Evidence map›Paper›PMID 24549644›Full record

ArticleProtein science : a publication of the Protein Society2014

Structural insight into the dimerization of human protein disulfide isomerase.

Sara Bastos-Aristizabal, Guennadi Kozlov, Kalle Gehring

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

15 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. ERO1-PDI Redox Signaling in Health and Disease.Antioxidants & redox signaling · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. 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

3 authors at 1 institution in 1 country.

Sara Bastos-AristizabalDepartment of Biochemistry, Groupe de recherche axé sur la structure des protéines, McGill University, 3649 Promenade Sir William Osler, Montréal, Québec, H3G 0B1, Canada.
Guennadi Kozlov
Kalle Gehring
McGill University · CA

Funding

ZINC FINGER-DNA COMPLEXP41RR001646 · NCRR · CORNELL UNIVERSITY ITHACA · PI THORNE, ROBERT E. · 1985 to 2011
$23.8M
Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
NCRR NIH HHS P41 RR001646NCRR NIH HHS RR-01646NIGMS NIH HHS DMR-0225180NIGMS NIH HHS P41 GM103485
6 · The paper itself

Abstract

Protein disulfide isomerases (PDIs) are responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum (ER). Here, it is shown that human PDI (PDIA1) dimerizes in vivo and proposed that the dimerization of PDI has physiological relevance by autoregulating its activity. The crystal structure of the dimeric form of noncatalytic bb' domains of human PDIA1 determined to 2.3 Å resolution revealed that the formation of dimers occludes the substrate binding site and may function as a mechanism to regulate PDI activity in the ER.

Indexed as

Protein MultimerizationBinding SitesCrystallography, X-RayEndoplasmic ReticulumHumansModels, MolecularProcollagen-Proline DioxygenaseProtein Disulfide-IsomerasesProtein Structure, TertiaryThioredoxinsP4HB protein, humanProcollagen-Proline DioxygenaseProtein Disulfide-IsomerasesThioredoxinscrystal structuredimerizationendoplasmic reticulumprotein disulfide isomerasethioredoxin-like domain

Identifiers

PMID24549644
PMCPMC4005713
OpenAlexW2102219684

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.