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rhizopuspepsin
Known as:
Rhizopus carboxyl proteinase
, rhizopepsin
, Rhizopus chinensis aspartic protease
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National Institutes of Health
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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.
A. Kadek
,
D. Kavan
,
+6 authors
P. Man
Biochimica et Biophysica Acta - General Subjects
2017
Corpus ID: 20060268
Highly Cited
2009
Highly Cited
2009
Recombinant immobilized rhizopuspepsin as a new tool for protein digestion in hydrogen/deuterium exchange mass spectrometry.
Martial Rey
,
P. Man
,
G. Brandolin
,
E. Forest
,
L. Pelosi
Rapid Communications in Mass Spectrometry
2009
Corpus ID: 206438058
Hydrogen/deuterium (H/D) exchange coupled to mass spectrometry is nowadays routinely used to probe protein interactions or…
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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
W. Todd Lowther
,
B. Dunn
,
P. Majer
Protein Science
1995
Corpus ID: 40370454
Rhizopuspepsin and other fungal aspartic proteinases are distinct from the mammalian enzymes in that they are able to cleave…
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Highly Cited
1994
Highly Cited
1994
X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.
T. Blundell
,
J. Jenkins
,
+5 authors
S. Wood
Journal of Molecular Biology
1994
Corpus ID: 25418836
Highly Cited
1994
Highly Cited
1994
Crystal structures of native and inhibited forms of human cathepsin D: implications for lysosomal targeting and drug design.
E. Baldwin
,
T. Bhat
,
+6 authors
J. Erickson
Proceedings of the National Academy of Sciences…
1994
Corpus ID: 31864603
Cathepsin D (EC 3.4.23.5) is a lysosomal protease suspected to play important roles in protein catabolism, antigen processing…
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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.
M. Newman
,
F. Watson
,
+6 authors
T. Blundell
Journal of Molecular Biology
1993
Corpus ID: 37842510
The structure of mucor pusillus pepsin (EC 3.4.23.6), the aspartic proteinase from Mucor pusillus, has been refined to a…
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1992
1992
Synthesis and crystallographic analysis of two rhizopuspepsin inhibitor complexes.
K. Parris
,
D. Hoover
,
D. B. Damon
,
D. Davies
Biochemistry
1992
Corpus ID: 41532823
The crystal structures of rhizopuspepsin complexed with two oligopeptide inhibitors have been determined. CP-69,799, an…
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1991
1991
Recombinant rhizopuspepsinogen. Expression, purification, and activation properties of recombinant rhizopuspepsinogens.
Z. Chen
,
G. Koelsch
,
+4 authors
J. Tang
Journal of Biological Chemistry
1991
Corpus ID: 42352368
Highly Cited
1988
Highly Cited
1988
Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus
H. Horiuchi
,
K. Yanai
,
T. Okazaki
,
M. Takagi
,
K. Yano
Journal of Bacteriology
1988
Corpus ID: 23171994
A gene encoding Rhizopus niveus aspartic proteinase was isolated from an R. niveus genomic library by using oligonucleotides…
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Highly Cited
1987
Highly Cited
1987
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
K. Suguna
,
R. Bott
,
+4 authors
D. Davies
Journal of Molecular Biology
1987
Corpus ID: 26397865
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