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References from Rational design of a consensus bothropic metalloproteinase as an immunogen for broadly protective antivenom development. Local targets link to admitted publications; unresolved targets remain external evidence.
Snakebite envenoming
2017 · External reference
Unresolved reference
2021 · External reference
Incidence and mortality due to snakebite in the Americas
10.1371/journal.pntd.0005662 · 2017 · External reference
Understanding the role of small-molecule therapeutics for snake envenoming
10.1016/j.ebiom.2025.105635 · 2025 · External reference
Unresolved reference
External reference
Current technology for the industrial manufacture of snake antivenoms
10.1016/j.toxicon.2018.06.084 · 2018 · External reference
Horse immunization with short-chain consensus α-neurotoxin generates antibodies against broad spectrum of elapid venomous species
10.1038/s41467-019-11639-2 · 2019 · External reference
Unresolved reference
External reference
Unresolved reference
External reference
Comparison of Phylogeny, Venom Composition and Neutralization by Antivenom in Diverse Species of Bothrops Complex
10.1371/journal.pntd.0002442 · 2013 · External reference
Coagulotoxicity of Bothrops (lancehead pit-vipers) venoms from Brazil: differential biochemistry and antivenom efficacy resulting from prey-driven venom variation
10.3390/toxins10100411 · 2018 · External reference
Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage
10.1016/s0300-9084(00)01163-9 · 2000 · External reference
Immunoglobulin G and F(ab’)2 polyvalent antivenoms do not differ in their ability to neutralize hemorrhage, edema and myonecrosis induced by Bothrops asper (terciopelo) snake venom
10.1016/s0041-0101(97)00034-2 · 1997 · External reference
Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom
10.1016/s0041-0101(98)00145-7 · 1998 · External reference
Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
10.1016/j.toxicon.2005.02.012 · 2005 · External reference
The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox (Jergón) snake venom acts both on blood vessel ECM and platelets
10.1016/j.abb.2010.01.010 · 2010 · External reference
Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom
10.1016/j.biochi.2005.07.008 · 2006 · External reference
Unraveling the distinctive features of hemorrhagic and non-hemorrhagic snake venom metalloproteinases using molecular simulations
10.1007/s10822-015-9889-5 · 2016 · External reference
Progress and challenges in the field of snakebite envenoming therapeutics
10.1146/annurev-pharmtox-022024-033544 · 2025 · External reference
Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins
10.3389/fbioe.2021.811905 · 2022 · External reference
Short-chain consensus alpha-neurotoxin: a synthetic 60-mer peptide with generic traits and enhanced immunogenic properties
10.1007/s00726-018-2556-0 · 2018 · External reference
A consensus recombinant elapid long-chain α-neurotoxin and how protein folding matters for antibody recognition and neutralization of elapid venoms
10.1016/j.bbrc.2024.150420 · 2024 · External reference
UniProt: the universal protein knowledgebase in 2025
10.1093/nar/gkae1010 · 2025 · External reference
MAFFT online service: multiple sequence alignment, interactive sequence choice and visualization
10.1093/bib/bbx108 · 2019 · External reference
WebLogo: A Sequence Logo Generator: Figure 1
10.1101/gr.849004 · 2004 · External reference
A semi-empirical method for prediction of antigenic determinants on protein antigens
10.1016/0014-5793(90)80535-q · 1990 · External reference
Comparative Protein Structure Modeling Using MODELLER
2016 · External reference
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
10.1107/s0907444904026460 · 2004 · External reference
Site mutation of residues in a loop surrounding the active site of a P[sbnd]I snake venom metalloproteinase abrogates its hemorrhagic activity
10.1016/j.bbrc.2019.03.152 · 2019 · External reference
The action of proteolytic enzymes on N,N-dimethyl proteins
10.1016/s0021-9258(18)91857-0 · 1969 · External reference
Proteomic profile, biological activities and antigenic analysis of the venom from Bothriopsis bilineata smaragdina (“loro machaco”), a pitviper snake from Peru
10.1016/j.jprot.2018.07.016 · 2018 · External reference
Isolation of a Proteinase with Plasminogen-Activating Activity from Lachesis muta muta (Bushmaster) Snake Venom
10.1006/abbi.2000.1781 · 2000 · External reference
Rhomb-I, a P–I metalloproteinase from Lachesis muta rhombeata venom degrades vessel extra cellular matrix components and impairs platelet aggregation
10.1016/j.toxicon.2023.107097 · 2023 · External reference
The chicken chorioallantoic membrane model in biology, medicine and bioengineering
10.1007/s10456-014-9440-7 · 2014 · External reference
Morphology, phylogeny and taxonomy of South American bothropoid pitvipers (Serpentes, Viperidae)
10.1111/j.1463-6409.2011.00511.x · 2012 · External reference
Snakebite envenoming: A systematic review and meta-analysis of global morbidity and mortality
10.1371/journal.pntd.0012080 · 2024 · External reference
Venom variation and the future of antivenom design: Integrating population venomics, evolutionary toxinology, and precision therapeutics
10.1016/j.toxcx.2026.100246 · 2026 · External reference
Experimental Bothrops atrox envenomation: efficacy of antivenom therapy and the combination of Bothrops antivenom with dexamethasone
10.1371/journal.pntd.0005458 · 2017 · External reference
ADAM and ADAMTS family proteins and snake venom metalloproteinases: a structural overview
10.3390/toxins8050155 · 2016 · External reference
Unresolved reference
2026 · External reference
Albocollagenase, a novel recombinant P-III snake venom metalloproteinase from green pit viper (Cryptelytrops albolabris), digests collagen and inhibits platelet aggregation
10.1016/j.toxicon.2011.02.011 · 2011 · External reference
Heterologous expression of Ts8, a neurotoxin from Tityus serrulatus venom, evidences its antifungal activity
10.1016/j.toxicon.2022.08.019 · 2022 · External reference
rJararacin, a recombinant disintegrin from Bothrops jararaca venom: exploring its effects on hemostasis and thrombosis
10.1016/j.abb.2023.109557 · 2023 · External reference
Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
10.1111/j.1742-4658.2008.06466.x · 2008 · External reference
A novel fibrinolytic metalloproteinase, barnettlysin-I from Bothrops barnetti (barnett’s pitviper) snake venom with anti-platelet properties
10.1016/j.bbagen.2015.12.021 · 2016 · External reference
Cytotoxic, thrombolytic and edematogenic activities of leucurolysin-a, a metalloproteinase from Bothrops leucurus snake venom
10.1016/j.toxicon.2007.03.002 · 2007 · External reference
Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
10.1016/j.toxicon.2005.02.029 · 2005 · External reference
Characterization of the local tissue damage induced by LHF-II, a metalloproteinase with weak hemorrhagic activity isolated from Lachesis muta muta snake venom
10.1016/s0041-0101(98)00268-2 · 1999 · External reference
The health status of horses used for at least six complete cycles of loxoscelic antivenom production
10.3390/toxins15100589 · 2023 · External reference
Recommandations pour la production, le contrôle et l’enregistrement des immunoglobulines antivenimeuses
10.1051/jbio/2009043 · 2010 · External reference
Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis
10.1016/j.jprot.2007.10.004 · 2008 · External reference
Snake venomics across genus Lachesis. Ontogenetic changes in the venom composition of Lachesis stenophrys and comparative proteomics of the venoms of adult Lachesis melanocephala and Lachesis acrochorda
10.1016/j.jprot.2012.09.003 · 2012 · External reference
Snake venomics of Lachesis muta rhombeata and genus-wide antivenomics assessment of the paraspecific immunoreactivity of two antivenoms evidence the high compositional and immunological conservation across Lachesis
10.1016/j.jprot.2013.05.028 · 2013 · External reference
Comparative proteomic profiling and functional characterization of venom pooled from captive Crotalus durissus terrificus specimens and the Brazilian crotalic reference venom
10.1016/j.toxicon.2020.07.001 · 2020 · External reference
Fast venomic analysis of Crotalus durissus terrificus from northeastern Argentina
10.1016/j.toxcx.2020.100047 · 2020 · External reference
Diversity of metalloproteinases in Bothrops neuwiedi snake venom transcripts: evidences for recombination between different classes of SVMPs
10.1186/1471-2156-12-94 · 2011 · External reference
Exploring the proteomes of the venoms of the Peruvian pit vipers Bothrops atrox, B. barnetti and B. pictus
10.1016/j.jprot.2012.01.020 · 2012 · External reference
Antibodies as snakebite antivenoms: past and future
10.3390/toxins14090606 · 2022 · External reference
Pros and cons of different therapeutic antibody formats for recombinant antivenom development
10.1016/j.toxicon.2018.03.004 · 2018 · External reference