Amyloid Fibril Structure

Amyloid Fibril Structure is a structural biology construct that refers to the highly ordered, β-sheet-rich, filamentous protein aggregate morphology characterized by its insolubility, resistance to proteolysis, and specific cross-β architecture, distinguishing it from other protein folding states such as native globular or amorphous aggregates.

2.7K

Publications

220.7K

Citations

9.4K

Authors

2.1K

Institutions

Publications per year

2017–2026

824

Authors

9.4K

  1. CM
    Christopher M. Dobson

    University of Cambridge, United Kingdom

    68 publications · 11.7K citations

    53

    h-index

  2. RM
    Raffaele Mezzenga

    ETH Zurich, Switzerland

    46 publications · 5.9K citations

    36

    h-index

  3. RT
    Robert Tycko

    National Institute of Diabetes and Digestive and Kidney Diseases, United States

    39 publications · 13.2K citations

    35

    h-index

  4. PW
    Per Westermark

    Uppsala University, Sweden

    48 publications · 5.9K citations

    33

    h-index

  5. MF
    Marcus Fändrich

    Universität Ulm, Germany

    42 publications · 5.3K citations

    30

    h-index

1–5 of 9.4K

Venues

  1. Proceedings of the National Academy of Sciences

    PNAS · 106 publications · 24.3K citations

    76

    h-index

  2. Journal of Molecular Biology

    JMB · 120 publications · 13.3K citations

    65

    h-index

  3. Biochemistry

    132 publications · 14.2K citations

    60

    h-index

  4. Journal of the American Chemical Society

    JACS · 102 publications · 10.6K citations

    59

    h-index

  5. Journal of Biological Chemistry

    JBC · 123 publications · 10.6K citations

    59

    h-index

1–5