Evidence map›Paper›PMID 39195771›Full record

ArticleToxins2024

Importance of the Cysteine-Rich Domain of Snake Venom Prothrombin Activators: Insights Gained from Synthetic Neutralizing Antibodies.

Laetitia E Misson Mindrebo, Jeffrey T Mindrebo, Quoc Tran, Mark C Wilkinson, Jessica M Smith, Megan Verma, Nicholas R Casewell, Gabriel C Lander, Joseph G Jardine

Abstract read
In one paragraph

Article in Toxins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Proteomic profiling and comparative hemotoxicity ofThe journal of venomous animals and toxins including tropical diseases · 2026
    Article
  3. Article
  4. 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

9 authors.

Laetitia E Misson MindreboDepartment of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-6318-1126
Jeffrey T MindreboDepartment of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
Quoc TranDepartment of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-1250-5853
Mark C WilkinsonCentre for Snakebite Research & Interventions, Department of Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool L3 5QA, UK.
Jessica M SmithInternational AIDS Vaccine Initiative, New York, NY 10004, USA.ORCID 0009-0000-1554-6768
Megan VermaDepartment of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA 92037, USA.
Nicholas R CasewellCentre for Snakebite Research & Interventions, Department of Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool L3 5QA, UK.ORCID 0000-0002-8035-4719
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-4921-1135
Joseph G JardineDepartment of Immunology and Microbiology, Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-8951-1074

Funding

IMPACTING MITOCHONDRIAL FUNCTION THROUGH ALTERED PROTEASE ACTIVITYR01NS095892 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2016 to 2025
$5.3M
Defining Structural and Molecular Mechanisms of The Human Multifunctional Mitochondrial Protease, LONP1F32GM145143 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI MINDREBO, JEFFREY TODD · 2022 to 2024
$216k
NIGMS NIH HHS F32 GM145143NIH HHS F32GM145143NIH HHS NS095892NIH HHS S10OD0216NINDS NIH HHS R01 NS095892U.K. Foreign Commonwealth & Development Office 300341-115Wellcome TrustWellcome Trust 221705/Z/20/ZWellcome Trust 223619/Z/21/Z
6 · The paper itself

Abstract

Snake venoms are cocktails of biologically active molecules that have evolved to immobilize prey, but can also induce a severe pathology in humans that are bitten. While animal-derived polyclonal antivenoms are the primary treatment for snakebites, they often have limitations in efficacy and can cause severe adverse side effects. Building on recent efforts to develop improved antivenoms, notably through monoclonal antibodies, requires a comprehensive understanding of venom toxins. Among these toxins, snake venom metalloproteinases (SVMPs) play a pivotal role, particularly in viper envenomation, causing tissue damage, hemorrhage and coagulation disruption. One of the current challenges in the development of neutralizing monoclonal antibodies against SVMPs is the large size of the protein and the lack of existing knowledge of neutralizing epitopes. Here, we screened a synthetic human antibody library to isolate monoclonal antibodies against an SVMP from saw-scaled viper (genus

Indexed as

Antibodies, NeutralizingProthrombinAnimalsAntibodies, MonoclonalAntiveninsCysteineHumansMetalloproteasesProtein DomainsViperidaeViper VenomsAntibodies, MonoclonalAntibodies, NeutralizingAntiveninsCysteineMetalloproteasesProthrombinViper Venomscysteine-rich domainecarin structureEchisneutralizing antibodyprothrombin activatorrecombinant antivenomsnake venom metalloproteinases

Identifiers

PMID39195771
PMCPMC11360484

What OpenQuestion holds

Textmetadata
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.