Evidence map›Paper›PMID 38641087›Full record

ReviewBiochimica et biophysica acta. Proteins and proteomics2024

Chemical proteomics approaches for protein post-translational modification studies.

Nan Zhang, Jinghua Wu, Qingfei Zheng

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta. Proteins and proteomics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Biocompatible Chemistry: A Plug-and-Play Toolbox for Chemical Biology Research.Chembiochem : a European journal of chemical biology · 2025
    Review
  8. Review
  9. Article
  10. Review
  11. The Role of E3 Ubiquitin Ligase GeneInternational journal of molecular sciences · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. 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

3 authors.

Nan ZhangDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, OH 43210, United States; Center for Cancer Metabolism, James Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, United States.
Jinghua WuDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, OH 43210, United States; Center for Cancer Metabolism, James Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, United States.
Qingfei ZhengDepartment of Radiation Oncology, College of Medicine, The Ohio State University, Columbus, OH 43210, United States; Center for Cancer Metabolism, James Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, United States; Department of Biological Chemistry and Pharmacology, College of Medicine, The Ohio State University, Columbus, OH 43210, United States. Electronic address: Qingfei.Zheng@osumc.edu.

Funding

Development of a Chemical Biology Toolbox to Investigate Histone MonoaminylationR35GM150676 · NIGMS · PURDUE UNIVERSITY · PI Qingfei Zheng · 2023 to 2026
$1.6M
NIGMS NIH HHS R35 GM150676
6 · The paper itself

Abstract

The diversity and dynamics of proteins play essential roles in maintaining the basic constructions and functions of cells. The abundance of functional proteins is regulated by the transcription and translation processes, while the alternative splicing enables the same gene to generate distinct protein isoforms of different lengths. Beyond the transcriptional and translational regulations, post-translational modifications (PTMs) are able to further expand the diversity and functional scope of proteins. PTMs have been shown to make significant changes in the surface charges, structures, activation states, and interactome of proteins. Due to the functional complexity, highly dynamic nature, and low presence percentage, the study of protein PTMs remains challenging. Here we summarize and discuss the major chemical biology tools and chemical proteomics approaches to enrich and investigate the protein PTM of interest.

Indexed as

Protein Processing, Post-TranslationalProteomicsAnimalsHumansProteinsProteinsBioorthogonal chemistryChemical biology toolChemical proteomicsProtein post-translational modificationSignaling transduction

Identifiers

PMID38641087
PMCPMC13073518

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.