Evidence map›Paper›PMID 35786742›Full record

ReviewOrganic & biomolecular chemistry2022

Peptide and protein chemistry approaches to study the tumor suppressor protein p53.

Champak Chatterjee, Sumeet K Singh

Open access · greenAbstract readReview
In one paragraph

Review in Organic & biomolecular chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 1 institution in 1 country.

Champak ChatterjeeDepartment of Chemistry, University of Washington, Seattle, WA 98195, USA. sumeet19@uw.edu.ORCID 0000-0001-5772-4438
Sumeet K SinghDepartment of Chemistry, University of Washington, Seattle, WA 98195, USA. sumeet19@uw.edu.ORCID 0000-0003-4682-8789
University of Washington · US

Funding

Chemical Strategies to Investigate Gene Regulation By Histone SumoylationR01GM110430 · NIGMS · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK · 2014 to 2022
$2.5M
Structure and Mechanism of the SET1/COMPASS H3K4 Methyltransferase ComplexR01HD097408 · NICHD · UNIVERSITY OF WASHINGTON · PI CHATTERJEE, CHAMPAK, ZHENG, NING · 2020 to 2024
$1.9M
NICHD NIH HHS R01 HD097408NIGMS NIH HHS R01 GM110430
6 · The paper itself

Abstract

The tumor suppressor and master gene regulator protein p53 has been the subject of intense investigation for several decades due to its mutation in about half of all human cancers. However, mechanistic studies of p53 in cells are complicated by its many dynamic binding partners and heterogeneous post-translational modifications. The design of therapeutics that rescue p53 functions in cells requires a mechanistic understanding of its protein-protein interactions in specific protein complexes and identifying changes in p53 activity by diverse post-translational modifications. This review highlights the important roles that peptide and protein chemistry have played in biophysical and biochemical studies aimed at elucidating p53 regulation by several key binding partners. The design of various peptide inhibitors that rescue p53 function in cells and new opportunities in targeting p53-protein interactions are discussed. In addition, the review highlights the importance of a protein semisynthesis approach to comprehend the role of site-specific PTMs in p53 regulation.

Indexed as

NeoplasmsTumor Suppressor Protein p53HumansMutationPeptidesProtein Processing, Post-TranslationalPeptidesTumor Suppressor Protein p53

Identifiers

PMID35786742
PMCPMC10112546
OpenAlexW4283835631

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.