Evidence map›Paper›PMID 18172203›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Origins of barriers and barrierless folding in BBL.

Samuel S Cho, Patrick Weinkam, Peter G Wolynes

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

47 citing papers in PubMed, 97 citations in OpenAlex.

  1. Article
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  3. Article
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  6. Article
  7. Review
  8. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  9. Review
  10. Article
  11. Fast-folding proteins under stress.Cellular and molecular life sciences : CMLS · 2015
    Review
  12. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  13. Dodine as a protein denaturant: the best of two worlds?The journal of physical chemistry. B · 2013
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Folding without charges.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  20. Single-molecule observation of helix staggering, sliding, and coiled coil misfolding.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

3 authors at 1 institution in 1 country.

Samuel S ChoCenter for Theoretical Biological Physics and Departments of Chemistry and Biochemistry and Physics, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Patrick Weinkam
Peter G Wolynes
Center for Theoretical Biological Physics · US

Funding

CONCEPTUAL ASPECTS OF THE PROTEIN FOLDING PROBLEMR01GM044557 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI WOLYNES, PETER GUY · 1990 to 2018
$4.2M
NIGMS NIH HHS 5R01 GM44557NIGMS NIH HHS R01 GM044557
6 · The paper itself

Abstract

In contrast to classical chemical phenomenology, theory suggests that proteins may undergo downhill folding without an activation barrier under certain thermodynamic conditions. Recently, the BBL protein was proposed to fold by such a downhill scenario, but discrepancies between experimental results found in different groups argue against this. After briefly reviewing the major experimental studies of the BBL folding mechanism, we show that simulations of both coarse-grained and atomistic models can reconcile the seemingly conflicting observations.

Indexed as

AcyltransferasesAmino Acid SequenceBiochemistryEscherichia coliHydrogen-Ion ConcentrationMagnetic Resonance SpectroscopyModels, TheoreticalMolecular ConformationMolecular Sequence DataProtein ConformationProtein FoldingProtein Structure, SecondaryStatic ElectricityTemperatureThermodynamicsAcyltransferasesdihydrolipoamide succinyltransferase

Identifiers

PMID18172203
PMCPMC2224170
OpenAlexW2148634928

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.