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animals (608) 608
index medicus (280) 280
venom (223) 223
toxicology (219) 219
crotalus (199) 199
pharmacology & pharmacy (193) 193
amino acid sequence (188) 188
biochemistry & molecular biology (183) 183
molecular sequence data (170) 170
snakes (167) 167
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male (147) 147
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proteins (96) 96
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crotalid venoms - pharmacology (78) 78
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crotalus-atrox venom (66) 66
female (66) 66
purification (66) 66
electrophoresis, polyacrylamide gel (63) 63
rats (63) 63
fibrinogen - metabolism (62) 62
amino-acid-sequence (61) 61
phospholipase a (61) 61
crotoxin (59) 59
poisonous snakes (56) 56
crotalus - physiology (55) 55
enzymes (54) 54
bothrops (50) 50
species specificity (49) 49
molecular weight (48) 48
sequence alignment (48) 48
base sequence (46) 46
crotalid venoms - isolation & purification (46) 46
crotalid venoms - genetics (45) 45
crotalus-atrox (45) 45
research (45) 45
chromatography, high pressure liquid (44) 44
phospholipases a - metabolism (44) 44
hemorrhage - chemically induced (43) 43
kinetics (43) 43
phospholipases a2 (43) 43
physiology (43) 43
snake (42) 42
evolution (41) 41
metalloendopeptidases - metabolism (41) 41
sequence homology, amino acid (41) 41
peptides (40) 40
rats, wistar (40) 40
rattlesnake (40) 40
mass spectrometry (39) 39
metabolism (39) 39
physiological aspects (38) 38
western diamondback rattlesnake (38) 38
crotalus durissus terrificus (37) 37
models, molecular (37) 37
protein binding (37) 37
viperidae (37) 37
biology (36) 36
biophysics (36) 36
hydrolysis (36) 36
platelet aggregation - drug effects (36) 36
substrate specificity (36) 36
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metalloproteinase (34) 34
snake-venoms (34) 34
temperature (34) 34
dose-response relationship, drug (33) 33
metalloendopeptidases - chemistry (33) 33
snake venoms - chemistry (33) 33
spectrometry, mass, matrix-assisted laser desorption-ionization (33) 33
crotamine (32) 32
research article (32) 32
cloning, molecular (31) 31
crotalus - genetics (31) 31
chromatography, gel (30) 30
medicine (30) 30
toxins (30) 30
blood coagulation - drug effects (29) 29
metalloproteases - metabolism (29) 29
amino acids (28) 28
complex mixtures (28) 28
hemorrhage (28) 28
hydrogen-ion concentration (28) 28
in vitro techniques (28) 28
platelet-aggregation (28) 28
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binding sites (27) 27
biochemistry, general (27) 27
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Journal Article
Comparative Biochemistry and Physiology, Part C, ISSN 1532-0456, 01/2019, Volume 215, pp. 18 - 24
While it has been known for a while that some snake species are extremely sensitive to acetaminophen, the underlying mechanism for this toxicity has not been... 
UDP‑glucuronosyltransferase | Mammalia | Acetaminophen | Toxicity | Snake | Biotransformation | N‑acetyltransferase | Reptilia | Phylogeny | ASSAY | UDP-glucuronosyltransferase | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLUCURONIDATION | PARACETAMOL | N-acetyltransferase | ZOOLOGY | METABOLISM | DEACETYLATION | ENDOCRINOLOGY & METABOLISM | TOXICOLOGY | Acetaminophen - adverse effects | Acetaminophen - metabolism | Acetyltransferases - metabolism | Liver - enzymology | Reptilian Proteins - genetics | Species Specificity | Snakes - physiology | Databases, Genetic | Environmental Pollutants - metabolism | Acetyltransferases - genetics | Agkistrodon - genetics | Glucuronosyltransferase - genetics | Glutathione Transferase - genetics | Isoenzymes - metabolism | Analgesics, Non-Narcotic - adverse effects | Colubridae - genetics | Crotalus - physiology | Sulfotransferases - metabolism | Colubridae - physiology | Boidae - physiology | Environmental Pollutants - toxicity | Boidae - genetics | Agkistrodon - physiology | Drug Resistance | Sulfotransferases - genetics | Acetaminophen - toxicity | Isoenzymes - genetics | Glutathione Transferase - metabolism | Analgesics, Non-Narcotic - metabolism | Toxicokinetics | Snakes - genetics | Animals | Glucuronosyltransferase - metabolism | Crotalus - genetics | Reptilian Proteins - metabolism | Animal genetics | Aromatic amines | Metabolites | Gene mutations | Glutathione transferase | Genomics | Turtles | Alligators | Comparative analysis | Snakes | Index Medicus
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2011, Volume 6, Issue 12, p. e28017
Hemorrhage is a clinically important manifestation of viperid snakebite envenomings, and is induced by snake venom metalloproteinases (SVMPs). Hemorrhagic and... 
HUMAN ALPHA-2-MACROGLOBULIN | CROTALUS-ATROX VENOM | ACUTUS VENOM | CYSTEINE-RICH DOMAIN | LOCAL TISSUE-DAMAGE | CRYSTAL-STRUCTURE | BIOLOGY | BASEMENT-MEMBRANES | VON-WILLEBRAND-FACTOR | BOTHROPS-ASPER TERCIOPELO | WEAK HEMORRHAGIC ACTIVITY | Immunohistochemistry | Metalloproteases - pharmacology | Molecular Weight | Basement Membrane - drug effects | Hydrolysis - drug effects | Caseins - metabolism | Capillaries - drug effects | Crotalid Venoms - enzymology | Muscles - pathology | Proteolysis - drug effects | Capillaries - metabolism | Extracellular Matrix Proteins - metabolism | Bothrops | Wounds and Injuries - pathology | Electrophoresis, Polyacrylamide Gel | Alpha-Globulins - metabolism | Proteoglycans - metabolism | Basement Membrane - metabolism | Blotting, Western | Collagen - metabolism | Insulin - metabolism | Animals | Heparan Sulfate Proteoglycans - metabolism | Metalloendopeptidases - pharmacology | Muscles - drug effects | Proteomics | Mice | Laminin - metabolism | Hemorrhage - pathology | Drug Combinations | Exudates and Transudates | Enzymes | Comparative analysis | Collagen | Venom | Phosphorylation | Pathogenesis | Perlecan | Collagens | Hemorrhage | Snakes | Degradation | Proteins | Laminin | Proteolysis | Fibroblasts | Extracellular matrix | Collagen (type IV) | Gastrocnemius muscle | Stability | Muscles | Substrates | Musculoskeletal system | Exudates | Skin | Microvasculature | Exudation | Laboratory animals
Journal Article
Toxicon, ISSN 0041-0101, 07/2014, Volume 85, pp. 5 - 16
Crotoxin (Crtx), the main toxin in the venom of snake, is a heterodimer with a basic subunit, CB, and an acidic subunit, CA. CB is a phospholipase A2 that... 
l-glutamate | PLA2 | Calcium channels | Synaptosomes | Crotoxin | CRYSTAL-STRUCTURE | PHOSPHOLIPASE A | FATTY-ACIDS | L-glutamate | ARACHIDONIC-ACID | NEUROTOXINS | RATTLESNAKE VENOM | AMINO-ACIDS | PHARMACOLOGY & PHARMACY | TOXICOLOGY | CORTICAL SYNAPTOSOMES | NEUROMUSCULAR-JUNCTION | BINDING | Synaptosomes - drug effects | Protein Subunits - pharmacology | Crotoxin - antagonists & inhibitors | Rats, Wistar | Male | Crotalid Venoms - enzymology | Protein Transport - drug effects | Group II Phospholipases A2 - antagonists & inhibitors | Synaptosomes - metabolism | Calcium Channels, N-Type - metabolism | Group II Phospholipases A2 - metabolism | Cerebral Cortex - metabolism | Protein Subunits - metabolism | Reptilian Proteins - pharmacology | Crotoxin - pharmacology | Group II Phospholipases A2 - pharmacology | Crotalus | Calcium Channel Agonists - metabolism | Synaptic Transmission - drug effects | Neurons - metabolism | Cerebral Cortex - drug effects | Neurons - drug effects | Nerve Tissue Proteins - antagonists & inhibitors | Nerve Tissue Proteins - agonists | Cells, Cultured | Calcium Channel Blockers - pharmacology | Nerve Tissue Proteins - metabolism | Neurotoxins - pharmacology | Crotoxin - metabolism | Animals | Calcium Signaling - drug effects | Calcium Channel Agonists - pharmacology | Neurotoxins - metabolism | Crotalid Venoms - chemistry | Glutamic Acid - metabolism | Protein Subunits - antagonists & inhibitors | Reptilian Proteins - antagonists & inhibitors | Neurotoxins - antagonists & inhibitors | Calcium Channels, N-Type - chemistry | Reptilian Proteins - metabolism | Venom | Amino acids | Phospholipases | Seizures (Medicine) | Glutamate | Rattlesnakes | Index Medicus
Journal Article
Journal Article
Cellular and Molecular Life Sciences, ISSN 1420-682X, 09/2009, Volume 66, Issue 17, pp. 2851 - 2871
Snake venom contains mixture of bioactive proteins and polypeptides. Most of these proteins and polypeptides exist as monomers, but some of them form complexes... 
Dimeric disintegrin | Synergistic three-finger toxin | Covalent and non-covalent three-finger toxin | PLA | Metalloprotease complexes | Serine protease complexes | complexes | 2-DIMENSIONAL NMR-SPECTROSCOPY | OXYURANUS-S-SCUTELLATUS | TRIMERESURUS-STEJNEGERI VENOM | BIOCHEMISTRY & MOLECULAR BIOLOGY | RUSSELLS VIPER VENOM | PLA complexes | CELL BIOLOGY | C-TYPE LECTINS | NEURONAL NICOTINIC RECEPTOR | CROTALUS-DURISSUS-TERRIFICUS | AMINO-ACID OXIDASE | CA2+-DEPENDENT PROTHROMBIN ACTIVATOR | X-BINDING PROTEIN | L-Amino Acid Oxidase - chemistry | Molecular Sequence Data | Snake Venoms - chemistry | Metalloproteases - metabolism | Protein Subunits - metabolism | Multiprotein Complexes - metabolism | Crotoxin - genetics | Disintegrins - chemistry | Dimerization | Bungarotoxins - metabolism | Metalloproteases - chemistry | Phospholipases A2 - chemistry | Protein Subunits - genetics | Amino Acid Sequence | Disintegrins - metabolism | Bungarotoxins - chemistry | Metalloproteases - genetics | Models, Molecular | Phospholipases A2 - metabolism | Crotoxin - metabolism | Multiprotein Complexes - chemistry | Animals | L-Amino Acid Oxidase - metabolism | Bungarotoxins - genetics | Protein Conformation | Protein Subunits - chemistry | Crotoxin - chemistry | Proteins | Thrombin | Amino acids | Universities and colleges | Venom | Peptides | Toxicity | Proteases | Snake bites | Molecular biology | Snakes | Index Medicus
Journal Article
Journal Article
International Journal of Molecular Sciences, ISSN 1661-6596, 08/2018, Volume 19, Issue 8, p. 2405
Snake venom serine proteases (SVSPs) represent an essential group of enzymatic toxins involved in several pathophysiological effects on blood homeostasis. Some... 
Edema | Oxidative stress | Snake venom serine protease | COX-2 | Inflammation | MDA | Protease-activated receptor | Crotalus durissus terrificus (Cdt) | CYTOSOLIC PHOSPHOLIPASE A | SIGNALING PATHWAYS | ACID RELEASE | SNAKE-VENOM | edema | THROMBIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | CHEMISTRY, MULTIDISCIPLINARY | snake venom serine protease | INHIBITION | inflammation | NEURONS | protease-activated receptor | COUPLED RECEPTORS | MEDIATORS | oxidative stress | Reptilian Proteins - chemistry | Receptors, Proteinase-Activated - metabolism | Type C Phospholipases - metabolism | Crotalid Venoms - adverse effects | Serine Proteases - adverse effects | Protein Kinase C - metabolism | Crotalus - metabolism | Female | Serine Proteases - chemistry | Snake Venoms | Crotalid Venoms - metabolism | Serine Proteases - metabolism | Amino Acid Sequence | Models, Molecular | Enzyme Activation - drug effects | Reptilian Proteins - adverse effects | Edema - metabolism | Animals | Signal Transduction - drug effects | Crotalid Venoms - chemistry | Mice | Edema - chemically induced | Oxidative Stress - drug effects | Edema - pathology | Reptilian Proteins - metabolism | Animal models | Protein kinase C | Serine | Homeostasis | Prostaglandin E2 | Arachidonic acid | Kinases | Snakes | Prostaglandin endoperoxide synthase | Proteins | Receptors | Enzymatic activity | Arginine | Protease | Dual energy X-ray absorptiometry | Dexamethasone | Three dimensional analysis | Amino acid sequence | Programmable logic controllers | Pharmacology | Metabolism | Malondialdehyde | Phospholipase C | Fibrin | Phospholipase | Inhibitors | Proteases | Programmable logic devices | Venom | Toxins | Serine proteinase | Cyclooxygenase-2 | Three dimensional models | Structural analysis
Journal Article
Journal Article