Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

By F. Hartl, M. Hayer-Hartl. Science, 2002

3,467 citations recorded by the source corpus.

Subfields: Cell Biology, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9675ac67a9b3413e3bd0dddd9653b9f45d3c6a5a

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Citations in the corpus

Heat shock protein 70 surface-positive tumor exosomes stimulate migratory and cytolytic activity of natural killer cells. (2005, background): “Heat shock proteins (HSP) inhabit nearly all cellular compartments, where they support folding of nascent polypeptides, prevent protein aggregation, and assist transport of other proteins across membranes (1).”
Heat shock protein 70 regulates the abscisic acid-induced antioxidant response of maize to combined drought and heat stress (2010, background): “HSP70 is one of the major classes of chaperone molecules and is involved in a variety of tasks in eukaryotic cells (Frydman 2001; Hartl and Hayer-Hartl 2002; Neupert and Brunner 2002; Mayer 2005; Bukau et al. 2006; Voellmy and Boellmann 2007).”
Thermal history-dependent expression of the hsp70 gene in purple sea urchins: Biogeographic patterns and the effect of temperature acclimation (2005, neutral): “Mechanistically, as cellular proteins, Hsps are molecular chaperones and play an important role in basic protein biosynthesis and protection from thermally induced protein denaturation and aggregation across virtually every taxa (Parsell et al., 1993; Hartl and Hayer-Hartl, 2002).”
Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “molecular chaperones, inducible Hsps bind to and aid the refolding of unfolded proteins, thereby preventing protein aggregation [105].”
Chaperoning signaling pathways: molecular chaperones as stress-sensing 'heat shock' proteins. (2002, background): “The chaperone activities of heat shock proteins enable folding of newly synthesized proteins and assist protein translocation across intracellular membranes (Hartl and Hayer-Hartl, 2002; Neupert, 1997).”
HSP expression in bivalves (2008, background): “Most of the information we have on chaperone functioning relies on studies on bacteria, where proteins are on average smaller and less complex than the corresponding proteins of eukaryotes (Hartl and Hayer-Hartl, 2002).”
Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones (2004, background): “…matrix each contain unique DnaK/Hsp70-type and DnaJ/Hsp40-type chaperones encoded by specific nuclear genes (Martin, 1997; Fewell et al., 2001; Hartl and Hayer-Hartl, 2002), whereas distinct GroE/Hsp10/60-type chaperonins are found in the cytoplasm and mitochondrial matrix but not in the ER…”