Chaperone-bound Intermediates

Chaperone-Bound Intermediates is a folding intermediate that is transiently associated with molecular chaperones during protein folding, distinguishing it from other folding intermediates by its specific stabilization and regulation through chaperone binding to prevent misfolding or aggregation.

37

Publications

4K

Citations

156

Authors

58

Institutions

Publications per year

2017–2026

3

Authors

156

  1. MH
    Manajit Hayer‐Hartl

    Max Planck Institute of Biochemistry, Germany

    4 publications · 1.2K citations

    4

    h-index

  2. FU
    F. Ulrich Hartl

    Max Planck Institute of Biochemistry, Germany

    3 publications · 1.2K citations

    3

    h-index

  3. AL
    Arthur L. Horwich

    Yale University, United States

    2 publications · 154 citations

    2

    h-index

  4. JZ
    Junjie Zhang

    Texas A&M University, United States

    2 publications · 266 citations

    2

    h-index

  5. NR
    Nicholai R. Douglas

    Stanford University, United States

    2 publications · 266 citations

    2

    h-index

1–5 of 156

Venues

  1. Journal of Molecular Biology

    JMB · 8 publications · 420 citations

    8

    h-index

  2. Journal of Biological Chemistry

    JBC · 6 publications · 239 citations

    6

    h-index

  3. The EMBO Journal

    3 publications · 790 citations

    3

    h-index

  4. Cell

    2 publications · 966 citations

    2

    h-index

  5. Nature Structural & Molecular Biology

    2 publications · 108 citations

    2

    h-index

1–5