Leucine Zipper Dimerization

Leucine Zipper Dimerization is a protein dimerization mechanism characterized by the association of two alpha-helical regions containing regularly spaced leucine residues that interlock in a coiled-coil structure, thereby facilitating sequence-specific DNA binding or protein-protein interactions in transcription factors.

336

Publications

36.1K

Citations

1.3K

Authors

403

Institutions

Publications per year

2017–2026

19

Authors

1.3K

  1. KS
    Kevin Struhl

    Harvard University, United States

    7 publications · 1.2K citations

    7

    h-index

  2. CV
    Charles Vinson

    National Institutes of Health, United States

    7 publications · 1K citations

    7

    h-index

  3. PS
    Peter S. Kim

    Whitehead Institute for Biomedical Research, United States

    6 publications · 3.1K citations

    6

    h-index

  4. TC
    Tom Curran

    La Roche College, United States

    6 publications · 2.3K citations

    6

    h-index

  5. DH
    Daniel H. González

    Universidad Nacional del Litoral, Argentina

    6 publications · 281 citations

    6

    h-index

1–5 of 1.3K

Venues

  1. Journal of Biological Chemistry

    JBC · 43 publications · 3K citations

    32

    h-index

  2. Molecular and Cellular Biology

    MCB · 34 publications · 2.8K citations

    28

    h-index

  3. Biochemistry

    23 publications · 1.1K citations

    21

    h-index

  4. Proceedings of the National Academy of Sciences

    PNAS · 23 publications · 3.3K citations

    20

    h-index

  5. Journal of Virology

    JVI · 16 publications · 768 citations

    16

    h-index

1–5