Evidence map›Paper›PMID 29217641›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Molecular chaperones maximize the native state yield on biological times by driving substrates out of equilibrium.

Shaon Chakrabarti, Changbong Hyeon, Xiang Ye, George H Lorimer, D Thirumalai

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Moderate activity of RNA chaperone maximizes the yield of self-spliced pre-RNA in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Iterative annealing mechanism explains the functions of the GroEL and RNA chaperones.Protein science : a publication of the Protein Society · 2020
    Review
  16. Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Proteostasis collapse is a driver of cell aging and death.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Crick's sequence hypothesis - a review.Communicative & integrative biology · 2019
    Review
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 5 institutions in 2 countries.

Shaon ChakrabartiDepartment of Biostatistics and Computational Biology, Dana-Farber Cancer Institute, Boston, MA 02115.
Changbong HyeonSchool of Computational Sciences, Korea Institute for Advanced Study, Seoul 02455, Korea.ORCID 0000-0002-4844-7237
Xiang YeDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104.
George H LorimerDepartment of Chemistry and Biochemistry, Institute for Physical Sciences and Technology, University of Maryland, College Park, MD 20742; glorimer@umd.edu dave.thirumalai@gmail.com.
D ThirumalaiDepartment of Chemistry, University of Texas at Austin, Austin, TX 78712 glorimer@umd.edu dave.thirumalai@gmail.com.
Harvard University · USKorea Institute for Advanced Study · KRThe University of Texas at Austin · USUniversity of Maryland, College Park · USUniversity of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molecular chaperones facilitate the folding of proteins and RNA in vivo. Under physiological conditions, the in vitro folding of

Indexed as

AlgorithmsChaperonin 60KineticsModels, MolecularMolecular ChaperonesMolecular ConformationProtein FoldingRNARNA FoldingStructure-Activity RelationshipSubstrate SpecificityChaperonin 60Molecular ChaperonesRNAmolecular chaperonesnonequilibrium steady stateoptimizing short-term yieldprotein foldingRNA folding

Identifiers

PMID29217641
PMCPMC5754791
OpenAlexW2775336518

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.