Evidence map›Paper›PMID 35230102›Full record

ArticleJournal of the American Chemical Society2022

Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.

Dustin T King, Jesús E Serrano-Negrón, Yanping Zhu, Christopher L Moore, Matthew D Shoulders, Leonard J Foster, David J Vocadlo

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  7. Article
  8. Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024
    Article
  9. Review
  10. Article
  11. Stability-based approaches in chemoproteomics.Expert reviews in molecular medicine · 2024
    Review
  12. OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024
    Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
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

7 authors at 3 institutions in 2 countries.

Dustin T KingDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.ORCID 0000-0003-1775-2885
Jesús E Serrano-NegrónDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.ORCID 0000-0001-9666-3797
Yanping ZhuDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
Christopher L MooreDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.
Matthew D ShouldersDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States.ORCID 0000-0002-6511-3431
Leonard J FosterMichael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada.ORCID 0000-0001-8551-4817
David J VocadloDepartment of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.ORCID 0000-0001-6897-5558
Simon Fraser University · CAMassachusetts Institute of Technology · USUniversity of British Columbia · CA

Funding

Leveraging Next-Generation Directed Evolution Platforms and Chemical Control of Proteostasis to Deliver Robust Biotechnologies and Illuminate Roles of Chaperone Networks in Protein EvolutionR35GM136354 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHOULDERS, MATTHEW DONALD · 2020 to 2024
$2.1M
CIHR PJT-148732CIHR PJT-156202NIGMS NIH HHS R35 GM136354
6 · The paper itself

Abstract

Posttranslational modifications alter the biophysical properties of proteins and thereby influence cellular physiology. One emerging manner by which such modifications regulate protein functions is through their ability to perturb protein stability. Despite the increasing interest in this phenomenon, there are few methods that enable global interrogation of the biophysical effects of posttranslational modifications on the proteome. Here, we describe an unbiased proteome-wide approach to explore the influence of protein modifications on the thermodynamic stability of thousands of proteins in parallel. We apply this profiling strategy to study the effects of O-linked

Indexed as

AcetylglucosamineProteomeAnimalsMammalsProtein Processing, Post-TranslationalProteomicsAcetylglucosamineProteome

Identifiers

PMID35230102
PMCPMC8969899
OpenAlexW4214615178

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.