clostripain

Known as: clostridiopeptiase B 
 
National Institutes of Health

Topic mentions per year

Topic mentions per year

1968-2016
051019682016

Papers overview

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Highly Cited
2013
Highly Cited
2013
Half of the microbial cells in the Earth's oceans are found in sediments. Many of these cells are members of the Archaea, single… (More)
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2004
2004
In this study we investigate the active-site structure and the catalytic mechanism of clostripain by using a combination of three… (More)
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1998
1998
We show by site-directed mutagenesis that the catalytic residues of mammalian legumain, a recently discovered lysosomal… (More)
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1996
1996
The clostripain core protein is composed of the light and heavy chain subunits linked by a nonapeptide into a single polypeptide… (More)
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1993
1993
Clostripain (EC 3.4.22.8) is a heterodimeric cysteine endopeptidase with strict specificity for Arg-Xaa peptidyl bonds. It is… (More)
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1991
1991
In view of the probability that clostripain (EC 3.4.22.8) is fundamentally different in structure from other known cysteine… (More)
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1986
1986
Rat liver chromatin core particles digested with clostripain yield a structurally well-defined nucleoprotein particle with an… (More)
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Highly Cited
1982
Highly Cited
1982
1. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) at a concentration of 0.5 mM had no effect on the serine… (More)
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1979
1979
A highly active form of clostripain, composed of two polypeptide chains (Mr = 43,000 and 12,500), was isolated by hydrophobic… (More)
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1968
1968
The proteolytic enzyme, clostridiopeptidase B (clostripain), from Clostridium histo2yticum culture filtrates has been purified to… (More)
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