Evidence map›Paper›PMID 34786438›Full record

ArticleBio-protocol2021

Urea Denaturation, Zinc Binding, and DNA Binding Assays of Mutant p53 DNA-binding Domains and Full-length Proteins.

Jeung-Hoi Ha, Xin Yu, Darren R Carpizo, Stewart N Loh

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bio-protocol, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Jeung-Hoi HaDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, United States.
Xin YuDepartment of Surgery, Rutgers Cancer Institute of New Jersey, Rutgers Robert Wood Johnson Medical School, New Brunswick, United States.
Darren R CarpizoDepartment of Surgery, University of Rochester School of Medicine and Dentistry and Wilmot Cancer Center, Rochester, United States.
Stewart N LohDepartment of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, United States.
SUNY Upstate Medical University · USUniversity of Rochester · US

Funding

Development of Zinc Metallochaperones as Mutant p53 Targeted Anti-cancerDrugsR01CA200800 · NCI · UNIVERSITY OF ROCHESTER · PI CARPIZO, DARREN RICHARD · 2016 to 2020
$1.9M
NCI NIH HHS R01 CA200800
6 · The paper itself

Abstract

In the cell, the thermodynamic stability of a protein - and hence its biological activity - can change dramatically as a result of perturbations in its amino acid sequence and the concentration of stabilizing ligands. This interplay is particularly evident in zinc-binding transcription factors such as the p53 tumor suppressor, whose DNA-binding activity can critically depend on levels of intracellular zinc as well as point mutations that alter either metal binding or folding stability. Separate protocols exist for determining a protein's metal affinity and its folding free energy. These properties, however, are intimately connected, and a technique is needed to integrate these measurements. Our protocols employ common non-fluorescent and fluorescent zinc chelators to control and report on free Zn

Indexed as

CancerMetal bindingProtein foldingProtein stabilityTranscription factorTumor suppressorZinc fingerZinc metallochaperone

Identifiers

PMID34786438
PMCPMC8558834
OpenAlexW3206762536

What OpenQuestion holds

Textmetadata
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.