Evidence map›Paper›PMID 32541047›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.

Tae Wu Kim, Sang Jin Lee, Junbeom Jo, Jong Goo Kim, Hosung Ki, Chang Woo Kim, Kwang Hyun Cho, Jungkweon Choi, Jae Hyuk Lee, Michael Wulff and 2 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Article
  10. Article
  11. Systems biology of protein network.Biophysical reviews · 2022
    Article
  12. Review
  13. Reaction dynamics studiedChemical science · 2022
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Time-resolved X-ray scattering studies of proteins.Current opinion in structural biology · 2021
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Tae Wu KimDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.ORCID 0000-0002-6370-0907
Sang Jin LeeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Junbeom JoDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Jong Goo KimDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Hosung KiDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Chang Woo KimDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Kwang Hyun ChoDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea.
Jungkweon ChoiCenter for Nanomaterials and Chemical Reactions, Institute for Basic Science, Daejeon 34141, Republic of Korea.ORCID 0000-0002-9979-305X
Jae Hyuk LeeXFEL Beamline Department, Pohang Accelerator Laboratory, Pohang 37673, Republic of Korea.
Michael WulffExperiments Division, European Synchrotron Radiation Facility, F-38043 Grenoble Cedex, France.
Young Min RheeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea; ymrhee@kaist.ac.kr hyotcherl.ihee@kaist.ac.kr.ORCID 0000-0002-2392-3962
Hyotcherl IheeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon 34141, Republic of Korea; ymrhee@kaist.ac.kr hyotcherl.ihee@kaist.ac.kr.ORCID 0000-0003-0397-5965

Funding

Electric Field-stimulated Protein MechanicsP41GM118217 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH, RANGANATHAN, RAMA · 2019 to 2021
$5.3M
BioCARS: A Synchrotron Structure Biology ResourceR24GM111072 · NIGMS · UNIVERSITY OF CHICAGO · PI MOFFAT, JOHN KEITH · 2013 to 2016
$2.3M
NIGMS NIH HHS P41 GM118217NIGMS NIH HHS R24 GM111072
6 · The paper itself

Abstract

One of the most challenging tasks in biological science is to understand how a protein folds. In theoretical studies, the hypothesis adopting a funnel-like free-energy landscape has been recognized as a prominent scheme for explaining protein folding in views of both internal energy and conformational heterogeneity of a protein. Despite numerous experimental efforts, however, comprehensively studying protein folding with respect to its global conformational changes in conjunction with the heterogeneity has been elusive. Here we investigate the redox-coupled folding dynamics of equine heart cytochrome

Indexed as

AnimalsCytochromes cHorsesKineticsMolecular Dynamics SimulationOxidation-ReductionProtein FoldingCytochromes ccytochrome censemblemolecular dynamics simulationprotein foldingtime-resolved X-ray scattering

Identifiers

PMID32541047
PMCPMC7334511

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

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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.