Evidence map›Paper›PMID 27787696›Full record

ArticleJournal of thrombosis and thrombolysis2017

Carbon monoxide releasing molecule-2 inhibition of snake venom thrombin-like activity: novel biochemical "brake"?

Vance G Nielsen, Charles M Bazzell

Abstract read
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In one paragraph

Article in Journal of thrombosis and thrombolysis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

12 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Ruthenium, Not Carbon Monoxide, Inhibits the Procoagulant Activity ofInternational journal of molecular sciences · 2020
    Article
  4. Characterization of L-amino Acid Oxidase Derived fromInternational journal of molecular sciences · 2019
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. CatroxMP-II: a heme-modulated fibrinogenolytic metalloproteinase isolated from Crotalus atrox venom.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2018
    Article
  10. Article
  11. Review
  12. 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

2 authors at 1 institution in 1 country.

Vance G NielsenDepartment of Anesthesiology, The University of Arizona College of Medicine, 1501 North Campbell Avenue, P.O. Box 245114, Tucson, AZ, 85724-5114, USA. vgnielsen333@gmail.com.
Charles M BazzellDepartment of Anesthesiology, The University of Arizona College of Medicine, 1501 North Campbell Avenue, P.O. Box 245114, Tucson, AZ, 85724-5114, USA.
University of Arizona · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A complication of defibrinogenation therapy with snake venom enzymes such as ancrod is hypofibrinogenemia associated bleeding secondary to no human-derived inhibitor being available to inactivate or diminish the activity of such enzymes. Of interest, ancrod contains a critical histidine residue without which enzymatic activity is inhibited, and carbon monoxide has been demonstrated to inhibit biomolecular function by interacting with histidine moieties in ion channels. We tested the hypothesis that exposure of three different snake venoms containing serine proteases with thrombin-like activity (which included ancrod) to carbon monoxide derived from carbon monoxide releasing molecule-2 would diminish their effects on plasmatic coagulation as assessed by thrombelastography. In the case of the Malayan pit viper and Eastern diamondback rattlesnake venoms, carbon monoxide diminished the effects of thrombin-like activity. In contrast, timber rattlesnake venom demonstrated enhancement of "thrombin-generating" activity with simultaneous loss of thrombin-like activity in response to carbon monoxide exposure. These findings may serve as the rational basis for not just continuing to investigate the potential of snake venom enzymes as clinical defibrinogenating agents, but to also to assess the potential to stop such agents from becoming a catalytic "runaway train" by judicious application of a biochemical "brake" such as carbon monoxide.

Indexed as

AncrodAnimalsBlood CoagulationCarbon MonoxideCrotalid VenomsFibrinolytic AgentsHumansOrganometallic CompoundsSerine ProteasesSerine Proteinase InhibitorsThrombelastographyThrombinAncrodCarbon MonoxideCrotalid VenomsFibrinolytic AgentsOrganometallic CompoundsSerine ProteasesSerine Proteinase InhibitorsThrombintricarbonyldichlororuthenium (II) dimerCarbon monoxideFibrinogen depleting agentHistidineSnake venom serine proteaseThrombelastography

Identifiers

PMID27787696
OpenAlexW2540683849

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.