Cell
Volume 78, Issue 3, 12 August 1994, Pages 365-372
Journal home page for Cell

Meeting review
Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell

https://doi.org/10.1016/0092-8674(94)90416-2Get rights and content

First page preview

First page preview
Click to open first page preview

References (23)

  • L. Van Dyck et al.

    PIM1 encodes a mitochondrial ATP-dependent protease that is required for mitochondrial function of the yeast Saccharomyces cerevisiae

    J. Biol. Chem.

    (1994)
  • A.-P. Arrigo et al.

    Expression and function of the low-molecular-weight heat shock proteins

  • J.L. Brodsky et al.

    Heat shock cognate proteins and polypeptide translocation across the endoplasmic reticulum membrane

  • E.A. Craig et al.

    Cytosolic hsp70s of Saccharomyces cerevisiae: roles in protein synthesis, protein translocation, proteolysis, and regulation

  • M. Fernandes et al.

    Structure and regulation of heat shock gene promoters

  • J. Frydman et al.

    Molecular chaperone functions of hsp70 and hsp60 in protein folding

  • M.-J. Gething et al.

    Structure, function, and regulation of the endoplasmic reticulum chaperone, BiP

  • C. Georgopoulos et al.

    Properties of the heat shock proteins of Escherichia coli and the autoregulation of the heat shock response

  • S. Gottesman et al.

    Regulation by proteolysis: energy-dependent proteases and their targets

    Microbiol. Rev.

    (1992)
  • C.J. Harrison et al.

    Crystal structure of the DNA binding domain of the heat shock transcription factor

    Science

    (1994)
  • J.P. Hendrick et al.

    Molecular chaperone functions of heat-shock proteins

    Annu. Rev. Biochem.

    (1993)
  • Cited by (426)

    • Heat shock protein vaccines in glioblastoma

      2021, Immunotherapeutic Strategies for the Treatment of Glioma
    • Cellular quality control during gametogenesis

      2020, Experimental Cell Research
    • Warmer temperature increases mercury toxicity in a marine copepod

      2020, Ecotoxicology and Environmental Safety
      Citation Excerpt :

      HSPs are large, highly conserved molecular chaperone proteins in prokaryotes and vertebrates (Craig et al., 1994). Under environmental stressors that include heat, osmotic stress, and chemical exposure, the proteins that are damaged are recovered/repaired by inducible HSPs (Craig et al., 1994; Schlesinger, 1990). In this study, the expression of hsp70 and hsp90 in P. annandalei might have been induced to compensate for the increase in Hg toxicity caused by the combined exposure to the warmer temperature and Hg.

    • Transcriptome analysis of Liriomyza trifolii (Diptera: Agromyzidae) in response to temperature stress

      2020, Comparative Biochemistry and Physiology - Part D: Genomics and Proteomics
    View all citing articles on Scopus
    View full text