Evidence map›Paper›PMID 30525611›Full record

ArticleThe journal of physical chemistry. B2019

Solution Ensemble of the C-Terminal Domain from the Transcription Factor Pdx1 Resembles an Excluded Volume Polymer.

Erik C Cook, Debashish Sahu, Monique Bastidas, Scott A Showalter

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  4. Article
  5. Chemical reviews · 2022
    Review
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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.

Erik C Cook
Debashish Sahu
Monique Bastidas
Scott A ShowalterORCID 0000-0001-5179-032X
Pennsylvania State University · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Biophysical Characterization of PDX1 interactions with DNA and other transcriptioF31GM101936 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI BASTIDAS, MONIQUE · 2012 to 2014
$95k
NIGMS NIH HHS F31 GM101936NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

The pancreatic and duodenal homeobox 1 (Pdx1) is an essential pancreatic transcription factor. The C-terminal intrinsically disordered domain of Pdx1 (Pdx1-C) has a heavily biased amino acid composition; most notably, 18 of 83 residues are proline, including a hexaproline cluster near the middle of the chain. For these reasons, Pdx1-C is an attractive target for structure characterization, given the availability of suitable methods. To determine the solution ensembles of disordered proteins, we have developed a suite of

Indexed as

Protein DomainsHomeodomain ProteinsHumansNuclear Magnetic Resonance, BiomolecularPolymersSolutionsTrans-ActivatorsHomeodomain Proteinspancreatic and duodenal homeobox 1 proteinPolymersSolutionsTrans-Activators

Identifiers

PMID30525611
PMCPMC7874520
OpenAlexW2904119627

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.