Evidence map›Paper›PMID 26933738›Full record

ReviewCell chemical biology2016

Chemical Methods for Encoding and Decoding of Posttranslational Modifications.

Kelly N Chuh, Anna R Batt, Matthew R Pratt

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Review
  6. Orthogonal Site-Specific Dual Bioconjugation of Aryl and Alkyl Thiols.Journal of the American Chemical Society · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
    Article
  13. Review
  14. Review
  15. Article
  16. [Precise identification ofSe pu = Chinese journal of chromatography · 2021
    Article
  17. Review
  18. Article
  19. Review
  20. ProteinOpen biology · 2021
    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

3 authors at 1 institution in 1 country.

Kelly N ChuhDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Anna R BattDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA; Department of Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089, USA. Electronic address: matthew.pratt@usc.edu.
University of Southern California · US

Funding

Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024
$3.1M
NIGMS NIH HHS R01 GM114537NIGMS NIH HHS R01GM114537
6 · The paper itself

Abstract

A large array of posttranslational modifications can dramatically change the properties of proteins and influence different aspects of their biological function such as enzymatic activity, binding interactions, and proteostasis. Despite the significant knowledge that has been gained about the function of posttranslational modifications using traditional biological techniques, the analysis of the site-specific effects of a particular modification, the identification of the full complement of modified proteins in the proteome, and the detection of new types of modifications remains challenging. Over the years, chemical methods have contributed significantly in both of these areas of research. This review highlights several posttranslational modifications where chemistry-based approaches have made significant contributions to our ability to both prepare homogeneously modified proteins and identify and characterize particular modifications in complex biological settings. As the number and chemical diversity of documented posttranslational modifications continues to rise, we believe that chemical strategies will be essential to advance the field in years to come.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsBiochemistryChemistry Techniques, AnalyticalChemistry Techniques, SyntheticGlycosylationHumansLipidsMethylationPhosphorylationProteinsProteomicsLipidsProteins

Identifiers

PMID26933738
PMCPMC4779183
OpenAlexW2267244979

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.