Evidence map›Paper›PMID 10339536›Full record

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

Observation of strange kinetics in protein folding.

J Sabelko, J Ervin, M Gruebele

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 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing 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

108 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Dynamical Signatures of Multifunnel Energy Landscapes.The journal of physical chemistry letters · 2022
    Review
  7. Nonrefoldability is Pervasive Across theJournal of the American Chemical Society · 2021
    Article
  8. Real-time observation of ligand-induced allosteric transitions in a PDZ domain.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Heterogeneous folding and stretched kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Review
  15. Proteins: "Boil 'Em, Mash 'Em, Stick 'Em in a Stew".The journal of physical chemistry. B · 2019
    Review
  16. Review
  17. Measuring the average shape of transition paths during the folding of a single biological molecule.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. A non-equilibrium approach to allosteric communication.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  20. Protein folding transition path times from single molecule FRET.Current opinion in structural biology · 2018
    Review

48 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

J SabelkoSchool of Chemical Sciences and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, IL 61801, USA.
J Ervin
M Gruebele

Funding

SUBMILLISECOND LASER T JUMP INDUCED PROTEIN FOLDINGR01GM057175 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GRUEBELE, MARTIN · 1998 to 2001
$338k
NIGMS NIH HHS GM057175
6 · The paper itself

Abstract

Highly nonexponential folding kinetics in aqueous solution have been observed during temperature jump-induced refolding of two proteins, yeast phosphoglycerate kinase and a ubiquitin mutant. The observations are most easily interpreted in terms of downhill folding, which posits a heterogeneous ensemble of structures en route to the folded state. The data are also reconciled with exponential kinetics measured under different experimental conditions and with titration experiments indicating cooperative folding.

Indexed as

Protein FoldingAmino Acid SubstitutionHumansKineticsNuclear Magnetic Resonance, BiomolecularPhosphoglycerate KinasePoint MutationProtein DenaturationRecombinant ProteinsSaccharomyces cerevisiaeSpectrometry, FluorescenceThermodynamicsUbiquitinsPhosphoglycerate KinaseRecombinant ProteinsUbiquitins

Identifiers

PMID10339536
PMCPMC26830

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.