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rhizopuspepsin

Known as: Rhizopus carboxyl proteinase, rhizopepsin, Rhizopus chinensis aspartic protease 
 
National Institutes of Health

Papers overview

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2009
2009
Hydrogen/deuterium (H/D) exchange coupled to mass spectrometry is nowadays routinely used to probe protein interactions or… Expand
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  • table 1
  • table 1
1995
1995
Rhizopuspepsin and other fungal aspartic proteinases are distinct from the mammalian enzymes in that they are able to cleave… Expand
Highly Cited
1993
Highly Cited
1993
Cathepsin D (EC 3.4.23.5) is a lysosomal protease suspected to play important roles in protein catabolism, antigen processing… Expand
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  • table 1
1993
1993
The structure of mucor pusillus pepsin (EC 3.4.23.6), the aspartic proteinase from Mucor pusillus, has been refined to a… Expand
1992
1992
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been… Expand
  • table 11
  • figure 1
  • table I
  • table I
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1992
1992
The crystal structures of rhizopuspepsin complexed with two oligopeptide inhibitors have been determined. CP-69,799, an… Expand
Highly Cited
1990
Highly Cited
1990
The molecular structure of endothiapepsin (EC 3.4.23.6), the aspartic proteinase from Endothia parasitica, has been refined to a… Expand
Highly Cited
1989
Highly Cited
1989
A detailed and rule-based side-chain modelling procedure for globular proteins is presented. It uses the conformational… Expand
Highly Cited
1987
Highly Cited
1987
The structure of rhizopuspepsin (EC 3.4.23.6), the aspartic proteinase from Rhizopus chinensis, has been refined to a… Expand
1987
1987
  • K. Takahashi
  • The Journal of biological chemistry
  • 1987
  • Corpus ID: 22246997
The complete amino acid sequence of rhizopuspepsin, an aspartic proteinase from the fungus Rhizopus chinensis was determined by… Expand