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

Publications

99.8K

Citations

6.6K

Authors

1.6K

Institutions

Publications per year

2017–2026

163

Variants

Aspartic Protease

Authors

6.6K

  1. BM
    Ben M. Dunn

    University of Florida, United States

    39 publications · 2K citations

    28

    h-index

  2. JK
    John Kay

    University of Wales, United Kingdom

    39 publications · 3.3K citations

    27

    h-index

  3. MM
    Michel Monod

    University Hospital of Lausanne, Switzerland

    26 publications · 1.7K citations

    22

    h-index

  4. JT
    Jordan Tang

    Oklahoma Medical Research Foundation, United States

    27 publications · 3.4K citations

    21

    h-index

  5. DE
    Daniel E. Goldberg

    Howard Hughes Medical Institute, United States

    24 publications · 2.9K citations

    20

    h-index

1–5 of 6.6K

Venues

  1. Journal of Biological Chemistry

    JBC · 114 publications · 10.1K citations

    61

    h-index

  2. FEBS Letters

    54 publications · 3.1K citations

    33

    h-index

  3. Biochemistry

    45 publications · 2.8K citations

    30

    h-index

  4. Journal of Medicinal Chemistry

    46 publications · 2.8K citations

    28

    h-index

  5. European Journal of Biochemistry

    EJB · 30 publications · 1.6K citations

    22

    h-index

1–5