Amyloid Fibrillogenesis

Amyloid Fibrillogenesis is a biochemical process defined as the pathogenic self-assembly of misfolded proteins into highly ordered, insoluble fibrillar aggregates characterized by a cross-β sheet quaternary structure, distinct from other protein aggregation mechanisms by its specific structural morphology and resistance to degradation.

3.7K

Publications

318.3K

Citations

13.9K

Authors

2.7K

Institutions

Publications per year

2017–2026

845

Authors

13.9K

  1. CM
    Christopher M. Dobson

    University of Cambridge, United Kingdom

    63 publications · 11.5K citations

    50

    h-index

  2. PW
    Per Westermark

    Uppsala University, Sweden

    67 publications · 8.3K citations

    41

    h-index

  3. HN
    Hironobu Naiki

    University of Fukui, Japan

    58 publications · 6.6K citations

    39

    h-index

  4. YG
    Yuji Goto

    The University of Osaka, Japan

    54 publications · 3.7K citations

    36

    h-index

  5. MF
    Marcus Fändrich

    Universität Ulm, Germany

    39 publications · 4.3K citations

    30

    h-index

1–5 of 13.9K

Venues

  1. Journal of Biological Chemistry

    JBC · 238 publications · 29.1K citations

    94

    h-index

  2. Proceedings of the National Academy of Sciences

    PNAS · 123 publications · 33.2K citations

    87

    h-index

  3. Journal of Molecular Biology

    JMB · 141 publications · 14K citations

    72

    h-index

  4. Biochemistry

    159 publications · 16.9K citations

    67

    h-index

  5. Biochemical and Biophysical Research Communications

    BBRC · 103 publications · 8.7K citations

    48

    h-index

1–5