Chaperone-mediated Folding

Chaperone-Mediated Folding is a protein folding mechanism in which molecular chaperones selectively bind to nascent or misfolded polypeptides to prevent aggregation and facilitate proper folding through transient, non-covalent interactions, distinguishing it from spontaneous or co-translational folding pathways.

4.9K

Publications

394.3K

Citations

16.7K

Authors

2.8K

Institutions

Publications per year

2017–2026

809

Authors

16.7K

  1. JB
    Johannes Büchner

    Technical University of Munich, Germany

    94 publications · 14.6K citations

    62

    h-index

  2. FU
    F. Ulrich Hartl

    Max Planck Institute of Biochemistry, Germany

    84 publications · 18.3K citations

    60

    h-index

  3. BB
    Bernd Bukau

    Heidelberg University, Germany

    75 publications · 13.4K citations

    59

    h-index

  4. JF
    Judith Frydman

    Stanford University, United States

    58 publications · 8.2K citations

    42

    h-index

  5. MP
    Matthias P. Mayer

    Heidelberg University, Germany

    41 publications · 5.9K citations

    35

    h-index

1–5 of 16.7K

Venues

  1. Journal of Biological Chemistry

    JBC · 712 publications · 58.1K citations

    122

    h-index

  2. Proceedings of the National Academy of Sciences

    PNAS · 246 publications · 28.7K citations

    100

    h-index

  3. The EMBO Journal

    123 publications · 23.3K citations

    93

    h-index

  4. Cell

    76 publications · 22.4K citations

    72

    h-index

  5. Nature

    75 publications · 27.9K citations

    71

    h-index

1–5