Evidence map›Paper›PMID 19766568›Full record

ArticleCell2009

Detecting folding intermediates of a protein as it passes through the bacterial translocation channel.

Hiroshi Kadokura, Jon Beckwith

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Disulphide bond-forming enzymes in clostridial species.Microbiology (Reading, England) · 2025
    Article
  5. Review
  6. A Buried Water Network Modulates the Activity of theAntioxidants (Basel, Switzerland) · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Strategies to Enhance Periplasmic Recombinant Protein Production Yields inFrontiers in bioengineering and biotechnology · 2021
    Review
  12. Review
  13. Review
  14. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    Article
  15. Journal of virology · 2020
    Article
  16. Observing the nonvectorial yet cotranslational folding of a multidomain protein, LDL receptor, in the ER of mammalian cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. Review

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

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 at 1 institution in 2 countries.

Hiroshi KadokuraDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, USA. hkadokura@bs.naist.jp
Jon Beckwith
Harvard University · US

Funding

Microbial Diversity in Mechanisms of Disulfide Bond Formation and ReductionR01GM041883 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BOYD, DANA · 1989 to 2014
$7.8M
NIGMS NIH HHS GM41883NIGMS NIH HHS R01 GM041883
6 · The paper itself

Abstract

Most bacterial exported proteins cross the cytoplasmic membrane as unfolded polypeptides. However, little is known about how they fold during or after this process due to the difficulty in detecting folding intermediates. Here we identify cotranslational and posttranslational folding intermediates of a periplasmic protein in which the protein and DsbA, a periplasmic disulfide bond-forming enzyme, are covalently linked by a disulfide bond. The cotranslational mixed-disulfide intermediate is, upon further chain elongation, resolved, releasing the oxidized polypeptide, thus allowing us to follow the folding process. This analysis reveals that two cysteines that are joined to form a structural disulfide can play different roles during the folding reaction and that the mode of translocation (cotranslational verse posttranslational) can affect the folding process of a protein in the periplasm. The latter finding leads us to propose that the activity of the ribosome (translation) can modulate protein folding even in an extracytosolic compartment.

Indexed as

Alkaline PhosphataseCysteineEscherichia coliEscherichia coli ProteinsPeriplasmProtein BiosynthesisProtein Disulfide-IsomerasesProtein FoldingAlkaline PhosphataseCysteinedsbA protein, E coliEscherichia coli ProteinsphoA protein, E coliProtein Disulfide-Isomerases

Identifiers

PMID19766568
PMCPMC2750780
OpenAlexW2042799385

What OpenQuestion holds

Textmetadata
LicenceTDM
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.