Skip to search formSkip to main contentSkip to account menu

rhizopuspepsin

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

Related topics

Related topics

1 relation

Broader (1)

Aspartic Acid Endopeptidases

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2017
2017
Interdomain electron transfer in cellobiose dehydrogenase is governed by surface electrostatics.
Highly Cited
2009
Highly Cited
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… 
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… 
Highly Cited
1994
Highly Cited
1994
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
Highly Cited
1994
Highly Cited
1994
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… 
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… 
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… 
1991
1991
Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.
Highly Cited
1988
Highly Cited
1988
Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus
A gene encoding Rhizopus niveus aspartic proteinase was isolated from an R. niveus genomic library by using oligonucleotides… 
Highly Cited
1987
Highly Cited
1987
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)