Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (1795) 1795
Publication (128) 128
Book Chapter (36) 36
Newsletter (15) 15
Book / eBook (10) 10
Book Review (9) 9
Newspaper Article (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
animals (1489) 1489
snakes (537) 537
index medicus (508) 508
biochemistry & molecular biology (477) 477
amino acid sequence (471) 471
humans (468) 468
venom (420) 420
molecular sequence data (411) 411
snake venom (385) 385
toxicology (384) 384
crotalid venoms - enzymology (362) 362
mice (347) 347
snake venoms - enzymology (343) 343
pharmacology & pharmacy (327) 327
venoms (302) 302
snake-venom (280) 280
male (258) 258
purification (250) 250
proteins (222) 222
kinetics (220) 220
base sequence (198) 198
enzymes (198) 198
rats (195) 195
snake venoms (183) 183
electrophoresis, polyacrylamide gel (181) 181
molecular weight (180) 180
phospholipases a2 (166) 166
bothrops (164) 164
phospholipase a (155) 155
viper venoms - enzymology (153) 153
hydrogen-ion concentration (150) 150
cattle (148) 148
pancreas - enzymology (148) 148
sequence homology, amino acid (146) 146
analysis (135) 135
chromatography, gel (130) 130
substrate specificity (130) 130
crotalid venoms - chemistry (125) 125
sequence alignment (119) 119
biophysics (115) 115
chromatography, ion exchange (113) 113
models, molecular (111) 111
hydrolysis (108) 108
fibrinogen - metabolism (106) 106
amino-acid-sequence (105) 105
chemistry (105) 105
phosphoric diester hydrolases (105) 105
metalloproteinase (104) 104
cloning, molecular (103) 103
crotalid venoms - toxicity (102) 102
species specificity (101) 101
hemorrhage - chemically induced (100) 100
phospholipases (99) 99
structure-activity relationship (99) 99
proteases (97) 97
time factors (96) 96
escherichia coli - enzymology (95) 95
female (94) 94
elapid venoms - enzymology (92) 92
phospholipases a - metabolism (91) 91
metalloproteases - chemistry (88) 88
amino acids (87) 87
poisonous snakes (86) 86
binding sites (85) 85
chromatography, high pressure liquid (84) 84
metalloproteases - metabolism (84) 84
phospholipases a2 - chemistry (84) 84
rabbits (83) 83
chromatography, thin layer (82) 82
dose-response relationship, drug (82) 82
mass spectrometry (82) 82
snake-venoms (82) 82
phospholipases a - chemistry (81) 81
viperidae (81) 81
phylogeny (79) 79
metalloendopeptidases - chemistry (78) 78
protein conformation (78) 78
in vitro techniques (77) 77
platelet aggregation - drug effects (77) 77
research article (77) 77
chemical phenomena (76) 76
medicine (76) 76
ribonucleases (75) 75
peptides (74) 74
protein (74) 74
blood coagulation - drug effects (73) 73
fibrin (72) 72
fibrinogen (72) 72
platelet-aggregation (72) 72
methods (71) 71
temperature (71) 71
biochemistry (70) 70
phospholipase a2 (70) 70
spleen - enzymology (70) 70
cloning (69) 69
molecular-cloning (69) 69
crystal-structure (67) 67
enzyme activation (67) 67
protein binding (67) 67
thrombin (65) 65
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (1787) 1787
Russian (14) 14
German (10) 10
French (7) 7
Japanese (3) 3
Chinese (1) 1
Czech (1) 1
Finnish (1) 1
Norwegian (1) 1
Spanish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Snake venom metalloproteinases
by Markland, Francis S and Swenson, Stephen
Toxicon, ISSN 0041-0101, 02/2013, Volume 62, pp. 3 - 18
Recent proteomic analyses of snake venoms show that metalloproteinases represent major components in most of the and venoms. In this chapter we discuss the... 
Prothrombin activators | Hemorrhagic metalloproteinases | X-ray crystallography | Fibrolase/alfimeprase | Fibrinolytic metalloproteinases | Factor X activators | HEMORRHAGIC TOXIN-E | PLATELET-AGGREGATION INHIBITOR | ADAMANTEUS PROTEINASE-II | ACTING FIBRINOLYTIC ENZYME | VIPERA-LEBETINA VENOM | CROTALUS-ATROX VENOM | AGKISTRODON-CONTORTRIX-CONTORTRIX | AMINO-ACID-SEQUENCE | BOTHROPS-JARARACA VENOM | WESTERN DIAMONDBACK RATTLESNAKE | PHARMACOLOGY & PHARMACY | TOXICOLOGY | Consensus Sequence | Fibrinolytic Agents - classification | Protein Structure, Tertiary | Fibrinolytic Agents - chemistry | Metalloproteases - isolation & purification | Metalloproteases - pharmacology | Crystallography, X-Ray | Snake Venoms - enzymology | Fibrinolytic Agents - isolation & purification | Fibrinolytic Agents - pharmacology | Proteomics | Hydrophobic and Hydrophilic Interactions | Metalloproteases - classification | Metalloproteases - chemistry | Fibrin | Thrombin | Structure | Venom | Crystals | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity
by Fox, Jay W and Serrano, Solange M. T
FEBS Journal, ISSN 1742-464X, 06/2008, Volume 275, Issue 12, pp. 3016 - 3030
As more data are generated from proteome and transcriptome analyses of snake venoms, we are gaining an appreciation of the complexity of the venoms and, to... 
disulfide bond | metalloproteinase | proteome snake venom | disintegrin | post‐translational processing | SVMP transcriptome | structure | autolysis | Autolysis | Proteome snake venom | Disintegrin | Disulfide bond | Metalloproteinase | Structure | Post-translational processing | PLATELET-AGGREGATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AGKISTRODON-ACUTUS | VON-WILLEBRAND-FACTOR | CROTALUS-ATROX VENOM | post-translational processing | CYSTEINE-RICH DOMAIN | AMINO-ACID-SEQUENCE | BOTHROPS-JARARACA VENOM | TRIMERESURUS-FLAVOVIRIDIS | HEMORRHAGIC METALLOPROTEASE | Protein Structure, Tertiary | Amino Acid Sequence | Sequence Alignment | Animals | Disulfides - chemistry | Viper Venoms - enzymology | Molecular Sequence Data | Protein Processing, Post-Translational | Metalloproteases - classification | Metalloproteases - chemistry | Metalloproteases - metabolism | Protein Folding | Venom | Chemical bonds | Toxicology | Biochemistry | Protein folding | Snakes | Genomics
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. Full Text The effects of hybridization on divergent venom phenotypes: Characterization of venom from Crotalus scutulatus scutulatus × Crotalus oreganus helleri hybrids
by Smith, Cara Francesca and Mackessy, Stephen P
Toxicon, ISSN 0041-0101, 09/2016, Volume 120, pp. 110 - 123
Hybridization between divergent species can be analyzed to elucidate expression patterns of distinct parental characteristics, as well as to provide... 
Western blot | Enzymes | MALDI-TOF MS | Metalloprotease | Serine protease | Mojave toxin | HPLC | Phosphodiesterase | Serine Proteases - metabolism | Phosphoric Diester Hydrolases - metabolism | Electrophoresis, Polyacrylamide Gel | Male | Crotalid Venoms - enzymology | Chromatography, High Pressure Liquid | Blotting, Western | Metalloproteases - metabolism | Animals | Crotalid Venoms - genetics | Crotalus - classification | Hybridization, Genetic | Crotalus - genetics | Female | Crotalid Venoms - chemistry | Crotalid Venoms - toxicity | Index Medicus | Hybrid systems | Ontogeny | Toxins | Enzymology | Males | Females | Snakes | Information dissemination
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
4. Full Text Comparative venom gland transcriptome surveys of the saw-scaled vipers (Viperidae: Echis) reveal substantial intra-family gene diversity and novel venom transcripts
by Casewell, Nicholas R and Harrison, Robert A and Wüster, Wolfgang and Wagstaff, Simon C
BMC Genomics, ISSN 1471-2164, 11/2009, Volume 10, Issue 1, pp. 564 - 564
Background: Venom variation occurs at all taxonomical levels and can impact significantly upon the clinical manifestations and efficacy of antivenom therapy... 
CARINATUS VENOM | SNAKE-VENOM | DIPEPTIDYL-PEPTIDASE-III | ACCELERATED EVOLUTION | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | ACIDIC PHOSPHOLIPASE A | GENETICS & HEREDITY | SYNAPTIC-MEMBRANES | CARPET VIPER | EXPRESSED SEQUENCE TAGS | ADAPTIVE EVOLUTION | PHARMACOLOGICAL-PROPERTIES | Adaptation, Physiological | Viper Venoms - genetics | Viper Venoms - enzymology | Humans | RNA, Messenger - genetics | Viperidae - metabolism | Databases, Genetic | RNA, Messenger - analysis | Viper Venoms - secretion | Gene Expression Profiling | Genetic Variation | Viperidae - physiology | Animals | Viper Venoms - metabolism | Expressed Sequence Tags - metabolism | Viperidae - genetics | Genetic aspects | Research | Genetic transcription | Venom | Biological diversity | Proteins | Diet | Mortality | Colleges & universities | Snakes | Experiments | Data bases | Manuscripts | Adaptations | protein families | Triacylglycerol lipase | Blast | Gene expression | Natural selection | Recruitment | Diets | Antivenom | peptidase | Venom gland | Chromium | Lectins | Evolution | Metalloproteinase | Neprilysin | Serine proteinase | Toxins | expressed sequence tags
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Proteomics and antivenomics of Echis carinatus carinatus venom: Correlation with pharmacological properties and pathophysiology of envenomation
by Patra, Aparup and Kalita, Bhargab and Chanda, Abhishek and Mukherjee, Ashis K
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 17119 - 17
The proteome composition of Echis carinatus carinatus venom (ECV) from India was studied for the first time by tandem mass spectrometry analysis. A total of... 
NAJA-NAJA | SNAKE-VENOM | C-TYPE LECTIN | PLATELET-AGGREGATION | SHOTGUN PROTEOMICS | MULTIDISCIPLINARY SCIENCES | DABOIA-RUSSELII-RUSSELII | PHOSPHOLIPASE A | ANTICOAGULANT ACTIVITY | ENZYMATIC-ACTIVITY | SAW-SCALED VIPER | Elapid Venoms - chemistry | Hemolysis - drug effects | Intercellular Signaling Peptides and Proteins - analysis | Goats | Antivenins - immunology | Viper Venoms - enzymology | Elapid Venoms - enzymology | Elapid Venoms - immunology | Viper Venoms - pharmacology | Peptide Hydrolases - analysis | Elapid Venoms - pharmacology | Proteome - chemistry | Viper Venoms - chemistry | Animals | Blood Coagulation - drug effects | Viper Venoms - immunology | Reptilian Proteins - analysis | Phospholipase A2 | Cross-reactivity | Nerve growth factor | Mass spectroscopy | Gene expression | Snakes | Proteins | Phospholipase | Antivenom | Venom | Aspartic endopeptidase | Proteomics | Aminopeptidase | Growth factors | Vascular endothelial growth factor | Protein families
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text Snake venom: From fieldwork to the clinic: Recent insights into snake biology, together with new technology allowing high-throughput screening of venom, bring new hope for drug discovery
by Vonk, Freek J and Jackson, Kate and Doley, Robin and Madaras, Frank and Mirtschin, Peter J and Vidal, Nicolas
BioEssays, ISSN 0265-9247, 04/2011, Volume 33, Issue 4, pp. 269 - 279
Snake venoms are recognized here as a grossly under-explored resource in pharmacological prospecting. Discoveries in snake systematics demonstrate that former... 
Drug | Screening | Toxin | Snake | Venom | Snake Venoms - genetics | Snake Venoms - therapeutic use | Humans | Phylogeography | Phylogeny | Snake Venoms - enzymology | Drug Discovery | Biological Evolution | Snakes - genetics | Snakes - metabolism | Animals | Endangered Species | Evolution, Molecular | High-Throughput Screening Assays - methods
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text Differential evolution and neofunctionalization of snake venom metalloprotease domains (Molecular and Cellular Proteomics 2013, 12, (651-663))
by Brust, Andreas and Sunagar, Kartik and Undheim, Eivind A. B and Vetter, Irina and Yang, Daryl C and Casewell, Nicholas R and Jackson, Timothy N. W and Koludarov, Ivan and Alewood, Paul F and Hodgson, Wayne C and Lewis, Richard J and King, Glenn F and Antunes, Agostinho and Hendrikx, Iwan and Fry, Bryan G
Molecular and Cellular Proteomics, ISSN 1535-9476, 05/2013, Volume 12, Issue 5, pp. 1488 - 1488
Snake venom metalloproteases (SVMP) are composed of five domains: signal peptide, propeptide, metalloprotease, disintegrin, and cysteine-rich. Secreted toxins... 
BIOCHEMICAL RESEARCH METHODS | Snake Venoms - genetics | Species Specificity | Protein Precursors - chemistry | Humans | Molecular Sequence Data | Nicotinic Antagonists - pharmacology | Phylogeny | Snake Venoms - enzymology | Metalloproteases - metabolism | Dose-Response Relationship, Drug | Metalloproteases - classification | Protein Structure, Tertiary | Amino Acid Sequence | Snake Venoms - classification | Receptors, Nicotinic - metabolism | Protein Precursors - genetics | Selection, Genetic | Metalloproteases - genetics | Models, Molecular | Binding Sites - genetics | Peptides - pharmacology | Protein Precursors - metabolism | Sequence Homology, Amino Acid | Animals | Cell Line, Tumor | Mutation | Evolution, Molecular | alpha7 Nicotinic Acetylcholine Receptor | Additions and s
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text Phospholipases A2: Unveiling the secrets of a functionally versatile group of snake venom toxins
by Gutiérrez, José María and Lomonte, Bruno
Toxicon, ISSN 0041-0101, 02/2013, Volume 62, pp. 27 - 39
Phospholipases A (PLA s) are abundant components of snake venoms, where they play toxic and digestive roles. Despite having a similar three-dimensional... 
Molecular evolution | Snake venom | Neurotoxicity | Receptors | Phospholipase A2 | Enzymatic activity | Toxicity | Myotoxicity | Phospholipase A | Protein Structure, Tertiary | Neurotoxins - chemistry | Reptilian Proteins - chemistry | Models, Molecular | Phospholipases A2 - pharmacology | Neurotoxins - toxicity | Snake Venoms - chemistry | Structure-Activity Relationship | Phospholipases A2 - toxicity | Snake Venoms - enzymology | Reptilian Proteins - pharmacology | Neurotoxins - pharmacology | Sequence Analysis, Protein | Reptilian Proteins - toxicity | Phospholipases A2 - isolation & purification | Evolution, Molecular | Phospholipases A2 - chemistry | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text Snake venoms from Angola: Intra-specific variations and immunogenicity
by Oliveira, Paula Regina Simões de and França, Felipe Silva de and Villas Boas, Isadora Maria and Rocha, Marisa Maria Teixeira da and Sant’Anna, Sávio Stefanini and Bastos, Maria de Lourdes and Tambourgi, Denise V
Toxicon, ISSN 0041-0101, 06/2018, Volume 148, pp. 85 - 94
Snakebite is a public health problem in many countries of world. These accidents are considered a Neglected Tropical Disease and are responsible for a high... 
Geographic distribution | Immunogenicity | Bitis arietans | Naja nigricollis | Bitis gabonica | Intra-specific variations | Gender | Angolan snake venoms | NAJA-NIGRICOLLIS | BITE | SPITTING COBRA | AFRICA | PHARMACOLOGY & PHARMACY | TOXICOLOGY | Elapid Venoms - chemistry | Angola | Species Specificity | Viper Venoms - enzymology | Elapid Venoms - enzymology | Elapid Venoms - immunology | Male | Neglected Diseases | Viperidae | Naja | Viper Venoms - chemistry | Animals | Sex Factors | Viper Venoms - immunology | Electrophoresis | Female | Mice | Snake Bites | Snakes | Venom | Biological products | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text Examination of biochemical and biological activities of Bothrops jararaca (Serpentes: Viperidae; Wied-Neuwied 1824) snake venom after up to 54 years of storage
by Hatakeyama, Daniela M and de Morais-Zani, Karen and Serino-Silva, Caroline and Grego, Kathleen F and Sant'Anna, Savio S and Fernandes, Wilson and Aniz, Patrícia A.E.A and Torquato, Ricardo J.S and Tanaka, Aparecida S and Sanz, Libia and Calvete, Juan J and Tanaka-Azevedo, Anita M
Toxicon, ISSN 0041-0101, 01/2018, Volume 141, pp. 34 - 42
The number of snakes donated to the Brazilian Instituto Butantan has been decreasing in the past 10 years. This circumstance motivated us to compare the... 
Long-term stored venom | Bothrops jararaca snake venom | Activities of vintage venom pools | Venom composition and stability of B. jararaca venom pools | Venom composition and stability of B. jararaca venom pools | VARIABILITY | WILD | ASSAY | JUVENILE | PROTEOME | STABILITY | PHARMACOLOGY & PHARMACY | TOXICOLOGY | Animals | Antivenins | Bothrops | Time Factors | Male | Preservation, Biological | Crotalid Venoms - chemistry | Crotalid Venoms - enzymology | Mice | Crotalid Venoms - toxicity | Hemorrhage | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Full Text An analysis of venom ontogeny and prey-specific toxicity in the Monocled Cobra (Naja kaouthia)
by Modahl, Cassandra M and Mukherjee, Ashis K and Mackessy, Stephen P
Toxicon, ISSN 0041-0101, 09/2016, Volume 119, pp. 8 - 20
Venoms of snakes of the family Elapidae (cobras, kraits, mambas, and relatives) are predominantly composed of numerous phospholipases A (PLA s) and... 
Three-finger toxins | Enzymes | Phospholipases A2 | Venom variation | Mass spectrometry | Phospholipases A | RATTLESNAKES | SNAKE-VENOM | 3-FINGER TOXIN | NEUROTOXIN | JUVENILE | BIOLOGICAL PROPERTIES | PURIFICATION | AMINO-ACID-SEQUENCES | PHARMACOLOGY & PHARMACY | LANCE BOTHROPS-ATROX | TOXICOLOGY | THAILAND COBRA | Elapid Venoms - toxicity | Predatory Behavior | Chromatography, Ion Exchange | Animals | Elapidae | Electrophoresis, Polyacrylamide Gel | Lizards | Elapid Venoms - enzymology | Phospholipases A2 - metabolism | Mice | Mass Spectrometry - methods | Poisonous snakes | Biological products | Analysis | Venom | Index Medicus | Reptiles | Correlation | Toxicity | Abundance | Adults | Toxins | Mammals | Biological diversity
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
12. Full Text Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis
by Kang, Tse Siang and Georgieva, Dessislava and Genov, Nikolay and Murakami, Mário T and Sinha, Mau and Kumar, Ramasamy P and Kaur, Punit and Kumar, Sanjit and Dey, Sharmistha and Sharma, Sujata and Vrielink, Alice and Betzel, Christian and Takeda, Soichi and Arni, Raghuvir K and Singh, Tej P and Kini, R. Manjunatha
FEBS Journal, ISSN 1742-464X, 12/2011, Volume 278, Issue 23, pp. 4544 - 4576
Snake venoms are cocktails of enzymes and non‐enzymatic proteins used for both the immobilization and digestion of prey. The most common snake venom enzymes... 
acetylcholinesterase | phospholipase A | amino acid oxidase | metalloproteinase | serine proteinase | l -amino acid oxidase | l-amino acid oxidase | COAGULATION-FACTOR-XA | phospholipase A2 | BIOCHEMISTRY & MOLECULAR BIOLOGY | SECRETORY PHOSPHOLIPASE A | VON-WILLEBRAND-FACTOR | AGKISTRODON-HALYS PALLAS | CYSTEINE-RICH DOMAIN | AMINO-ACID OXIDASE | VIPERA-AMMODYTES-AMMODYTES | HUMAN PLATELET-AGGREGATION | DABOIA-RUSSELLI-PULCHELLA | ANTIINFLAMMATORY DRUGS NSAIDS | Catalytic Domain | Biocatalysis | L-Amino Acid Oxidase - chemistry | Stereoisomerism | Humans | Models, Molecular | Substrate Specificity | Phospholipases A2 - metabolism | Snake Venoms - chemistry | Structure-Activity Relationship | Acetylcholinesterase - chemistry | Snake Venoms - enzymology | Metalloproteases - metabolism | Animals | Cholinesterase Inhibitors - pharmacology | L-Amino Acid Oxidase - metabolism | Protein Conformation | Enzyme Activation | Phospholipase A2 Inhibitors | Acetylcholinesterase - metabolism | Metalloproteases - chemistry | Phospholipases A2 - chemistry | Oxidases | Usage | Proteases | Proteolysis | Analysis | Venom | Amino acids | Lead compounds | Catalysis | Phospholipases
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights