Amyloid Fibrils

Amyloid Fibrils is a highly ordered, insoluble protein aggregate structure composed of misfolded polypeptides arranged in a cross-β-sheet conformation, distinguished from other protein aggregates by its characteristic fibrillar morphology, β-strand alignment perpendicular to the fibril axis, and resistance to proteolytic degradation.

11.3K

Publications

923.7K

Citations

35.9K

Authors

5.2K

Institutions

Publications per year

2017–2026

3.3K

Authors

35.9K

  1. CM
    Christopher M. Dobson

    University of Cambridge, United Kingdom

    179 publications · 30.4K citations

    94

    h-index

  2. RM
    Raffaele Mezzenga

    ETH Zurich, Switzerland

    127 publications · 11.7K citations

    61

    h-index

  3. DE
    David Eisenberg

    University of California, Los Angeles, United States

    84 publications · 18.7K citations

    61

    h-index

  4. PW
    Per Westermark

    Uppsala University, Sweden

    113 publications · 13.4K citations

    54

    h-index

  5. TP
    Tuomas P. J. Knowles

    University of Cambridge, United Kingdom

    94 publications · 13K citations

    53

    h-index

1–5 of 35.9K

Venues

  1. Proceedings of the National Academy of Sciences

    PNAS · 409 publications · 107K citations

    179

    h-index

  2. Journal of Biological Chemistry

    JBC · 546 publications · 72.3K citations

    140

    h-index

  3. Biochemistry

    483 publications · 48.6K citations

    117

    h-index

  4. Journal of the American Chemical Society

    JACS · 291 publications · 29.4K citations

    105

    h-index

  5. Journal of Molecular Biology

    JMB · 270 publications · 29.7K citations

    98

    h-index

1–5