Aspartic Proteases
Aspartic Protease is a class of proteolytic enzymes characterized by the use of two conserved aspartic acid residues in the active site to catalyze peptide bond hydrolysis through a mechanism involving a nucleophilic water molecule activated by the aspartates.
1.7K
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99.8K
Citations
6.6K
Authors
1.6K
Institutions
Publications per year
2017–2026
163
Variants
Aspartic Protease
Parents
1.7K
Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
Riqiang Yan, Michael J. Bienkowski, Mary E. Shuck et al. · Nature · 1999 · 1.4K citations
Rational Design of Peptide-Based HIV Proteinase Inhibitors
Noel A. Roberts, Joseph A. Martin, Derek Kinchington et al. · Science · 1990 · 925 citations
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University of Wales
Cardiff, United Kingdom
26 h-index
60 publications
5.2K citations
Oklahoma Medical Research Foundation
Oklahoma City, United States
25 h-index
128 publications
14.6K citations

Birkbeck, University of London
London, United Kingdom
24 h-index
121 publications
8.2K citations
University of Florida
Gainesville, United States
23 h-index
115 publications
5.5K citations

Kyoto University
Kyoto, Japan
22 h-index
99 publications
3.6K citations
The University of Tokyo
Tokyo, Japan
22 h-index
131 publications
5.3K citations
University Hospital of Lausanne
Lausanne, Switzerland
21 h-index
43 publications
3.1K citations
National Cancer Institute
Bethesda, United States
21 h-index
98 publications
11.7K citations
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JBC · 114 publications · 10.1K citations
61
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54 publications · 3.1K citations
33
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45 publications · 2.8K citations
30
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46 publications · 2.8K citations
28
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EJB · 30 publications · 1.6K citations
22
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