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ecarin

Known as: echarin, Echis carinatus prothrombin-activating proteins, prothrombin activator (Echis carinatus venom) 
 
National Institutes of Health

Papers overview

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2015
2015
BACKGROUND Cysteine-rich secretory protein (CRISP) is present in majority of vertebrate including human. The physiological role… Expand
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2004
2004
This is the first structure of a biological homodimer of disintegrin. Disintegrins are a class of small (4-14 kDa) proteins that… Expand
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2003
2003
Snake venoms contain a number of hemostatically active C-type lectin-like proteins (CLPs), which affect the blood coagulation… Expand
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Highly Cited
2001
Highly Cited
2001
Echicetin, a heterodimeric snake C-type lectin from Echis carinatus, is known to bind specifically to platelet glycoprotein (GP… Expand
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Highly Cited
1997
Highly Cited
1997
Echistatin is a 49-amino-acid peptide belonging to the family of disintegrins that are derived from snake venoms and are potent… Expand
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1997
1997
Echicetin, a heterodimeric protein from the venom of Echis carinatus, binds to platelet glycoprotein Ib (GPIb) and so inhibits… Expand
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Highly Cited
1996
Highly Cited
1996
The venom of the viper Echis carinatus contains a metalloprotease, ecarin, that is a potent prothrombin activator. We here show… Expand
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Highly Cited
1995
Highly Cited
1995
The complete amino acid sequence of ecarin is deduced from the nucleotide sequence of a cDNA clone isolated by screening a… Expand
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Highly Cited
1990
Highly Cited
1990
The venom protein, s-echistatin, originally derived from the saw-scaled viper Echis carinatus, was found to be a potent inhibitor… Expand
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Highly Cited
1988
Highly Cited
1988
A 49-residue protein, echistatin, which inhibits platelet aggregation, was purified from the venom of the saw-scaled viper Echis… Expand
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