Crotoxin
Crotalus
A genus of snakes of the family VIPERIDAE, one of the pit vipers, so-called from the pit hollowing out the maxillary bone, opening between the eye and the nostril. They are distinctively American serpents. Most of the 25 recognized species are found in the southwestern United States and northern Mexico. Several species are found as far north as Canada and east of the Mississippi, including southern Appalachia. They are named for the jointed rattle (Greek krotalon) at the tip of their tail. (Goin, Goin, and Zug: Introduction to Herpetology, 3d ed; Moore: Poisonous Snakes of the World, 1980, p335)
Crotalid Venoms
Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.
Ophthalmoplegia
Phospholipases A2
Viperidae
A family of snakes comprising three subfamilies: Azemiopinae (the mountain viper, the sole member of this subfamily), Viperinae (true vipers), and Crotalinae (pit vipers). They are widespread throughout the world, being found in the United States, Central and South America, Europe, Asia and Africa. Their venoms act on the blood (hemotoxic) as compared to the venom of elapids which act on the nervous system (neurotoxic). (Goin, Goin, and Zug, Introduction to Herpetology, 3d ed, pp333-36)
Snake Venoms
Phospholipases A
Elapid Venoms
Venoms from snakes of the family Elapidae, including cobras, kraits, mambas, coral, tiger, and Australian snakes. The venoms contain polypeptide toxins of various kinds, cytolytic, hemolytic, and neurotoxic factors, but fewer enzymes than viper or crotalid venoms. Many of the toxins have been characterized.
Neuromuscular Blocking Agents
Drugs that interrupt transmission of nerve impulses at the skeletal neuromuscular junction. They can be of two types, competitive, stabilizing blockers (NEUROMUSCULAR NONDEPOLARIZING AGENTS) or noncompetitive, depolarizing agents (NEUROMUSCULAR DEPOLARIZING AGENTS). Both prevent acetylcholine from triggering the muscle contraction and they are used as anesthesia adjuvants, as relaxants during electroshock, in convulsive states, etc.
Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2. (1/46)
Utilizing Marathon-ready cDNA library and a gene-specific primer corresponding to a partial amino acid sequence determined previously, the complete nucleotide sequence for the cDNA of crocalbin, which binds crotoxin (a phospholipase A2) and Ca2+, was obtained by polymerase chain reaction. The open reading frame of the cDNA encodes a novel polypeptide of 315 amino acid residues, including a signal sequence of 19 residues. This protein contains six potential Ca(2+)-binding domains, one N-glycosylation site, and a large amount of acidic amino acid residues. The ability to bind Ca2+ has been ascertained by calcium overlay experiment. Evidenced by sequence similarity in addition, it is concluded that crocalbin is a new member of the reticulocalbin family of calcium-binding proteins. (+info)Combining phage display and molecular modeling to map the epitope of a neutralizing antitoxin antibody. (2/46)
Crotoxin is a potent presynaptic neurotoxin from the venom of the rattlesnake Crotalus durissus terrificus. It is composed of the noncovalent and synergistic association of a weakly toxic phospholipase A2, CB, and a nontoxic three-chain subunit, CA, which increases the lethal potency of CB. The A-56.36 mAb is able to dissociate the crotoxin complex by binding to the CA subunit, thereby neutralizing its toxicity. Because A-56.36 and CB show sequence homology and both compete for binding to CA, we postulated that A-56.36 and CB had overlapping binding sites on CA. By screening random phage-displayed libraries with the mAb, phagotopes bearing the (D/S)GY(A/G) or AAXI consensus motifs were selected. They all bound A-56.36 in ELISA and competed with CA for mAb binding, although with different reactivities. When mice were immunized with the selected clones, polyclonal sera reacting with CA were induced. Interestingly, the raised antibodies retained the crotoxin-dissociating effect of A-56.36, suggesting that the selected peptides may be used to produce neutralizing antibodies. By combining these data with the molecular modeling of CA, it appeared that the functional epitope of A-56.36 on CA was conformational, one subregion being discontinuous and corresponding to the first family of peptides, the other subregion being continuous and composed of amino acids of the second family. Phage-displayed peptides corresponding to fragments of the two identified regions on CA reacted with A-56.36 and with CB. Our data support the hypothesis that A-56.36 and CB interact with common regions of CA, and highlight residues which are likely to be critical for CA-CB complex formation. (+info)Interaction of the neurotoxic and nontoxic secretory phospholipases A2 with the crotoxin inhibitor from Crotalus serum. (3/46)
Crotalus durissus terrificus snakes possess a protein in their blood, named crotoxin inhibitor from Crotalus serum (CICS), which protects them against crotoxin, the main toxin of their venom. CICS neutralizes the lethal potency of crotoxin and inhibits its phospholipase A2 (PLA2) activity. The aim of the present study is to investigate the specificity of CICS towards snake venom neurotoxic PLA2s (beta-neurotoxins) and nontoxic mammalian PLA2s. This investigation shows that CICS does not affect the enzymatic activity of pancreatic and nonpancreatic PLA2s, bee venom PLA2 and Elapidae beta-neurotoxins but strongly inhibits the PLA2 activity of Viperidae beta-neurotoxins. Surface plasmon resonance and PAGE studies further demonstrated that CICS makes complexes with monomeric and multimeric Viperidae beta-neurotoxins but does not interact with nontoxic PLA2s. In the case of dimeric beta-neurotoxins from Viperidae venoms (crotoxin, Mojave toxin and CbICbII), which are made by the noncovalent association of a PLA2 with a nonenzymatic subunit, CICS does not react with the noncatalytic subunit, instead it binds tightly to the PLA2 subunit and induces the dissociation of the heterocomplex. In vitro assays performed with Torpedo synaptosomes showed a protective action of CICS against Viperidae beta-neurotoxins but not against other PLA2 neurotoxins, on primary and evoked liberation of acetylcholine. In conclusion, CICS is a specific PLA2 inhibitor of the beta-neurotoxins from the Viperidae family. (+info)Crotoxin, the major toxin from the rattlesnake Crotalus durissus terrificus, inhibits 3H-choline uptake in guinea pig ileum. (4/46)
We examined the effect of crotoxin, the neurotoxic complex from the venom of the South American rattlesnake Crotalus durissus terrificus, on the uptake of 3H-choline in minces of smooth muscle myenteric plexus from guinea pig ileum. In the concentration range used (0. 03-1 microM) and up to 10 min of treatment, crotoxin decreased 3H-choline uptake by 50-75% compared to control. This inhibition was time dependent and did not seem to be associated with the disruption of the neuronal membrane, because at least for the first 20 min of tissue exposure to the toxin (up to 1 microM) the levels of lactate dehydrogenase (LDH) released into the supernatant were similar to those of controls. Higher concentrations of crotoxin or more extensive incubation times with this toxin resulted in elevation of LDH activity detected in the assay supernatant. The inhibitory effect of crotoxin on 3H-choline uptake seems to be associated with its phospholipase activity since the equimolar substitution of Sr2+ for Ca2+ in the incubation medium or the modification of the toxin with p-bromophenacyl bromide substantially decreased this effect. Our results show that crotoxin inhibits 3H-choline uptake with high affinity (EC25 = 10 +/- 5 nM). We suggest that this inhibition could explain, at least in part, the blocking effect of crotoxin on neurotransmission. (+info)Role of crotoxin, a phospholipase A2 isolated from Crotalus durissus terrificus snake venom, on inflammatory and immune reactions. (5/46)
BACKGROUND: Crotoxin (CTX) is a potent neurotoxin from Crotalus durissus terrificus snake venom (CdtV) composed of two subunits: one without catalytic activity (crotapotin), and a basic phospolipase A2. Recent data have demonstrated that CdtV or CTX inhibit some immune and inflammatory reactions. AIM: The aim of this paper was to investigate the mechanisms involved in these impaired responses. MATERIALS AND METHODS: Male Swiss mice were bled before and at different intervals of time after subcutaneous injection of CTX or bovine serum albumin (BSA) (control animals). The effect of treatments on circulating leukocyte mobilisation and on serum levels of interleukin (IL)-6, IL-10, interferon (IFN)-gamma and corticosterone were investigated. Spleen cells from treated animals were also stimulated in vitro with concanavalin A to evaluate the profile of IL-4, IL-6, IL-10 or IFN-gamma secretion. Cytokine levels were determined by immunoenzymatic assay and corticosterone levels by radioimmunoassay. To investigate the participation of endogenous corticosteroid on the effects evoked by CTX, animals were treated with metyrapone, an inhibitor of glucocorticoid synthesis, previous to CTX treatment. RESULTS: Marked alterations on peripheral leukocyte distribution, characterised by a drop in the number of lymphocytes and monocytes and an increase in the number of neutrophils, were observed after CTX injection. No such alteration was observed in BSA-treated animals. Increased levels of IL-6, IL-10 and corticosterone were also detected in CTX-injected animals. IFN-gamma levels were not modified after treatments. In contrast, spleen cells obtained from CTX-treated animals and stimulated with concanavalin A secreted less IL-10 and IL-4 in comparison with cells obtained from control animals. Metyrapone pretreatment was effective only to reverse the neutrophilia observed after CTX administration. CONCLUSIONS: Our results suggest that CTX may contribute to the deficient inflammatory and immune responses induced by crude CdtV. CTX induces endogenous mechanisms that are responsible, at least in part, for these impaired responses. (+info)Actions of Crotalus durissus terrificus venom and crotoxin on the isolated rat kidney. (6/46)
Many studies have reported the occurrence of lethal acute renal failure after snakebites. The aim of the present investigation was to determine alterations in renal function produced by Crotalus durissus terrificus venom and crotoxin as well as the histological alterations induced by these venoms. Isolated kidneys from Wistar rats weighing 240 to 280 g were perfused with Krebs-Henseleit solution containing 6 g% of previously dialyzed bovine serum albumin. The effects of Crotalus durissus terrificus venom and crotoxin were studied on glomerular filtration rate (GFR), urinary flow (UF), perfusion pressure (PP) and percentage sodium tubular transport (%TNa+). The infusion of Crotalus durissus terrificus venom (10 microg/ml) and crotoxin (10 microg/ml) increased GFR (control80 = 0.78 +/- 0.07, venom80 = 1.1 +/- 0.07, crotoxin80 = 2.0 +/- 0.05 ml g(-1) min(-1), P<0.05) and UF (control80 = 0.20 +/- 0.02, venom80 = 0.32 +/- 0.03, crotoxin80 = 0.70 +/- 0.05 ml g(-1) min(-1), P<0.05), and decreased %TNa+ (control100 = 75.0 +/- 2.3, venom100 = 62.9 +/- 1.0, crotoxin80 = 69.0 +/- 1.0 ml g(-1) min(-1), P<0.05). The infusion of crude venom tended to reduce PP, although the effect was not significant, whereas with crotoxin PP remained stable during the 100 min of perfusion. The kidneys perfused with crude venom and crotoxin showed abundant protein material in the urinary space and tubules. We conclude that Crotalus durissus terrificus venom and crotoxin, its major component, cause acute nephrotoxicity in the isolated rat kidney. The current experiments demonstrate a direct effect of venom and crotoxin on the perfused isolated kidney. (+info)Phase I and pharmacokinetics study of crotoxin (cytotoxic PLA(2), NSC-624244) in patients with advanced cancer. (7/46)
A Phase I clinical trial was performed on patients with solid tumors refractory to conventional therapy. Crotoxin was administered i.m. for 30 consecutive days at doses ranging from 0.03 to 0.22 mg/m(2). Patients entered the study after providing a written informed consent. Although 26 patients were entered only 23 were evaluated. Reversible, nonlimiting neuromuscular toxicity evidenced as diplopia because of pareses of the external ocular muscles was present in 13 patients. It started at doses of 0.18 mg/m(2) and lasted from 2 to 6 h. These episodes did not require dose adjustment and disappeared in 1-3 weeks of treatment. Three patients experienced palpebral ptosis, nystagmus (grade 2), and anxiety (grade 2-3) at the dose-limiting toxicity of 0.22 mg/m(2). Also at dose-limiting toxicity, 1 patient showed nystagmus (grade 2) and anxiety (grade 3) without evidence of palpebral ptosis. Transient increases (grades 1-3) in the levels of creatinine kinase, aspartate aminotransferase, and alanine transaminase attributed to crotoxin myotoxicity were observed but returned to normal by the last week of treatment. At 0.21 mg/m(2) there was a case of grade-3 anaphylactic reaction on day 31, which required treatment. Hypersensitivity was regarded as an adverse drug-related reaction, and the patient was removed from the protocol. Two patients at different doses (0.12 mg/m(2) and 0.22 mg/m(2)) had sialorrhea. Four patients had asymptomatic transient increase in blood pressure (up to 20 mm Hg) 12 h after the first injection, which lasted 24 h. No treatment was required and toxicity did not reappear. Six patients experienced slight eosinophilia during the first 2 weeks. The maximum tolerated dose was set at 0.21 mg/m(2). Objective measurable partial responses (>50% reduction of tumor mass) were noted in 2 patients treated at 0.21 mg/m(2) and 1 at 0.12 mg/m(2). One patient (at 0.21 mg/m(2)) presented a complete response on day 110. Crotoxin pharmacokinetics showed rapid absorption from the injection site to blood (t(1/2 A) = 5.2 +/- 0.6 min). Plasma concentration reached a peak (C(max) = 0.79 +/- 0.1 ng/ml) at tau(max) = 19 +/- 3 min. The half-life of the distribution (alpha) phase is 22 +/- 2 min. Starting at 1.5 h after injection, the decrease in plasma concentration becomes slower, reaching 14 +/- 3 pg/ml 24 h after injection. The profile is dominated by the elimination (beta) phase with a half-life of 5.2 +/- 0.6 h. Consequently, 24 h after the injection ( approximately 5 half-life) 97% of the product was eliminated. The area under plasma concentration versus time curve was 0.19 +/- 0.05 microg/min/ml. Assuming availability (F) approximately 1, the clearance is C(L) = 26.3 +/- 7 ml/min, and the apparent volume of distribution is V(d) = 12 +/- 3 liter/kg. The recommended dose for a Phase II study is 0.18 mg/m(2). (+info)Molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms. (8/46)
Some myotoxic or neurotoxic PLA2s (phospholipases A2) from pit viper venoms contain characteristic N6 substitutions. Our survey of the venoms of more than ten pit viper genera revealed that N6-PLA2s exist only in limited Asian pit vipers of two genera, Protobothrops and Gloydius, and exist as either monomers or the basic subunits of heterodimers in some New World pit vipers. For the newly identified N6-PLA2s, the neuromuscular blocking activities were assayed with the chick biventer cervicis neuromuscular tissue, whereas the increased serum creatine kinase level assessed their myotoxicities. The purified N6-PLA2s from Protobothrops mangshanensis and Gloydius intermedius saxatilis were found to be presynaptic neurotoxins. In contrast, all N6-PLA2s from the venoms of Sistrurus miliarius strackeri, S. m. barbouri, Crotalus viridis viridis, C. lepidus lepidus, Cerrophidion godmani and Bothreichis schlegelii were myotoxins without neurotoxicity even in the presence of crotoxin A. Crotoxin-like complexes were for the first time purified from the venoms of Sitrurus catenatus tergeminus, C. mitchelli mitchelli, C. horridus atricaudatus, C. basiliscus and C. durissus cumanensis. The cDNAs encoding six novel N6-PLA2s and subunits of the crotoxin-like complex from S. c. tergeminus were cloned and fully sequenced. Phylogeny analysis showed that two structural subtypes of N6-PLA2s with either F24 or S24 substitution have been evolved in parallel, possibly descended respectively from species related to present-day Protobothrops and Gloydius. Calmodulin binds all the N6-PLA2s but crotoxin A may inhibit its binding to crotoxin B and to other neurotoxic N6-PLA2s. Structure-activity relationships at various regions of the PLA2 molecules were extensively discussed. (+info)
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RCSB PDB - Protein Feature View
- Phospholipase A2 crotoxin basic subunit CBb - P0CG56 (PA2BB CRODU)
Toxins | Free Full-Text | Secreted Phospholipases A2 of Snake Venoms: Effects on the Peripheral Neuromuscular System with...
NORDIC-MUBIO - REPRESENTADAS : 1 mg, Basal cell Cytokein, actin Alpha-cardiac, Crotalus durissus terrificus venom Phospholipase...
NORDIC-MUBIO - REPRESENTADAS : 1 mg, Basal cell Cytokein, actin Alpha-cardiac, Crotalus durissus terrificus venom Phospholipase...
Permalien vers Molecular structure and mechanism of action of the crotoxin inhibitor from Crotalus durissus terrificus serum.
Role of crotoxin, a phospholipase A2 isolated from Crotalus durissus terrificus snake venom, on inflammatory and immune...
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Los anticuerpos IgG de conejos anti-fosfolipasa A2 de Crotalus durissus terrificus neutralizan la actividad letal del veneno
The amino acid sequence of the acidic subunit B-chain of crotoxin
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Crotalus
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Crotoxin
Later was discovered that the crotoxin protein is not homogeneous, but consists of 2 subunits. The toxic effect of crotoxin is ... Since 1966 until today, investigations into pharmacological applications for crotoxin are conducted. The structure of crotoxin ... In one study, Crotoxin has shown to improve the ocular alignment of a group of cross-eyed patients after injection. The same ... Crotoxin is a heterodimeric beta-neurotoxin, composed of an acidic, non-toxic and non-enzymatic subunit (CA), and a basic, ...
Management of strabismus
Crotoxin appears to act similarly.[unreliable medical source] To weaken an eye muscle, 1 to 12 units (a few nanograms) of toxin ... Crotoxin, a snake neurotoxin, is being developed in Belo Horizonte, Brazil as a potential alternative.[unreliable medical ... "Study of crotoxin on the induction of paralysis in extraocular muscle in animal model". Arquivos Brasileiros de Oftalmologia. ... "Crotoxin in humans: analysis of the effects on extraocular and facial muscles". Arquivos Brasileiros de Oftalmologia. 75 (6): ...
Crotalus simus
Only venom from neonates contains crotoxin; a constituent typically found in C. durissus venom that produces neurotoxic ...
Spotlight Innovation
Crotoxin was tested on patients in the George Pompidou University Hospital in Paris. In 2014, Celtic Biotech LTD entered into a ... "Crotoxin Administration for Cancer Treatment and Pain Relief". Google.com/patents. Google Patents. Retrieved 7 September 2015 ... In January, 2015, Celtic Biotech Iowa was granted a patent by the U.S. Patent and Trademark Office entitled Crotoxin ... "Open Label Clinical Trial of Intravenous Crotoxin - Full Text View". Clinicaltrials.gov. Retrieved 2 June 2019. Wood, Megan. " ...
Animal attacks in Latin America
"Actions of Crotalus durissus terrificus venom and crotoxin on the isolated rat kidney". Brazilian Journal of Medical and ...
Crotalus durissus
Bite symptoms are very different from those of Nearctic species due to the presence of neurotoxins (crotoxin and crotamine) ... "Actions of Crotalus durissus terrificus venom and crotoxin on the isolated rat kidney". Brazilian Journal of Medical and ...
Karl Slotta
In 1938, Slotta and his brother-in-law Heinz Fraenkel-Conrat isolated crotoxin from venom, the first snake toxin to be isolated ... Their research suggested that the toxicity of crotoxin was due to effects on nerve lipids. He subsequently co-founded a ...
Calumenin
Hseu MJ, Yen CH, Tzeng MC (1999). "Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a ...
List of dangerous snakes
Bite symptoms are very different from those of Nearctic species due to the presence of neurotoxins (crotoxin and crotamine) ...
CTX
... a toxin found in cone snail venom Crotoxin, toxic compound in snake venom Cyclophosphamide, an anticancer drug Centrex, a ...
List of MeSH codes (D20)
... crotoxin MeSH D20.944.380 - hazardous waste MeSH D20.944.380.638 - radioactive waste MeSH D20.944.420 - industrial waste MeSH ...
Varespladib
... crotoxin B and myotoxin I) was evaluated. The results obtained showed that Varespladib was able to neutralize the in vitro ... myotoxin-I and crotoxin B), however further detailed analysis are needed. Varespladib also effectively inhibited the non- ...
List of MeSH codes (D23)
... crotoxin MeSH D23.946.896.980 - virulence factors, bordetella MeSH D23.946.896.980.040 - adenylate cyclase toxin MeSH D23.946. ...
Crotoxin Definition & Meaning | Dictionary.com
Crotoxin definition, a toxin in the venom of the North American rattlesnake, Crotalus terrificus. See more. ... Words nearby crotoxin. crotonbug, Crotone, crotonic acid, crotonism, croton oil, crotoxin, crottin, crottle, crouch, croup, ... crotoxin. First recorded in 1915-20; blend of Crotalus (genus name) + toxin ...
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Potassium channel blocking actions of β‐bungarotoxin and related toxins on mouse and frog motor nerve terminals<...
Other prejunctionally active snake toxins (taipoxin, notexin and crotoxin) had similar effects to those of β‐bungarotoxin, but ... Other prejunctionally active snake toxins (taipoxin, notexin and crotoxin) had similar effects to those of β‐bungarotoxin, but ... Other prejunctionally active snake toxins (taipoxin, notexin and crotoxin) had similar effects to those of β‐bungarotoxin, but ... Other prejunctionally active snake toxins (taipoxin, notexin and crotoxin) had similar effects to those of β‐bungarotoxin, but ...
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Botulinum toxin
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Crotoxin inhibited cell proliferation, viability, colony formation, and migration, favoring cell death. Furthermore, crotoxin ... Mice treated with crotoxin at 10 µg/kg did not alter biochemical parameters total cholesterol, very-low-density lipoprotein, ... Crotoxin treatment significantly reduced the frequency of oral squamous cell carcinoma lesions by 50%. Thus, this study ... In the animal model, after induction of oral cancer by 4-nitroquinoline-1-oxide carcinogen, mice were treated with crotoxin to ...
Accepted Abstracts | Biology of Pitvipers
Give and take: testing for exchange of crotoxin in rock rattlesnakes (Crotalus lepidus) within and between species Mellor, N. ... Give and take: testing for exchange of crotoxin in rock rattlesnakes (Crotalus lepidus) within and b ... Give and take: testing for exchange of crotoxin in rock rattlesnakes (Crotalus lepidus) within and b ...
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A monoclonal antibody directed against the non-toxic subunit of a dimeric phospholipase A2 neurotoxin, crotoxin, neutralizes...
CB is less toxic than crotoxin, has a higher enzymatic activity and triggers a higher acetylcholine release than crotoxin, due ... was shown to fully neutralize the toxicity of crotoxin. When the in vitro pharmacological properties of crotoxin were further ... Crotoxin is the main toxic component of the venom of the South-American rattlesnake Crotalus durissus terrificus. It is a ... These effects were explained by the fast dissociation of the crotoxin complex in the presence of the monoclonal antibody A- ...
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Acidic phospholipase A2 - Gloydius halys (Chinese water mocassin)
Low-dose thickness measurement of glucose-embedded protein crystals by electron energy loss spectroscopy and STEM dark-field...
... imaging in a scanning transmission electron microscope were used to determine the thickness of glucose-embedded crotoxin ... Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 keV electrons at near-atomic resolution. Brink J, ... imaging in a scanning transmission electron microscope were used to determine the thickness of glucose-embedded crotoxin ...
Full-Length Venom Protein cDNA Sequences from Venom-Derived mRNA: Exploring Compositional Variation and Adaptive Multigene...
Newly sequenced crotoxin homologs are indicated by double asterisks (crotoxin A-left side; crotoxin B-right side). GenBank ... Sequences similar to crotoxin/Mojave toxin acidic subunit A derived from from venom (asterisks) were discovered in Crotalus ... Sequences similar to the crotoxin or Mojave toxin basic B subunits derived from venom (asterisks) were discovered in Crotalus ... A) Sequence alignments of the acidic (A) subunit of crotoxin or Mojave toxin homologs with identical residues shaded; the ...
SMART: PA2c domain annotation
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MeSH Browser
Crotoxin A Crotoxin B Registry Number. 9007-40-3. CAS Type 1 Name. Crotoxin. Previous Indexing. Snake Venoms (1975-1977). ... Crotoxin A Narrower Concept UI. M0005364. Registry Number. 0. Terms. Crotoxin A Preferred Term Term UI T010016. Date12/09/1983 ... Crotoxin B Narrower Concept UI. M0005365. Registry Number. 0. Terms. Crotoxin B Preferred Term Term UI T010017. Date12/09/1983 ... Crotoxin Preferred Term Term UI T010015. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1978). ...
Research Grants 12/51241-5 - Antineoplásicos, Venenos de origem animal - BV FAPESP
Effect of Crotoxin on several steps in angiogenese evaluated in two dimensional and three dimensional matrices: in vitro ... Crotoxin-induced macrophage secretory activity on fibroblast functions involved wi.... Study of the angiogenic potential and of ... Effect of Crotoxin on several steps in angiogenese evaluated in two dimensional and three dimensional matrices: in vitro ... Crotoxin promotes macrophage reprogramming towards an antiangiogenic phenotype. SCIENTIFIC REPORTS, v. 9, MAR 12 2019. (13/ ...
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Crotoxin A Crotoxin B Registry Number. 9007-40-3. CAS Type 1 Name. Crotoxin. Previous Indexing. Snake Venoms (1975-1977). ... Crotoxin A Narrower Concept UI. M0005364. Registry Number. 0. Terms. Crotoxin A Preferred Term Term UI T010016. Date12/09/1983 ... Crotoxin B Narrower Concept UI. M0005365. Registry Number. 0. Terms. Crotoxin B Preferred Term Term UI T010017. Date12/09/1983 ... Crotoxin Preferred Term Term UI T010015. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1978). ...
Snake Venoms < Venoms << Toxins (biological toxins) <<< Poisons @...
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- University of Strathclyde
Abigail Podufaly | Author | SciTechnol | Journal of Virology & A
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Blood coagulation cascade inhibiting toxin ~ VenomZone
PA2BA_CRODU Phospholipase A2 crotoxin basic chain CBa2 (CB2) ... Crotalus durissus terrificus (South American ... ... PA2BB_CRODU Phospholipase A2 crotoxin basic subunit CBb (CTX ... Crotalus durissus terrificus (South American ... ... PA2B6_CRODM Phospholipase A2 crotoxin basic chain (CB) ... Crotalus durissus cumanensis (South American ... ... PA2BC_CRODU Phospholipase A2 crotoxin basic subunit CBc ... Crotalus durissus terrificus (South American ... ...
Exploring levels of protein structure with molecular models and snake venom | Digital World Biology
Today, were going to explore crotoxin for a different reason. Were going to use crotoxin to investigate the four levels of ... The phospholipase from the South American rattlesnake is called crotoxin. Scientists are interested in studying crotoxin ... In crotoxin, the active site is the place where this enzyme chops up phospholipids. Exploring the active site To explore the ... Crotoxin has four protein chains, each with a different sequence. To view the amino acid sequences: *Open the sequence viewer. ...
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Uropsophus | definition of Uropsophus by Medical dictionary
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Crotoxin-induced mice lung impairment: role of nicotinic acetylcholine receptors and COX-derived prostanoids. Biomolecules, v. ... 2020). Role of crotoxin in coagulation: novel insights into anticoagulant mechanisms and impairment of inflammation-induced ... Crotoxin-induced mice lung impairment: role of nicotinic acetylcholine receptors and COX-derived prostanoids (2020) ... 2020). Crotoxin-induced mice lung impairment: role of nicotinic acetylcholine receptors and COX-derived prostanoids. ...
The Most Dangerous Places On Earth | sonar
Batroxobin. Medical search
rattlesnake venom effects
Each type of rattlesnake bite venom out there is an … However, the toxicity of crotoxin limits its medicinal use. Without them ... Venom ( T63.01 ) T63.004S the toxicity of crotoxin limits its medicinal use SBA-15 silica nanostructure Media. ... Crotoxin, found in snake venoms snake injected venom, on the sodium channel of murine skeletal muscle the.: some snake bites ...
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Toxicity of crotoxin2
- A murine monoclonal antibody directed to the non-toxic subunit CA, A-56.36, was shown to fully neutralize the toxicity of crotoxin. (pasteur.fr)
- Each type of rattlesnake bite venom out there is an … However, the toxicity of crotoxin limits its medicinal use. (diosuniversal.com)
Crotalus3
- Crotoxin is the main toxic component of the venom of the South-American rattlesnake Crotalus durissus terrificus. (pasteur.fr)
- Several studies, in vivo and in vitro have demonstrated antitumor activity of Crotoxin (CTX), the major toxin of Crotalus durissus terrificus venom. (fapesp.br)
- Crotalus durissus terrificus snake venom and its major toxin, crotoxin or type II PLA2 (CB) subunit of this toxin, modulates immune and inflammatory responses, interfering with the activity of leukocytes. (fapesp.br)
Phospholipase2
- Gopalakrishnakone P, Dempster DW, Hawgood BJ, Elder Nettle (1984) Cellular and mitochondrial changes induced in the structure of murine skeletal muscle nettle crotoxin, a neurotoxic phospholipase A2 complex. (t44.xyz)
- The phospholipase from the South American rattlesnake is called crotoxin. (digitalworldbiology.com)
Subunit1
- Both types of secondary structure are shown in this image of the crotoxin B subunit. (digitalworldbiology.com)
Venom1
- Venom characterization of the three species of Ophryacus and proteomic profiling of O. sphenophrys unveils Sphenotoxin, a novel Crotoxin-like heterodimeric beta-neurotoxin Journal of Proteomics, 192, 196-207. (unam.mx)
Vitro2
- When the in vitro pharmacological properties of crotoxin were further tested, A-56.36 was shown to enhance the enzymatic activity on negatively-charged phospholipids and to increase the acetylcholine release triggered by crotoxin on Torpedo synaptosomes. (pasteur.fr)
- It binds to CA with a similar affinity than the parental immunoglobulin and exhibits similar effects on the in vitro pharmacological properties of crotoxin. (pasteur.fr)
Enzyme1
- 5) release of metalloproteinases (MMP-2 and MMP-9) and VEGF, after treatment with crotoxin, by enzyme immunoassay (EIA). (fapesp.br)
Snake1
- Scientists are interested in studying crotoxin because snake bites are a serious health hazard and better treatments would help save lives and minimize nerve and muscle damage. (digitalworldbiology.com)
Complex2
- These effects were explained by the fast dissociation of the crotoxin complex in the presence of the monoclonal antibody A-56.36 and the immunocomplexation of CA, with CB being released in solution. (pasteur.fr)
- Electron energy loss spectroscopy and dark-field imaging in a scanning transmission electron microscope were used to determine the thickness of glucose-embedded crotoxin complex crystals. (nih.gov)
Activity2
- CB is less toxic than crotoxin, has a higher enzymatic activity and triggers a higher acetylcholine release than crotoxin, due to its strong enzymatic activity. (pasteur.fr)
- Crotoxin is a good protein for this activity because it contains both types of secondary structure, metals, disulfide bonds, and multiple protein chains. (digitalworldbiology.com)
Basic1
- Despite evidence of antitumor action of crotoxin, was not demonstrated yet the action of this toxin on basic parameters for neovascularization, essential for the growth and survival of the tumor. (fapesp.br)