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rhizopuspepsin

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

Related topics

Related topics

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Broader (1)

Aspartic Acid Endopeptidases

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2009
2009
Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.
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
Engineering the substrate specificity of rhizopuspepsin: The role of Asp 77 of fungal aspartic proteinases in facilitating the cleavage of oligopeptide substrates with lysine in P1
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
Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.
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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1993
1993
X-ray analyses of aspartic proteinases. V. Structure and refinement at 2.0 A resolution of the aspartic proteinase from Mucor pusillus.
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
pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants.
The pH dependence of the kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants has been… Expand
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  • table I
  • table I
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1992
1992
Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
The crystal structures of rhizopuspepsin complexed with two oligopeptide inhibitors have been determined. CP-69,799, an… Expand
Highly Cited
1990
Highly Cited
1990
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
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
Construction of side-chains in homology modelling. Application to the C-terminal lobe of rhizopuspepsin.
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
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
The structure of rhizopuspepsin (EC 3.4.23.6), the aspartic proteinase from Rhizopus chinensis, has been refined to a… Expand
1987
1987
The amino acid sequence of rhizopuspepsin, an aspartic proteinase from Rhizopus chinensis.
  • 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
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