Evidence map›Paper›PMID 12196629›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Cytochrome c folding pathway: kinetic native-state hydrogen exchange.

Linh Hoang, Sabrina Bedard, Mallela M G Krishna, Yan Lin, S Walter Englander

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. HDX-MS finds that partial unfolding with sequential domain activation controls condensation of a cellular stress marker.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. POPPeT: a New Method to Predict the Protection Factor of Backbone Amide Hydrogens.Journal of the American Society for Mass Spectrometry · 2019
    Article
  6. Article
  7. The case for defined protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  9. Cytochrome c folds through foldon-dependent native-like intermediates in an ordered pathway.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. The nature of protein folding pathways.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Review
  12. Capping motifs stabilize the leucine-rich repeat protein PP32 and rigidify adjacent repeats.Protein science : a publication of the Protein Society · 2014
    Article
  13. Article
  14. Article
  15. Protein dynamics viewed by hydrogen exchange.Protein science : a publication of the Protein Society · 2012
    Article
  16. Structural and kinetic mapping of side-chain exposure onto the protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
  18. Article
  19. Biomolecular NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010
    Review
  20. Native state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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

5 authors at 2 institutions in 1 country.

Linh HoangThe Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.med.upenn.edu
Sabrina Bedard
Mallela M G Krishna
Yan Lin
S Walter Englander
Johnson Foundation · USUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Native-state hydrogen exchange experiments under EX1 conditions can distinguish partially unfolded intermediates by their formation rates and identify the amide hydrogens exposed and protected in each. Results obtained define a cytochrome c intermediate seen only poorly before and place it early on the major unfolding pathway. Four distinct unfolding steps are found to be kinetically ordered in the same pathway sequence inferred before.

Indexed as

AnimalsBiophysical PhenomenaBiophysicsCytochrome c GroupHorsesHydrogenHydrogen-Ion ConcentrationIn Vitro TechniquesKineticsModels, MolecularProtein DenaturationProtein FoldingCytochrome c GroupHydrogen

Identifiers

PMID12196629
PMCPMC129417
OpenAlexW2061342938

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.