Evidence map›Paper›PMID 22280304›Full record

ArticleJournal of the American Chemical Society2012

Intramolecular disulfide bond between catalytic cysteines in an intein precursor.

Wen Chen, Lingyun Li, Zhenming Du, Jiajing Liu, Julie N Reitter, Kenneth V Mills, Robert J Linhardt, Chunyu Wang

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 47 citations in OpenAlex.

  1. Crystallization of L-Cysteine in Heavy Water Induces Intrinsic Fluorescence.Angewandte Chemie (International ed. in English) · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Methods to Study the Structure and Catalytic Activity of cis-Splicing Inteins.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Exploring the folding pathway of green fluorescent protein through disulfide engineering.Protein science : a publication of the Protein Society · 2015
    Article
  16. Thiol-based redox switches.Biochimica et biophysica acta · 2014
    Review
  17. Enigmatic distribution, evolution, and function of inteins.The Journal of biological chemistry · 2014
    Review
  18. Protein splicing: how inteins escape from precursor proteins.The Journal of biological chemistry · 2014
    Review
  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

8 authors at 2 institutions in 1 country.

Wen ChenDepartment of Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
Lingyun Li
Zhenming Du
Jiajing Liu
Julie N Reitter
Kenneth V Mills
Robert J Linhardt
Chunyu Wang
Rensselaer Polytechnic Institute · USCollege of the Holy Cross · US

Funding

SEQUENCING THE POLYSACCHARIDE COMPONENT OF PROTEOGLYCANSR01GM038060 · NIGMS · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1988 to 2012
$2.8M
Testing novel hypotheses in Mtu RecA intein splicingR01GM081408 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI WANG, CHUNYU · 2007 to 2011
$1.7M
NIGMS NIH HHS GM081408NIGMS NIH HHS R01 GM038060NIGMS NIH HHS R01 GM081408
6 · The paper itself

Abstract

Protein splicing is a self-catalyzed and spontaneous post-translational process in which inteins excise themselves out of precursor proteins while the exteins are ligated together. We report the first discovery of an intramolecular disulfide bond between the two active-site cysteines, Cys1 and Cys+1, in an intein precursor composed of the hyperthermophilic Pyrococcus abyssi PolII intein and extein. The existence of this intramolecular disulfide bond is demonstrated by the effect of reducing agents on the precursor, mutagenesis, and liquid chromatography-mass spectrometry (LC-MS) with tandem MS (MS/MS) of the tryptic peptide containing the intramolecular disulfide bond. The disulfide bond inhibits protein splicing, and splicing can be induced by reducing agents such as tris(2-carboxyethyl)phosphine (TCEP). The stability of the intramolecular disulfide bond is enhanced by electrostatic interactions between the N- and C-exteins but is reduced by elevated temperature. The presence of this intramolecular disulfide bond may contribute to the redox control of splicing activity in hypoxia and at low temperature and point to the intriguing possibility that inteins may act as switches to control extein function.

Indexed as

InteinsCatalysisCysteineDisulfidesPyrococcus abyssiCysteineDisulfides

Identifiers

PMID22280304
PMCPMC3279520
OpenAlexW2035379837

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.