Evidence map›Paper›PMID 22540015›Full record

ArticlePloS one2012

The proline rich homeodomain protein PRH/Hhex forms stable oligomers that are highly resistant to denaturation.

Anshuman Shukla, Nicholas M Burton, Padma-Sheela Jayaraman, Kevin Gaston

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. 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

4 authors at 2 institutions in 1 country.

Anshuman ShuklaInstitute for Biomedical Research, Birmingham University Medical School, Edgbaston, Birmingham, United Kingdom.
Nicholas M Burton
Padma-Sheela Jayaraman
Kevin Gaston
University of Birmingham · GBUniversity of Bristol · GB

Funding

Wellcome TrustWellcome Trust 076527
6 · The paper itself

Abstract

backgroundMany transcription factors control gene expression by binding to specific DNA sequences at or near the genes that they regulate. However, some transcription factors play more global roles in the control of gene expression by altering the architecture of sections of chromatin or even the whole genome. The ability to form oligomeric protein assemblies allows many of these proteins to manipulate extensive segments of DNA or chromatin via the formation of structures such as DNA loops or protein-DNA fibres. PRINCIPAL

findingsHere we show that the proline rich homeodomain protein PRH/Hhex forms predominantly octameric and/or hexadecameric species in solution as well as larger assemblies. We show that these assemblies are highly stable resisting denaturation by temperature and chemical denaturants.

conclusionThese data indicate that PRH is functionally and structurally related to the Lrp/AsnC family of proteins, a group of proteins that are known to act globally to control gene expression in bacteria and archaea.

Indexed as

Circular DichroismGuanidinesHomeodomain ProteinsProtein DenaturationProtein MultimerizationProtein Structure, SecondaryTemperatureThiocyanatesTranscription FactorsGuanidinesguanidine thiocyanateHHEX protein, humanHomeodomain ProteinsThiocyanatesTranscription Factors

Identifiers

PMID22540015
PMCPMC3335068
OpenAlexW2065148476

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.