Evidence map›Paper›PMID 22179065›Full record

ArticleNature chemical biology2011

Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins.

Anna L Mallam, Sophie E Jackson

Abstract read
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In one paragraph

Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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

59 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Is There a Functional Role for the Knotted Topology in Protein UCH-L1?Journal of chemical information and modeling · 2024
    Article
  7. Article
  8. Article
  9. AlphaFold predicts novel human proteins with knots.Protein science : a publication of the Protein Society · 2023
    Article
  10. AlphaFold predicts the most complex protein knot and composite protein knots.Protein science : a publication of the Protein Society · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Nascent Folding of Proteins Across the Three Domains of Life.Frontiers in molecular biosciences · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors.

Anna L MallamDepartment of Chemistry, The University of Cambridge, Cambridge, UK.
Sophie E Jackson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Topological knots are found in a considerable number of protein structures, but it is not clear how they knot and fold within the cellular environment. We investigated the behavior of knotted protein molecules as they are first synthesized by the ribosome using a cell-free translation system. We found that newly translated knotted proteins can spontaneously self-tie and do not require the assistance of molecular chaperones to fold correctly to their trefoil-knotted structures. This process is slow but efficient, and we found no evidence of misfolded species. A kinetic analysis indicates that the knotting process is rate limiting, occurs post-translationally, and is specifically and significantly (P < 0.001) accelerated by the GroEL-GroES chaperonin complex. This demonstrates a new active mechanism for this molecular chaperone and suggests that chaperonin-catalyzed knotting probably dominates in vivo. These results explain how knotted protein structures have withstood evolutionary pressures despite their topological complexity.

Indexed as

Protein BiosynthesisProtein FoldingBacterial ProteinsCell-Free SystemChaperonin 10Chaperonin 60ChaperoninsKineticsMolecular ChaperonesBacterial ProteinsChaperonin 10Chaperonin 60ChaperoninsMolecular Chaperones

Identifiers

PMID22179065

What OpenQuestion holds

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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.