Threonine Proteases

Threonine Protease is a proteolytic enzyme that catalyzes peptide bond hydrolysis using a nucleophilic threonine residue within its active site, distinguishing it from other serine, cysteine, or aspartic proteases by the specific involvement of threonine as the catalytic nucleophile.

57

Publications

6.8K

Citations

264

Authors

94

Institutions

Publications per year

2017–2026

1

Variants

Threonine Protease

Authors

264

  1. SK
    Shirley K. Knauer

    University of Duisburg-Essen, Germany

    4 publications · 116 citations

    4

    h-index

  2. CB
    Carolin Bier

    Johannes Gutenberg University Mainz, Germany

    3 publications · 101 citations

    3

    h-index

  3. OS
    Olaf Schneewind

    University of Chicago, United States

    3 publications · 958 citations

    3

    h-index

  4. RH
    Roland H. Stauber

    Johannes Gutenberg University Mainz, Germany

    3 publications · 101 citations

    3

    h-index

  5. JJ
    James J. Hsieh

    Memorial Sloan Kettering Cancer Center, United States

    3 publications · 246 citations

    3

    h-index

1–5 of 264

Venues

  1. Journal of Biological Chemistry

    JBC · 8 publications · 972 citations

    8

    h-index

  2. Proceedings of the National Academy of Sciences

    PNAS · 3 publications · 1K citations

    3

    h-index

  3. Biochemistry

    2 publications · 81 citations

    2

    h-index

  4. Protein Science

    PS · 2 publications · 80 citations

    2

    h-index

  5. FEBS Letters

    2 publications · 277 citations

    2

    h-index

1–5