Results 11 to 20 of about 112,374 (150)
Snake Venom Metalloproteinases and Their Peptide Inhibitors from Myanmar Russell’s Viper Venom [PDF]
Toxins, 2016 Russell’s viper bites are potentially fatal from severe bleeding, renal failure and capillary leakage. Snake venom metalloproteinases (SVMPs) are attributed to these effects.
Khin Than Yee +4 more
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Structures and Functions of Snake Venom Metalloproteinases (SVMP) from Protobothrops venom Collected in Japan [PDF]
Molecules, 2017 Snake venom metalloproteinases (SVMP) are widely distributed among the venoms of Crotalinae and Viperidae, and are organized into three classes (P-I, P-II and P-III) according to their size and domain structure.
Etsuko Oyama, Hidenobu Takahashi
doaj +4 more sources
Snake Venom Metalloproteinases [PDF]
, 2017 UCR::Vicerrectoría de Docencia::Salud::Facultad de ...
José María Gutiérrez, Jay Fox
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Activation of snake venom metalloproteinases by a cysteine switch‐like mechanism [PDF]
FEBS Letters, 1993 The cDNAs of several snake venom zinc endopeptidases code for a putative propeptide, which includes the conserved cysteine‐containing sequence PKMCGVT. It has been suggested that binding of the cysteine thiol function to the active‐site zinc, resulting in inactivation of the catalytic domain, occurs in a mode similar to the ‘cysteine switch’ mechanism ...
Grams, Frank +4 more
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Triacontyl p-coumarate: An inhibitor of snake venom metalloproteinases
Phytochemistry, 2013 Snake venom metalloproteinases (SVMPs) participate in a number of important biological, physiological and pathophysiological processes and are primarily responsible for the local tissue damage characteristic of viperid snake envenomations. The use of medicinal plant extracts as antidotes against animal venoms is an old practice, especially against ...
Mendes, M. M. +9 more
openaire +4 more sources
Snake Venom Metalloproteinases (SVMPs): A structure-function update
Toxicon: X, 2020 Snake venom metalloproteinases (SVMPs) represent a diverse group of multi-domain proteins with several biological activities such as the ability to induce hemorrhage, proteolytic degradation of fibrinogen and fibrin, induction of apoptosis and inhibition
Olamide Tosin Olaoba +3 more
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Dabsylated Bradykinin Is Cleaved by Snake Venom Proteases from Echis ocellatus
BiomedicinesThe vasoactive peptide bradykinin (BK) is an important member of the renin–angiotensin system. Its discovery is tightly interwoven with snake venom research, because it was first detected in plasma following the addition of viper venom.
Julius Abiola +4 more
doaj +2 more sources
Snake Venom Metalloproteinases [PDF]
Acta Medica Marisiensis, 2016 Abstract As more data are generated from proteome and transcriptome analysis revealing that metalloproteinases represent most of the Viperid and Colubrid venom components authors decided to describe in a short review a classification and some of the multiple activities of snake venom metalloproteinases.
Teresa Escalante +3 more
+6 more sources
Structure and Function of Snake Venom Metalloproteinase Family [PDF]
Journal of Protein Chemistry, 1992 Venoms of snakes belonging to families Viperidae (viper) and Crotalidae (pit viper) produce striking local effects, consisting of hemorrhage, necrosis, and edema, and often induce marked alterations of blood coagulation system as well (Iwanaga and Suzuki, 1979). Among these pathological effects, hemorrhage is a most common occurrence in a victim bitten
Sadaaki Iwanaga, Hiroyuki Takeya
openaire +2 more sources
Inhibition of a Snake Venom Metalloproteinase by the Flavonoid Myricetin [PDF]
Molecules, 2018 Most of the snakebite envenomations in Central and South America are caused by species belonging to Bothrops genus. Their venom is composed mainly by zinc-dependent metalloproteinases, responsible of the hemorrhage characteristic of these envenomations.
Pereañez Jiménez, Jaime Andrés +4 more
openaire +5 more sources