Evidence map›Paper›PMID 24576574›Full record

ReviewBiochimica et biophysica acta2014

Disulfide bond formation in prokaryotes: history, diversity and design.

Feras Hatahet, Dana Boyd, Jon Beckwith

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. 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, 119 citations in OpenAlex.

  1. Papain expression in theApplied and environmental microbiology · 2025
    Article
  2. Article
  3. Review
  4. A Proposal for a Consolidated Structural Model of the CagY Protein ofInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Distinct enzymatic strategies forCritical reviews in biochemistry and molecular biology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Interplay between DsbA1, DsbA2 and C8J_1298 Periplasmic Oxidoreductases ofInternational journal of molecular sciences · 2021
    Article
  15. Role of Disulfide Bonds and Sulfhydryl Blocked byFoods (Basel, Switzerland) · 2021
    Article
  16. Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

3 authors at 1 institution in 1 country.

Feras HatahetDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Dana BoydDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Jon BeckwithDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: jon_beckwith@hms.harvard.edu.
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 GM041883NIGMS NIH HHS R01 GM041883
6 · The paper itself

Abstract

The formation of structural disulfide bonds is essential for the function and stability of a great number of proteins, particularly those that are secreted. There exists a variety of dedicated cellular catalysts and pathways from archaea to humans that ensure the formation of native disulfide bonds. In this review we describe the initial discoveries of these pathways and report progress in recent years in our understanding of the diversity of these pathways in prokaryotes, including those newly discovered in some archaea. We will also discuss the various successful efforts to achieve laboratory-based evolution and design of synthetic disulfide bond formation machineries in the bacterium Escherichia coli. These latter studies have also led to new more general insights into the redox environment of the cytoplasm and bacterial cell envelope. This article is part of a Special Issue entitled: Thiol-Based Redox Processes.

Indexed as

AnimalsDisulfidesHumansOxidation-ReductionProkaryotic CellsDisulfidesDisulfide bond formationDsbADsbBHyperthermophilesPDIVKOR

Identifiers

PMID24576574
PMCPMC4048783
OpenAlexW2018148650

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.