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Comparative Analysis of the Venom Proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/pmic.200402024openalex-snapshot

Snake venomics: Comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes , Cerastes vipera and Macrovipera lebetina

inferredcites →https://doi.org/10.1006/abbi.1996.9814openalex-snapshot

Complete Amino Acid Sequence of an Acidic, Cardiotoxic Phospholipase A2from the Venom ofOphiophagus hannah(King Cobra): A Novel Cobra Venom Enzyme with “Pancreatic Loop”

inferredcites →https://doi.org/10.1007/s000180050440openalex-snapshot

Modulation of phospholipase A 2 activity generated by molecular evolution

inferredcites →https://doi.org/10.1016/0041-0101(76)90065-9openalex-snapshot

Action on phosphatidylcholine of the toxic phospholipase A2 from the venom of Bulgarian viper (Vipera ammodytes ammodytes)

inferredcites →https://doi.org/10.1016/0041-0101(78)90058-2openalex-snapshot

A neurotoxic complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes) and a partial amino acid sequence of the toxic phospholipase A2

inferredcites →https://doi.org/10.1016/0076-6879(71)17104-2openalex-snapshot

[218a] Assay of amino acid oxidase

inferredcites →https://doi.org/10.1016/0300-9084(96)82187-0openalex-snapshot

Biochemical characterization of a new disintegrin, flavostatin, isolated from Trimeresurus flavoviridis venom

inferredcites →https://doi.org/10.1016/j.bbrc.2004.01.174openalex-snapshot

The X-ray structure of a snake venom Gln48 phospholipase A2 at 1.9Å resolution reveals anion-binding sites

inferredcites →https://doi.org/10.1016/j.bbrc.2004.05.106openalex-snapshot

Asp49 phospholipase A(2)-elaidoylamide complex: a new mode of inhibition.

inferredcites →https://doi.org/10.1016/j.biochi.2006.06.008openalex-snapshot

Binding to the high-affinity M-type receptor for secreted phospholipases A2 is not obligatory for the presynaptic neurotoxicity of ammodytoxin A

inferredcites →https://doi.org/10.1016/j.ejim.2005.10.001openalex-snapshot

Snake venom poisoning in Greece. Experiences with 147 cases

inferredcites →https://doi.org/10.1016/j.toxicon.2004.05.023openalex-snapshot

Structure and function of snake venom cysteine-rich secretory proteins

inferredcites →https://doi.org/10.1016/j.toxicon.2006.12.003openalex-snapshot

Ammodytase, a metalloprotease from Vipera ammodytes ammodytes venom, possesses strong fibrinolytic activity

inferredcites →https://doi.org/10.1016/s0006-3495(04)74123-5openalex-snapshot

Interactions of the Neurotoxin Vipoxin in Solution Studied by Dynamic Light Scattering

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/s0041-0101(01)00188-xopenalex-snapshot

Purification and characterisation of two hemorrhagic metalloproteinases from the venom of the long-nosed viper, Vipera ammodytes ammodytes

inferredcites →https://doi.org/10.1016/s0041-0101(02)00102-2openalex-snapshot

Snake venom l-amino acid oxidases

inferredcites →https://doi.org/10.1016/s0041-0101(96)00116-xopenalex-snapshot

Procoagulant and platelet-aggregating properties of cerastocytin from Cerastes cerastes venom

inferredcites →https://doi.org/10.1021/pr0602500openalex-snapshot

Venom Proteomes of Closely RelatedSistrurusRattlesnakes with Divergent Diets

inferredcites →https://doi.org/10.1021/pr060494kopenalex-snapshot

Snake Venomics ofBitis gabonica gabonica. Protein Family Composition, Subunit Organization of Venom Toxins, and Characterization of Dimeric Disintegrins Bitisgabonin-1 and Bitisgabonin-2

inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

inferredcites →https://doi.org/10.1038/ismej.2007.39openalex-snapshot

Functional metaproteome analysis of protein extracts from contaminated soil and groundwater

inferredcites →https://doi.org/10.1042/bj20021739openalex-snapshot

Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering

inferredcites →https://doi.org/10.1042/bj3410139openalex-snapshot

An aromatic, but not a basic, residue is involved in the toxicity of group-II phospholipase A2 neurotoxins

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.1525-1373.1999.d01-122.xopenalex-snapshot

Role of Integrins in Cancer: Survey of Expression Patterns

inferredcites →https://doi.org/10.1073/pnas.131179698openalex-snapshot

Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X

inferredcites →https://doi.org/10.1074/jbc.c300454200openalex-snapshot

Snake Venom Vascular Endothelial Growth Factors (VEGFs) Exhibit Potent Activity through Their Specific Recognition of KDR (VEGF Receptor 2)

inferredcites →https://doi.org/10.1074/jbc.m508502200openalex-snapshot

Thrombomodulin-independent Activation of Protein C and Specificity of Hemostatically Active Snake Venom Serine Proteinases

inferredcites →https://doi.org/10.1093/molbev/msi077openalex-snapshot

Putting the Brakes on Snake Venom Evolution: The Unique Molecular Evolutionary Patterns of Aipysurus eydouxii (Marbled Sea Snake) Phospholipase A2 Toxins

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a126856openalex-snapshot

CRYSTALLINE BACTERIAL PROTEINASE

inferredcites →https://doi.org/10.1107/s0907444901013543openalex-snapshot

Structure of the neurotoxic complex vipoxin at 1.4 Å resolution

inferredcites →https://doi.org/10.1111/j.1432-1033.1992.tb16728.xopenalex-snapshot

Amino acid and cDNA sequences of a neutral phospholipase A2 from the long‐nosed viper (Vipera ammodytes ammodytes) venom

inferredcites →https://doi.org/10.1159/000092426openalex-snapshot

Vipera lebetina Venom Contains All Types of Snake Venom Metalloproteases

inferredcites →https://doi.org/10.1515/bchm2.1984.365.2.885openalex-snapshot

Sequence Homology between Phospholipase and its Inhibitor in Snake Venom. The Primary Structure of the Inhibitor of Vipoxin from the Venom of the Bulgarian Viper (Vipera ammodytes ammodytes,Serpentes)

inferredcites →https://doi.org/10.1515/bchm3.1987.368.1.343openalex-snapshot

Sequence Homology between Phospholipase and its Inhibitor in Snake Venom. The Primary Structure of Phospholipase A2of Vipoxin from the Venom of the Bulgarian Viper (Vipera ammodytes ammodytes,Serpentes)

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.11646/zootaxa.5537.1.2zenodo-depositor-declared

Assessment of the Linnaean type material of the Nose-horned viper, Vipera ammodytes (Linnaeus, 1758)

inferred← citeshttps://doi.org/10.11646/zootaxa.5696.3.4zenodo-depositor-declared

Nomenclatural historians are kindly requested to respect the intent of the Code: “Nomenclatural parsimony” and the case of the Nose-horned Viper, Vipera ammodytes (Linnaeus, 1758)

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Incorporation of carbon and nitrogen atoms into proteins measured by protein‐based stable isotope probing (Protein‐SIP)

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Snake Venomics, Antivenomics, and Venom Phenotyping: The Ménage à Trois of Proteomic Tools Aimed at Understanding the Biodiversity of Venoms

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Developing Snake Antivenom Sera by Genetic Immunization: A Review

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Developing Snake Antivenom Sera by Genetic Immunization: A Review

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Structure-Function Relationship in Heterodimeric Neurotoxin PLA2s from Viperidae Snakes Inhabiting Europe, South America, and Asia

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Snake Venom Proteopeptidomics: What Lies Behind the Curtain

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Structure-Function Relationship in Heterodimeric Neurotoxin PLA2s from Viperidae Snakes Inhabiting Europe, South America, and Asia

inferred← citeshttps://doi.org/10.1007/978-94-007-6649-5_6-1openalex-snapshot

Snake Venom Proteopeptidomics: What Lies Behind the Curtain

inferred← citeshttps://doi.org/10.1007/s00216-013-7453-5openalex-snapshot

Identification of proteins interacting with ammodytoxins in Vipera ammodytes ammodytes venom by immuno-affinity chromatography

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The benefits of active substances in amphibians and reptiles and the jeopardy of losing those species forever

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Comparison and optimization of methods for the simultaneous extraction of DNA, RNA, proteins, and metabolites

inferred← citeshttps://doi.org/10.1016/j.biochi.2015.11.031openalex-snapshot

A novel synthetic quinolinone inhibitor presents proteolytic and hemorrhagic inhibitory activities against snake venom metalloproteases

inferred← citeshttps://doi.org/10.1016/j.cbd.2020.100776openalex-snapshot

Study of the venom proteome of Vipera ammodytes ammodytes (Linnaeus, 1758): A qualitative overview, biochemical and biological profiling

inferred← citeshttps://doi.org/10.1016/j.febslet.2009.03.029openalex-snapshot

Venoms, venomics, antivenomics

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Snake venomics of the Siamese Russell's viper (Daboia russelli siamensis) — Relation to pharmacological activities

inferred← citeshttps://doi.org/10.1016/j.jprot.2011.05.027openalex-snapshot

Ending the drought: New strategies for improving the flow of affordable, effective antivenoms in Asia and Africa

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Venomics of Vipera berus berus to explain differences in pathology elicited by Vipera ammodytes ammodytes envenomation: Therapeutic implications

inferred← citeshttps://doi.org/10.1016/j.jprot.2020.103707openalex-snapshot

Venomics of the asp viper Vipera aspis aspis from France

inferred← citeshttps://doi.org/10.1016/j.jprot.2024.105320openalex-snapshot

Ontogeny, not prey availability, underlies allopatric venom variability in insular and mainland populations of Vipera ammodytes

inferred← citeshttps://doi.org/10.1016/j.jsb.2009.10.010openalex-snapshot

Comparative structural studies of two natural isoforms of ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which differ in neurotoxicity and anticoagulant activity☆

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Benzo[a]pyrene affects Jurkat T cells in the activated state via the antioxidant response element dependent Nrf2 pathway leading to decreased IL-2 secretion and redirecting glutamine metabolism

inferred← citeshttps://doi.org/10.1016/j.tox.2021.152724openalex-snapshot

Vipers of Major clinical relevance in Europe: Taxonomy, venom composition, toxicology and clinical management of human bites

inferred← citeshttps://doi.org/10.1016/j.toxicon.2009.06.010openalex-snapshot

Proteomic profiling of snake venom metalloproteinases (SVMPs): Insights into venom induced pathology

inferred← citeshttps://doi.org/10.1016/j.toxicon.2011.06.009openalex-snapshot

Ammodytoxin: A window into understanding presynaptic toxicity of secreted phospholipases A2 and more

inferred← citeshttps://doi.org/10.1016/j.toxicon.2012.03.009openalex-snapshot

The standard mouse assay of anti-venom quality does not measure antibodies neutralising the haemorrhagic activity of Vipera ammodytes venom

inferred← citeshttps://doi.org/10.1016/j.toxicon.2012.06.003openalex-snapshot

Recognition of Vipera ammodytes meridionalis neurotoxin vipoxin and its components using phage-displayed scFv and polyclonal antivenom sera

inferred← citeshttps://doi.org/10.1016/j.toxicon.2012.08.010openalex-snapshot

Proteomic profiling of dog urine after European adder (Vipera berus berus) envenomation by two-dimensional difference gel electrophoresis

inferred← citeshttps://doi.org/10.1016/j.toxicon.2012.09.004openalex-snapshot

Snake venom metalloproteinases

inferred← citeshttps://doi.org/10.1016/j.toxicon.2013.03.020openalex-snapshot

Snake venomics: From the inventory of toxins to biology

inferred← citeshttps://doi.org/10.1016/j.toxicon.2014.10.004openalex-snapshot

Testing the Toxicofera: Comparative transcriptomics casts doubt on the single, early evolution of the reptile venom system

inferred← citeshttps://doi.org/10.1016/j.toxicon.2016.09.001openalex-snapshot

Cardiotoxic effects of the Vipera ammodytes ammodytes venom fractions in the isolated perfused rat heart

inferred← citeshttps://doi.org/10.1016/j.toxicon.2017.10.003openalex-snapshot

Ammodytin L is the main cardiotoxic component of the Vipera ammodytes ammodytes venom

inferred← citeshttps://doi.org/10.1016/j.toxicon.2021.01.012openalex-snapshot

MTT based L-aminoacid oxidase activity test for determination of antivenom potency against Vipera ammodytes envenomation

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Composition characterization of various viperidae snake venoms using MS-based proteomics N-glycoproteomics and N-glycomics

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Beyond sexual maturity: Importance of dietary changes in venom variation in Vipera ammodytes

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Investigation of paraspecific effects of polyvalent snake antivenom on the venom of three vipers (Vipera berus berus; Linnaeus 1758, Vipera ammodytes ammodytes; Linnaeus, 1758 and Montivipera raddei; Boettger, 1890)

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First insights into the role of evolutionary history in shaping venom composition of Vipera ammodytes

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Resistance towards monensin is proposed to be acquired in aToxoplasma gondiimodel by reduced invasion and egress activities, in addition to increased intracellular replication

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Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins

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Chlorinated Benzenes Cause Concomitantly Oxidative Stress and Induction of Apoptotic Markers in Lung Epithelial Cells (A549) at Nonacute Toxic Concentrations

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DIGE-Based Protein Expression Analysis of B[a]P-Exposed Hepatoma Cells Reveals a Complex Stress Response Including Alterations in Oxidative Stress, Cell Cycle Control, and Cytoskeleton Motility at Toxic and Subacute Concentrations

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The Venomics of Bothrops alternatus is a Pool of Acidic Proteins with Predominant Hemorrhagic and Coagulopathic Activities

inferred← citeshttps://doi.org/10.1038/ismej.2008.64openalex-snapshot

Protein-based stable isotope probing (Protein-SIP) reveals active species within anoxic mixed cultures

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The structure of a native l -amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions

inferred← citeshttps://doi.org/10.1039/c1mb05309dopenalex-snapshot

Venom peptide analysis of Vipera ammodytes meridionalis (Viperinae) and Bothrops jararacussu (Crotalinae) demonstrates subfamily-specificity of the peptidome in the family Viperidae

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Crystal structure of a dimeric Ser49 PLA2-like myotoxic component of the Vipera ammodytes meridionalis venomics reveals determinants of myotoxicity and membrane damaging activity

inferred← citeshttps://doi.org/10.1097/md.0000000000013737openalex-snapshot

Thrombocytopenic purpura following envenomation by the nose-horned viper (Vipera ammodytes ammodytes)

inferred← citeshttps://doi.org/10.1107/s1744309108027036openalex-snapshot

Isolation, crystallization and preliminary X-ray diffraction analysis of L -amino-acid oxidase fromVipera ammodytes ammodytesvenom

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The new peptide from the Fea’s viper Azemiops feae venom interacts with nicotinic acetylcholine receptors

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Production and assessment of ovine antisera for the manufacture of a veterinary adder antivenom

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Mass spectrometry in snake venom research

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Screening of cytotoxic, anti-angiogenic, anti-tumorogenic and antimicrobial activities of Anatolian Vipera ammodytes (Nose-horned viper) venom

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Next-generation snake venomics: protein-locus resolution through venom proteome decomplexation

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De novo genome assembly of Vipera ammodytes ammodytes reveals venom gene expansion and ecological adaptations

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Venom-Induced Blood Disturbances by Palearctic Viperid Snakes, and Their Relative Neutralization by Antivenoms and Enzyme-Inhibitors

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A Pseudoenzymatic Regulatory Role of the Noncatalytic Subunit of the Neurotoxin Vipoxin at Arachidonic-Acid-Containing Membrane Interfaces

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Comparative Venomics of the Vipera ammodytes transcaucasiana and Vipera ammodytes montandoni from Turkey Provides Insights into Kinship

inferred← citeshttps://doi.org/10.3390/toxins10070259openalex-snapshot

Effect of Vipera ammodytes ammodytes Snake Venom on the Human Cytokine Network

inferred← citeshttps://doi.org/10.3390/toxins13060427openalex-snapshot

Old World Vipers—A Review about Snake Venom Proteomics of Viperinae and Their Variations

inferred← citeshttps://doi.org/10.3390/toxins16060255openalex-snapshot

A Guide to the Clinical Management of Vipera Snakebite in Italy

inferred← citeshttps://doi.org/10.3390/toxins16090396openalex-snapshot

Tiny but Mighty: Vipera ammodytes meridionalis (Eastern Long-Nosed Viper) Ontogenetic Venom Variations in Procoagulant Potency and the Impact on Antivenom Efficacies

inferred← citeshttps://doi.org/10.3390/toxins17040193openalex-snapshot

Electrical Cell Impedance Sensing (ECIS): Feasibility of a Novel In Vitro Approach to Studying Venom Toxicity and Potential Therapeutics

inferred← citeshttps://doi.org/10.3390/toxins8040105openalex-snapshot

Quantitative Proteomic Analysis of Venoms from Russian Vipers of Pelias Group: Phospholipases A2 are the Main Venom Components

inferred← citeshttps://doi.org/10.3390/vetsci11120605openalex-snapshot

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inferred← citeshttps://doi.org/10.5114/ceji.2024.142417openalex-snapshot

Comparison of cytotoxicity methods for studying Vipera ammodytes venom and the anticytotoxic potency of antivenom

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Large-scale 2-D DIGE studies - guidelines to overcome pitfalls and challenges along the experimental procedure

inferred← citeshttps://doi.org/10.59313/jsr-a.1323404openalex-snapshot

EFFECT OF TEMPERATURE ON THE PROTEIN PROFILE OF MACROVIPERA LEBETINUS (BLUNT-NOSED VIPER) VENOM: A PRELIMINARY STUDY

inferred← citeshttps://doi.org/10.61215/nwjz.2026.22.1.07openalex-snapshot

In vitro cellular effects of Montivipera xanthina and Vipera ammodytes meridionalis venoms

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Les venins animaux comme outils de recherche et d'identification de nouveaux composés thérapeutiques

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Synthèse de peptides bioactifs inspirés des venins

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