Evidence map›Paper›PMID 32855236›Full record

ArticleThe Journal of biological chemistry2020

Zymogen and activated protein C have similar structural architecture.

Bosko M Stojanovski, Leslie A Pelc, Xiaobing Zuo, Enrico Di Cera

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Thrombin has dual trypsin-like and chymotrypsin-like specificity.Journal of thrombosis and haemostasis : JTH · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Comparative sequence analysis of vitamin K-dependent coagulation factors.Journal of thrombosis and haemostasis : JTH · 2022
    Article
  13. Article
  14. 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

4 authors at 3 institutions in 2 countries.

Bosko M StojanovskiEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri, USA.
Leslie A PelcEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri, USA.
Xiaobing ZuoX-Ray Science Division, Argonne National Laboratory, Lemont, Illinois, USA.
Enrico Di CeraEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri, USA. Electronic address: enrico@slu.edu.
Saint Louis University · USArgonne National Laboratory · USSaint Louis University · ES

Funding

STUDIES ON THROMBIN ALLOSTERYR01HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI Enrico Di Cera · 2000 to 2026
$9.6M
Structural enzymology of factor V activationR01HL147821 · NHLBI · SAINT LOUIS UNIVERSITY · PI Enrico Di Cera · 2019 to 2026
$3.7M
Structural enzymology of protein CR01HL139554 · NHLBI · SAINT LOUIS UNIVERSITY · PI DI CERA, ENRICO · 2018 to 2025
$3.7M
BIOPHYSICAL STUDIES OF THROMBINR29HL049413 · NHLBI · WASHINGTON UNIVERSITY · PI DI CERA, ENRICO · 1995 to 1999
–
NHLBI NIH HHS R01 HL049413NHLBI NIH HHS R01 HL139554NHLBI NIH HHS R01 HL147821NHLBI NIH HHS R29 HL049413
6 · The paper itself

Abstract

Activated protein C is a trypsin-like protease with anticoagulant and cytoprotective properties that is generated by thrombin from the zymogen precursor protein C in a reaction greatly accelerated by the cofactor thrombomodulin. The molecular details of this activation remain elusive due to the lack of structural information. We now fill this gap by providing information on the overall structural organization of these proteins using single molecule FRET and small angle X-ray scattering. Under physiological conditions, both zymogen and protease adopt a conformation with all domains vertically aligned along an axis 76 Å long and maximal particle size of 120 Å. This conformation is stabilized by binding of Ca

Indexed as

Enzyme PrecursorsFluorescence Resonance Energy TransferHumansParticle SizeProtein CProtein ConformationScattering, Small AngleX-Ray DiffractionEnzyme PrecursorsProtein Cligand-binding proteinprotein Cprotein conformationserine proteasesingle molecule biophysicssingle-molecule biophysicsthrombin

Identifiers

PMID32855236
PMCPMC7650249
OpenAlexW3081226976

What OpenQuestion holds

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LicenceCC BY
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.