Evidence map›Paper›PMID 36245142›Full record

ArticleThe journal of physical chemistry. B2022

Variable Regions of p53 Isoforms Allosterically Hard Code DNA Interaction.

Isabel Armour-Garb, In Sub Mark Han, Benjamin S Cowan, Kelly M Thayer

Open access · bronzeAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

4 authors at 1 institution in 1 country.

Isabel Armour-Garb
Benjamin S Cowan
Wesleyan University · US

Funding

Ensemble Networks for Allosteric Drug DesignR15GM128102 · NIGMS · WESLEYAN UNIVERSITY · PI THAYER, KELLY MARIE · 2018 to 2021
$976k
NIGMS NIH HHS R15 GM128102
6 · The paper itself

Abstract

Allosteric regulation of protein activity pervades biology as the "second secret of life." We have been examining the allosteric regulation and mutant reactivation of the tumor suppressor protein p53. We have found that generalizing the definition of allosteric effector to include entire proteins and expanding the meaning of binding site to include the interface of a transcription factor with its DNA to be useful in understanding the modulation of protein activity. Here, we cast the variable regions of p53 isoforms as allosteric regulators of p53 interactions with its consensus DNA. We implemented molecular dynamics simulations and our lab's new techniques of molecular dynamics (MD) sectors and MD-Markov state models to investigate the effects of nine naturally occurring splice variant isoforms of p53. We find that all of the isoforms differ from wild type in their dynamic properties and how they interact with the DNA. We consider the implications of these findings on allostery and cancer treatment.

Indexed as

Molecular Dynamics SimulationTumor Suppressor Protein p53Allosteric RegulationDNAProtein BindingProtein IsoformsTranscription FactorsDNAProtein IsoformsTranscription FactorsTumor Suppressor Protein p53

Identifiers

PMID36245142
PMCPMC9623584
OpenAlexW4306382206

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.