Evidence map›Paper›PMID 10051589›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Stretching lattice models of protein folding.

N D Socci, J N Onuchic, P G Wolynes

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Probing static disorder in Arrhenius kinetics by single-molecule force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  7. Article
  8. Stabilizing effect of knots on proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  9. Article
  10. Article
  11. Force unfolding single RNAs.Biophysical journal · 2006
    Article
  12. Dissecting the mechanical unfolding of ubiquitin.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  13. Article
  14. Unfolding of titin domains studied by molecular dynamics simulations.Journal of muscle research and cell motility · 2002
    Article
  15. Article
  16. Article
  17. Native topology determines force-induced unfolding pathways in globular proteins.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  18. 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.

N D SocciBell Laboratories, Lucent Technologies, 700 Mountain Avenue, Murray Hill, NJ 07974, USA. soccin@rockefeller.edu
J N Onuchic
P G Wolynes

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 1R01 GM44557NIGMS NIH HHS R01 GM044557
6 · The paper itself

Abstract

A new class of experiments that probe folding of individual protein domains uses mechanical stretching to cause the transition. We show how stretching forces can be incorporated in lattice models of folding. For fast folding proteins, the analysis suggests a complex relation between the force dependence and the reaction coordinate for folding.

Indexed as

Models, TheoreticalProtein FoldingAmino Acid SequenceDrug StabilityKineticsMolecular Sequence DataPeptidesProtein DenaturationPeptides

Identifiers

PMID10051589
PMCPMC26731

What OpenQuestion holds

Texttitle and abstract
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.