Evidence map›Paper›PMID 27936491›Full record

ArticleProteins2017

Intrinsic α helix propensities compact hydrodynamic radii in intrinsically disordered proteins.

Lance R English, Erin C Tilton, Benjamin J Ricard, Steven T Whitten

Abstract read
In one paragraph

Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.5field-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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025
    Review
  2. Article
  3. Article
  4. ParSe 2.0: A web tool to identify drivers of protein phase separation at the proteome level.Protein science : a publication of the Protein Society · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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 1 institution in 1 country.

Lance R EnglishDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas.
Erin C TiltonDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas.
Benjamin J RicardDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas.
Steven T WhittenDepartment of Chemistry and Biochemistry, Texas State University, San Marcos, Texas.
Texas State University · US

Funding

South Texas Doctoral Bridge ProgramR25GM102783 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI OYAJOBI, BABATUNDE OLUKAYODE, WHITTEN, STEVEN T · 2013 to 2022
$3.1M
Quantitative Description of Phosphorylation Effects on Disordered Protein StructureR15GM115603 · NIGMS · TEXAS STATE UNIVERSITY · PI WHITTEN, STEVEN T · 2015 to 2015
$336k
NIGMS NIH HHS R15 GM115603NIGMS NIH HHS R25 GM102783
6 · The paper itself

Abstract

Proteins that lack tertiary stability under normal conditions, known as intrinsically disordered, exhibit a wide range of biological activities. Molecular descriptions for the biology of intrinsically disordered proteins (IDPs) consequently rely on disordered structural models, which in turn require experiments that assess the origins to structural features observed. For example, while hydrodynamic size is mostly insensitive to sequence composition in chemically denatured proteins, IDPs show strong sequence-specific effects in the hydrodynamic radius (R

Indexed as

HumansHydrodynamicsIntrinsically Disordered ProteinsProtein Conformation, alpha-HelicalProtein DomainsProtein FoldingProtein PrecursorsProto-Oncogene Proteins c-mdm2Static ElectricityThermodynamicsThymosinIntrinsically Disordered ProteinsMDM2 protein, humanProtein Precursorsprothymosin alphaProto-Oncogene Proteins c-mdm2Thymosindynamic light scatteringnet chargepolyproline type IIsimulationsize exclusion chromatography

Identifiers

PMID27936491
PMCPMC5258847
OpenAlexW2561683712

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.