  18. Article
  19. Article
  20. Article
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

5 authors.

Meghan S MartinDepartment of Chemistry, Tufts University, Medford, MA, USA.ORCID 0009-0006-9688-1309
Jeremiah W Jacob-DolanDepartment of Chemistry, Tufts University, Medford, MA, USA.ORCID 0000-0003-3686-6546
Vo Tri Tin PhamDepartment of Chemistry, Tufts University, Medford, MA, USA.ORCID 0009-0009-2656-0704
Nicole M SjoblomDepartment of Chemistry, Tufts University, Medford, MA, USA.
Rebecca A ScheckDepartment of Chemistry, Tufts University, Medford, MA, USA. rebecca.scheck@tufts.edu.ORCID 0000-0003-0916-0572

Funding

The Chemistry and Biology of Protein GlycationR01GM132422 · NIGMS · TUFTS UNIVERSITY MEDFORD · PI SCHECK, REBECCA · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM132422U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R01GM132422
6 · The paper itself

Abstract

Glycation is a non-enzymatic post-translational modification (PTM) that is correlated with many diseases, including diabetes, cancer and age-related disorders. Although recent work points to the importance of glycation as a functional PTM, it remains an open question whether glycation has a causal role in cellular signaling and/or disease development. In this Review, we contextualize glycation as a specific mechanism of carbon stress and consolidate what is known about advanced glycation end-product (AGE) structures and mechanisms. We highlight the current understanding of glycation as a PTM, focusing on mechanisms for installing, removing or recognizing AGEs. Finally, we discuss challenges that have hampered a more complete understanding of the biological consequences of glycation. The development of tools for predicting, modulating, mimicking or capturing glycation will be essential for interpreting a post-translational glycation network. Therefore, continued insights into the chemistry of glycation will be necessary to advance understanding of glycation biology.

Indexed as

Glycation End Products, AdvancedProteinsAnimalsGlycosylationHumansProtein Processing, Post-TranslationalGlycation End Products, AdvancedProteins

Identifiers

PMID38942948
PMCPMC12020258

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Registered trials

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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.