Chaperone-substrate Recognition

Chaperone-Substrate Recognition is a molecular interaction mechanism by which chaperone proteins selectively identify and bind non-native or misfolded protein substrates through exposed hydrophobic regions or specific sequence motifs, thereby initiating proper folding, preventing aggregation, or targeting for degradation.

875

Publications

70.2K

Citations

3.6K

Authors

945

Institutions

Publications per year

2017–2026

141

Authors

3.6K

  1. BB
    Bernd Bukau

    Heidelberg University, Germany

    29 publications · 4.9K citations

    24

    h-index

  2. JB
    Johannes Büchner

    Technical University of Munich, Germany

    18 publications · 1.6K citations

    18

    h-index

  3. JC
    James C.A. Bardwell

    University of Michigan, United States

    14 publications · 1.3K citations

    13

    h-index

  4. SW
    Sue Wickner

    National Institutes of Health, United States

    12 publications · 935 citations

    12

    h-index

  5. AM
    Axel Mogk

    Heidelberg University, Germany

    12 publications · 1.5K citations

    12

    h-index

1–5 of 3.6K

Venues

  1. Journal of Biological Chemistry

    JBC · 137 publications · 9.5K citations

    61

    h-index

  2. Journal of Molecular Biology

    JMB · 58 publications · 3.5K citations

    37

    h-index

  3. Proceedings of the National Academy of Sciences

    PNAS · 41 publications · 4.2K citations

    36

    h-index

  4. The EMBO Journal

    27 publications · 5.5K citations

    25

    h-index

  5. Biochemical and Biophysical Research Communications

    BBRC · 26 publications · 1K citations

    21

    h-index

1–5