Atp Synthase Structure

ATP Synthase Structure is a molecular machinery construct that belongs to the class of rotary nanomotor enzymes, distinguished by its dual-domain architecture comprising a membrane-embedded F₀ subunit for proton translocation and a catalytic F₁ subunit for ATP synthesis, organized with precise stoichiometry and symmetry to enable mechanochemical energy conversion in mitochondria, chloroplasts, and prokaryotic membranes.

800

Publications

55.1K

Citations

2.2K

Authors

635

Institutions

Publications per year

2017–2026

133

Variants

Atp Synthase Architecture

Authors

2.2K

  1. JE
    John E. Walker

    MRC Laboratory of Molecular Biology, United Kingdom

    44 publications · 10.3K citations

    34

    h-index

  2. TM
    Thomas Meier

    Max Planck Institute of Biophysics, Germany

    33 publications · 3.6K citations

    29

    h-index

  3. RF
    Robert Fillingame

    University of Wisconsin–Madison, United States

    38 publications · 2.5K citations

    28

    h-index

  4. JV
    Jean Velours

    Institut de Biochimie et Génétique Cellulaires, France

    35 publications · 1.9K citations

    27

    h-index

  5. WK
    Werner Kühlbrandt

    Max Planck Institute of Biophysics, Germany

    20 publications · 4.1K citations

    20

    h-index

1–5 of 2.2K

Venues

  1. Journal of Biological Chemistry

    JBC · 155 publications · 8.3K citations

    57

    h-index

  2. Proceedings of the National Academy of Sciences

    PNAS · 57 publications · 8.2K citations

    45

    h-index

  3. Biochemistry

    63 publications · 2.6K citations

    28

    h-index

  4. FEBS Letters

    40 publications · 2.4K citations

    25

    h-index

  5. 23

    h-index

1–5