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High throughput screening and identification of coagulopathic snake venom proteins and peptides using nanofractionation and proteomics approaches
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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The molecular cloning of a phospholipase A2 from Bothrops jararacussu snake venom: Evolution of venom group II phospholipase A2's may imply gene duplications
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Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes
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Liquid chromatographic nanofractionation with parallel mass spectrometric detection for the screening of plasmin inhibitors and (metallo)proteinases in snake venoms
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Myotoxin II from Bothrops asper (terciopelo) venom is a lysine-49 phospholipase A2
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Snake venom variability: methods of study, results and interpretation
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Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
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Prothrombin activation induced by ecarin - A prothrombin converting enzyme from echis carinatus venom
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Hemorrhagic metalloproteinases from snake venoms
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Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom
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Triwaglerin: a potent platelet aggregation inducer purified from Trimeresurus wagleri snake venom
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A basic phospholipase A from the venom of the australian king brown snake (Pseudechis australis) showing diverse activities against membranes
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Isolation and identification of angiotensin-like peptides from the plasma of the snake Bothrops jararaca
inferredcites →https://doi.org/10.1016/j.abb.2004.08.018openalex-snapshot
Cloning, characterization, and structural analysis of a C-type lectin from Bothrops insularis (BiL) venom
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Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis ocellatus on blood coagulation and platelets
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What killed Karl Patterson Schmidt? Combined venom gland transcriptomic, venomic and antivenomic analysis of the South African green tree snake (the boomslang), Dispholidus typus
inferredcites →https://doi.org/10.1016/j.bbrc.2005.01.148openalex-snapshot
Molecular cloning, functional expression, and molecular modeling of bothrostatin, a new highly active disintegrin from Bothrops jararaca venom
inferredcites →https://doi.org/10.1016/j.biochi.2011.08.003openalex-snapshot
Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms
inferredcites →https://doi.org/10.1016/j.chroma.2012.09.061openalex-snapshot
Coupling ultra high-pressure liquid chromatography with mass spectrometry: Constraints and possible applications
inferredcites →https://doi.org/10.1016/j.gene.2006.03.008openalex-snapshot
Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals novel α9β1 integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases
inferredcites →https://doi.org/10.1016/j.jprot.2008.10.003openalex-snapshot
Combined snake venomics and venom gland transcriptomic analysis of the ocellated carpet viper, Echis ocellatus
inferredcites →https://doi.org/10.1016/j.jprot.2011.06.019openalex-snapshot
Research strategies to improve snakebite treatment: Challenges and progress
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Comparative proteomic analysis of the venom of the taipan snake, Oxyuranus scutellatus, from Papua New Guinea and Australia: Role of neurotoxic and procoagulant effects in venom toxicity
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Venomics of Calloselasma rhodostoma , the Malayan pit viper: A complex toxin arsenal unraveled
inferredcites →https://doi.org/10.1016/j.peptides.2004.04.006openalex-snapshot
Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography
inferredcites →https://doi.org/10.1016/j.toxicon.2003.08.009openalex-snapshot
Cloning of a prothrombin activator-like metalloproteinase from the West African saw-scaled viper, Echis ocellatus
inferredcites →https://doi.org/10.1016/j.toxicon.2004.07.028openalex-snapshot
Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom
inferredcites →https://doi.org/10.1016/j.toxicon.2005.02.021openalex-snapshot
Structures and functions of snake venom CLPs (C-type lectin-like proteins) with anticoagulant-, procoagulant-, and platelet-modulating activities
inferredcites →https://doi.org/10.1016/j.toxicon.2005.02.029openalex-snapshot
Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
inferredcites →https://doi.org/10.1016/j.toxicon.2008.11.006openalex-snapshot
C-type lectin protein isoforms of Macrovipera lebetina: cDNA cloning and genetic diversity
inferredcites →https://doi.org/10.1016/j.toxicon.2013.05.017openalex-snapshot
Cytotoxic activities of [Ser49]phospholipase A2 from the venom of the saw-scaled vipers Echis ocellatus, Echis pyramidum leakeyi, Echis carinatus sochureki, and Echis coloratus
inferredcites →https://doi.org/10.1016/j.toxicon.2015.03.019openalex-snapshot
Elucidation of procoagulant mechanism and pathophysiological significance of a new prothrombin activating metalloprotease purified from Daboia russelii russelii venom
inferredcites →https://doi.org/10.1016/j.toxicon.2015.12.008openalex-snapshot
At-line nanofractionation with parallel mass spectrometry and bioactivity assessment for the rapid screening of thrombin and factor Xa inhibitors in snake venoms
inferredcites →https://doi.org/10.1016/j.toxicon.2018.04.022openalex-snapshot
Neurotoxicity fingerprinting of venoms using on-line microfluidic AChBP profiling
inferredcites →https://doi.org/10.1016/j.toxicon.2018.08.009openalex-snapshot
Detection and identification of antibacterial proteins in snake venoms using at-line nanofractionation coupled to LC-MS
inferredcites →https://doi.org/10.1016/j.toxicon.2018.11.292openalex-snapshot
Neutralizing properties of LY315920 toward snake venom group I and II myotoxic phospholipases A2
inferredcites →https://doi.org/10.1016/j.toxlet.2017.08.020openalex-snapshot
Differential procoagulant effects of saw-scaled viper (Serpentes: Viperidae: Echis) snake venoms on human plasma and the narrow taxonomic ranges of antivenom efficacies
inferredcites →https://doi.org/10.1016/j.ympev.2016.07.029openalex-snapshot
Diversification in vipers: Phylogenetic relationships, time of divergence and shifts in speciation rates
inferredcites →https://doi.org/10.1016/s0021-9258(18)47808-8openalex-snapshot
Structure-function relationships of phospholipases. The anticoagulant region of phospholipases A2.
inferredcites →https://doi.org/10.1016/s0021-9258(18)98563-7openalex-snapshot
The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fc epsilon receptor for immunoglobulin E
inferredcites →https://doi.org/10.1016/s0021-9258(19)49685-3openalex-snapshot
Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains.
inferredcites →https://doi.org/10.1016/s0041-008x(03)00337-5openalex-snapshot
Pulmonary hemorrhage induced by jararhagin, a metalloproteinase from Bothrops jararaca snake venom
inferredcites →https://doi.org/10.1016/s0041-0101(00)00089-1openalex-snapshot
Mass spectrophotometric evidence for P-III/P-IV metalloproteinases in the venom of the Boomslang (Dispholidus typus)
inferredcites →https://doi.org/10.1016/s0041-0101(02)00312-4openalex-snapshot
Molecular cloning of phospholipases A2 from venom glands of Echis carpet vipers
inferredcites →https://doi.org/10.1016/s0378-1119(03)00716-9openalex-snapshot
Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species
inferredcites →https://doi.org/10.1016/s1357-2725(00)00073-xopenalex-snapshot
Cloning and cDNA sequence analysis of Lys49 and Asp49 basic phospholipase A2 myotoxin isoforms from Bothrops asper
inferredcites →https://doi.org/10.1021/bi00021a033openalex-snapshot
Purification, Characterization, and Amino Acid Sequence of a Serine Proteinase, PA-BJ, with Platelet-Aggregating Activity from the Venom of Bothrops jararaca
inferredcites →https://doi.org/10.1021/bi00173a030openalex-snapshot
Purification and Characterization of Bothrombin, a Fibrinogen-Clotting Serine Protease from the Venom of Bothrops jararaca
inferredcites →https://doi.org/10.1021/bi060217ropenalex-snapshot
Neurotoxicity and Other Pharmacological Activities of the Snake Venom Phospholipase A2OS2: The N-Terminal Region Is More Important Than Enzymatic Activity
inferredcites →https://doi.org/10.1038/nmeth.4147openalex-snapshot
High-fidelity mass analysis unveils heterogeneity in intact ribosomal particles
inferredcites →https://doi.org/10.1038/nrdp.2017.79openalex-snapshot
Correction: Snakebite envenoming
inferredcites →https://doi.org/10.1038/nsmb892openalex-snapshot
The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation
inferredcites →https://doi.org/10.1038/s41467-018-07480-8openalex-snapshot
Publisher Correction: In vivo neutralization of dendrotoxin-mediated neurotoxicity of black mamba venom by oligoclonal human IgG antibodies
inferredcites →https://doi.org/10.1038/s42003-018-0039-1openalex-snapshot
The paraspecific neutralisation of snake venom induced coagulopathy by antivenoms
inferredcites →https://doi.org/10.1039/c7an01629hopenalex-snapshot
Expanding the structural analysis capabilities on an Orbitrap-based mass spectrometer for large macromolecular complexes
inferredcites →https://doi.org/10.1042/bj2940387openalex-snapshot
Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma
inferredcites →https://doi.org/10.1046/j.1432-1327.1998.2510845.xopenalex-snapshot
Purification and characterization of a kinin‐releasing and fibrinogen‐clotting serine proteinase (KN‐BJ) from the venom of Bothrops jararaca, and molecular cloning and sequence analysis of its cDNA
inferredcites →https://doi.org/10.1046/j.1432-1327.2000.01766.xopenalex-snapshot
Phospholipases A2 from Callosellasma rhodostoma venom gland
inferredcites →https://doi.org/10.1073/pnas.1405484111openalex-snapshot
Medically important differences in snake venom composition are dictated by distinct postgenomic mechanisms
inferredcites →https://doi.org/10.1074/jbc.271.9.5200openalex-snapshot
Isolation and Characterization of Carinactivase, a Novel Prothrombin Activator in Echis carinatus Venom with a Unique Catalytic Mechanism
inferredcites →https://doi.org/10.1093/molbev/msu337openalex-snapshot
Venom-Related Transcripts from Bothrops jararaca Tissues Provide Novel Molecular Insights into the Production and Evolution of Snake Venom
inferredcites →https://doi.org/10.1093/oxfordjournals.qjmed.a030134openalex-snapshot
Neurotoxicity, anticoagulant activity and evidence of rhabdomyolysis in patients bitten by death adders (Acanthophis sp.) in southern Papua New Guinea
inferredcites →https://doi.org/10.1107/s0907444902003645openalex-snapshot
Crystallization of bothrombin, a fibrinogen-converting serine protease isolated from the venom ofBothrops jararaca
inferredcites →https://doi.org/10.1111/bcp.12739openalex-snapshot
Adverse reactions to snake antivenom, and their prevention and treatment
inferredcites →https://doi.org/10.1111/bjh.14591openalex-snapshot
Haemotoxic snake venoms: their functional activity, impact on snakebite victims and pharmaceutical promise
inferredcites →https://doi.org/10.1111/j.1742-4658.2012.08691.xopenalex-snapshot
Structural analysis of trimeric phospholipase A2 neurotoxin from the Australian taipan snake venom
inferredcites →https://doi.org/10.1124/mol.107.038018openalex-snapshot
Antithrombotic Effect of a Protein-Type I Class Snake Venom Metalloproteinase, Kistomin, Is Mediated by Affecting Glycoprotein Ib-von Willebrand Factor Interaction
inferredcites →https://doi.org/10.1126/scitranslmed.aay8314openalex-snapshot
Preclinical validation of a repurposed metal chelator as an early-intervention therapeutic for hemotoxic snakebite
inferredcites →https://doi.org/10.1145/1978942.1978963openalex-snapshot
The aligned rank transform for nonparametric factorial analyses using only anova procedures
inferredcites →https://doi.org/10.1159/000048066openalex-snapshot
Procoagulant Proteins from Snake Venoms
inferredcites →https://doi.org/10.1159/000048067openalex-snapshot
Snake Venom Activators of Factor X: An Overview
inferredcites →https://doi.org/10.1159/000092424openalex-snapshot
Serine Proteases Affecting Blood Coagulation and Fibrinolysis from Snake Venoms
inferredcites →https://doi.org/10.1186/1472-6807-7-82openalex-snapshot
Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics
inferredcites →https://doi.org/10.1201/9781420008661-14openalex-snapshot
Snake Venom Phospholipase A2 Enzymes
inferredcites →https://doi.org/10.1371/journal.pmed.0050218openalex-snapshot
The Global Burden of Snakebite: A Literature Analysis and Modelling Based on Regional Estimates of Envenoming and Deaths
inferredcites →https://doi.org/10.1371/journal.pntd.0000851openalex-snapshot
Pre-Clinical Assays Predict Pan-African Echis Viper Efficacy for a Species-Specific Antivenom
inferredcites →https://doi.org/10.1371/journal.pntd.0001670openalex-snapshot
Consequences of Neglect: Analysis of the Sub-Saharan African Snake Antivenom Market and the Global Context
inferredcites →https://doi.org/10.1371/journal.pntd.0003220openalex-snapshot
Current Treatment for Venom-Induced Consumption Coagulopathy Resulting from Snakebite
inferredcites →https://doi.org/10.1371/journal.pntd.0004088openalex-snapshot
Snakebite is Under Appreciated: Appraisal of Burden from West Africa
inferredcites →https://doi.org/10.1371/journal.pntd.0005969openalex-snapshot
Preclinical antivenom-efficacy testing reveals potentially disturbing deficiencies of snakebite treatment capability in East Africa
inferredcites →https://doi.org/10.2174/1568006043335916openalex-snapshot
C-type Lectin-related Proteins from Snake Venoms
inferredcites →https://doi.org/10.2220/biomedres.31.71openalex-snapshot
Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka
inferredcites →https://doi.org/10.3389/fevo.2019.00218openalex-snapshot
Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis
inferredcites →https://doi.org/10.3390/toxins10100411openalex-snapshot
Coagulotoxicity of Bothrops (Lancehead Pit-Vipers) Venoms from Brazil: Differential Biochemistry and Antivenom Efficacy Resulting from Prey-Driven Venom Variation
inferredcites →https://doi.org/10.3390/toxins8090248openalex-snapshot
Varespladib (LY315920) Appears to Be a Potent, Broad-Spectrum, Inhibitor of Snake Venom Phospholipase A2 and a Possible Pre-Referral Treatment for Envenomation
inferredcites →https://doi.org/10.3390/toxins8100284openalex-snapshot
Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites
inferredcites →https://doi.org/10.3390/toxins9050171openalex-snapshot
Coagulating Colubrids: Evolutionary, Pathophysiological and Biodiscovery Implications of Venom Variations between Boomslang (Dispholidus typus) and Twig Snake (Thelotornis mossambicanus)
inferredcites →https://doi.org/10.3390/toxins9110347openalex-snapshot
Single Chain Antibody Fragment against Venom from the Snake Daboia russelii formosensis
inferredcites →https://doi.org/10.3390/toxins9120382openalex-snapshot
Multipurpose HTS Coagulation Analysis: Assay Development and Assessment of Coagulopathic Snake Venoms
inferredcites →https://doi.org/10.3390/tropicalmed3020042openalex-snapshot
Recent Advances in Next Generation Snakebite Antivenoms
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1016/j.toxicon.2020.02.015openalex-snapshot
Development of a generic high-throughput screening assay for profiling snake venom protease activity after high-resolution chromatographic fractionation
inferred← citeshttps://doi.org/10.1016/j.toxicon.2020.05.022openalex-snapshot
Development of high-throughput screening assays for profiling snake venom phospholipase A2 activity after chromatographic fractionation
inferred← citeshttps://doi.org/10.1038/s41596-020-00463-4openalex-snapshot
Derivation of snake venom gland organoids for in vitro venom production
inferred← citeshttps://doi.org/10.3390/toxins12010053openalex-snapshot
Antivenom Neutralization of Coagulopathic Snake Venom Toxins Assessed by Bioactivity Profiling Using Nanofractionation Analytics
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