Chaperone Cooperation

Chaperone Cooperation is a molecular chaperone-mediated mechanism, distinguished from other folding-assistance strategies by the coordinated functional interaction between distinct chaperone systems to facilitate the efficient and selective folding of client proteins.

391

Publications

31.9K

Citations

1.8K

Authors

558

Institutions

Publications per year

2017–2026

72

Authors

1.8K

  1. JB
    Johannes Büchner

    Technical University of Munich, Germany

    15 publications · 1.8K citations

    15

    h-index

  2. BB
    Bernd Bukau

    Heidelberg University, Germany

    15 publications · 2K citations

    15

    h-index

  3. FU
    F. Ulrich Hartl

    Max Planck Institute of Biochemistry, Germany

    10 publications · 2.6K citations

    10

    h-index

  4. EA
    Elizabeth A. Craig

    University of Wisconsin–Madison, United States

    9 publications · 558 citations

    9

    h-index

  5. AM
    Axel Mogk

    Heidelberg University, Germany

    8 publications · 1.3K citations

    8

    h-index

1–5 of 1.8K

Venues

  1. Journal of Biological Chemistry

    JBC · 76 publications · 7.8K citations

    52

    h-index

  2. Proceedings of the National Academy of Sciences

    PNAS · 19 publications · 2K citations

    19

    h-index

  3. FEBS Letters

    18 publications · 922 citations

    15

    h-index

  4. Nature Communications

    13 publications · 898 citations

    13

    h-index

  5. Biochemistry

    12 publications · 611 citations

    12

    h-index

1–5