Evidence map›Paper›PMID 28684417›Full record

ArticleThe Journal of biological chemistry2017

Non-canonical proteolytic activation of human prothrombin by subtilisin from

Giulia Pontarollo, Laura Acquasaliente, Daniele Peterle, Roberta Frasson, Ilaria Artusi, Vincenzo De Filippis

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. The main protease (MCommunications biology · 2025
    Article
  3. The living medicine inside us:Gut microbes reports · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. The Role of Proteolysis in Amyloidosis.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Article
  11. Review
  12. Gut Serpinome: Emerging Evidence in IBD.International journal of molecular sciences · 2021
    Review
  13. Digestive Inflammation: Role of Proteolytic Dysregulation.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Observational
  16. Article
  17. Article
  18. Article
  19. Review
  20. Proteases: Pivot Points in Functional Proteomics.Methods in molecular biology (Clifton, N.J.) · 2019
    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

6 authors at 1 institution in 1 country.

Giulia PontarolloFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy.
Laura AcquasalienteFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy.
Daniele PeterleFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy.
Roberta FrassonFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy.
Ilaria ArtusiFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy.
Vincenzo De FilippisFrom the Department of Pharmaceutical and Pharmacological Sciences, University of Padua, via Marzolo 5, Padua 35131, Italy vincenzo.defilippis@unipd.it.
University of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Blood coagulation is a finely regulated physiological process culminating with the factor Xa (FXa)-mediated conversion of the prothrombin (ProT) zymogen to active α-thrombin (αT). In the prothrombinase complex on the platelet surface, FXa cleaves ProT at Arg-271, generating the inactive precursor prethrombin-2 (Pre2), which is further attacked at Arg-320-Ile-321 to yield mature αT. Whereas the mechanism of physiological ProT activation has been elucidated in great detail, little is known about the role of bacterial proteases, possibly released in the bloodstream during infection, in inducing blood coagulation by direct proteolytic ProT activation. This knowledge gap is particularly concerning, as bacterial infections are frequently complicated by severe coagulopathies. Here, we show that addition of subtilisin (50 nm to 2 μm), a serine protease secreted by the non-pathogenic bacterium

Indexed as

Blood CoagulationModels, MolecularPlatelet AggregationAdultBacillus subtilisBacterial ProteinsCatalytic DomainEnzyme ActivationEnzyme StabilityFemaleHumansMalePeptide FragmentsProtein ConformationProtein Interaction Domains and MotifsProteolysisBacterial ProteinsPeptide FragmentsProthrombinprothrombin fragment 2Recombinant ProteinsSerine Proteinase InhibitorsSubtilisincoagulation factorinfectionproteolysisprothrombinserine protease

Identifiers

PMID28684417
PMCPMC5602379
OpenAlexW2728519024

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.