Evidence map›Paper›PMID 28605189›Full record

ArticleThe journal of physical chemistry. B2017

Cosolutes, Crowding, and Protein Folding Kinetics.

Annelise H Gorensek-Benitez, Austin E Smith, Samantha S Stadmiller, Gerardo M Perez Goncalves, Gary J Pielak

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Enthalpic stabilization of an SH3 domain by DProtein science : a publication of the Protein Society · 2018
    Article
  14. Large cosolutes, small cosolutes, and dihydrofolate reductase activity.Protein science : a publication of the Protein Society · 2017
    Article
  15. 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

5 authors at 1 institution in 1 country.

Annelise H Gorensek-BenitezDepartment of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Austin E SmithDepartment of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Samantha S StadmillerDepartment of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Gerardo M Perez GoncalvesDepartment of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina , Chapel Hill, North Carolina 27599, United States.
Gary J PielakDepartment of Chemistry, ‡Department of Biochemistry and Biophysics, and §Lineberger Comprehensive Cancer Center, University of North Carolina , Chapel Hill, North Carolina 27599, United States.ORCID 0000-0001-6307-542X
University of North Carolina at Chapel Hill · US

Funding

MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
NIGMS NIH HHS T32 GM008570
6 · The paper itself

Abstract

Long accepted as the most important interaction, recent work shows that steric repulsions alone cannot explain the effects of macromolecular cosolutes on the equilibrium thermodynamics of protein stability. Instead, chemical interactions have been shown to modulate, and even dominate, crowding-induced steric repulsions. Here, we use

Indexed as

Protein FoldingAnimalsDrosophilaDrosophila ProteinsKineticsMacromolecular SubstancesMethylaminesMuramidaseProtein Stabilitysrc Homology DomainsSucroseThermodynamicsUreaViscositydrk protein, DrosophilaDrosophila ProteinsMacromolecular SubstancesMethylaminesMuramidaseSucrosetrimethylamineUrea

Identifiers

PMID28605189
PMCPMC5982521
OpenAlexW2626550761

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.