Transition State Stabilization

Transition State Stabilization is a mechanism of enzymatic catalysis whereby an enzyme lowers the activation free energy of a reaction by preferentially binding and stabilizing the transition state relative to the ground-state substrates and products, typically through optimally arranged noncovalent interactions.

331

Publications

18.7K

Citations

1K

Authors

353

Institutions

Publications per year

2017–2026

41

Authors

1K

  1. JP
    John P. Richard

    University at Buffalo, State University of New York, United States

    18 publications · 713 citations

    15

    h-index

  2. TL
    Tina L. Amyes

    University at Buffalo, State University of New York, United States

    15 publications · 526 citations

    15

    h-index

  3. RW
    Richard Wolfenden

    University of North Carolina at Chapel Hill, United States

    7 publications · 447 citations

    7

    h-index

  4. AJ
    Adrian J. Mulholland

    University of Bristol, United Kingdom

    6 publications · 438 citations

    6

    h-index

  5. AW
    Arieh Warshel

    University of Southern California, United States

    6 publications · 920 citations

    6

    h-index

1–5 of 1K

Venues

  1. Journal of the American Chemical Society

    JACS · 53 publications · 3.3K citations

    34

    h-index

  2. Biochemistry

    42 publications · 2.6K citations

    29

    h-index

  3. Journal of Molecular Biology

    JMB · 15 publications · 1.1K citations

    14

    h-index

  4. Proceedings of the National Academy of Sciences

    PNAS · 13 publications · 1.4K citations

    12

    h-index

  5. The Journal of Organic Chemistry

    JOC · 14 publications · 501 citations

    12

    h-index

1–5