Chaperone-mediated Interactions

Chaperone-Mediated Interactions is a molecular recognition process in which chaperone proteins selectively bind to client macromolecules to regulate their folding, assembly, or trafficking, distinguishing it from spontaneous or covalent interaction mechanisms by its dependence on transient, non-covalent chaperone-client engagements.

463

Publications

35K

Citations

2.3K

Authors

660

Institutions

Publications per year

2017–2026

94

Authors

2.3K

  1. JB
    Johannes Büchner

    Technical University of Munich, Germany

    14 publications · 1.4K citations

    14

    h-index

  2. LL
    Linda L. Randall

    Washington State University, United States

    8 publications · 614 citations

    8

    h-index

  3. WB
    William B. Pratt

    University of Michigan, United States

    8 publications · 1.2K citations

    8

    h-index

  4. FU
    F. Ulrich Hartl

    Max Planck Institute of Biochemistry, Germany

    6 publications · 985 citations

    6

    h-index

  5. CM
    Christopher M. Dobson

    University of Cambridge, United Kingdom

    6 publications · 686 citations

    6

    h-index

1–5 of 2.3K

Venues

  1. Journal of Biological Chemistry

    JBC · 65 publications · 4.8K citations

    40

    h-index

  2. Journal of Molecular Biology

    JMB · 30 publications · 1.8K citations

    24

    h-index

  3. Biochemical and Biophysical Research Communications

    BBRC · 19 publications · 680 citations

    17

    h-index

  4. The EMBO Journal

    16 publications · 3.8K citations

    16

    h-index

  5. Biochemistry

    14 publications · 1.1K citations

    14

    h-index

1–5