Chaperone machines for protein folding, unfolding and disaggregation

By H. Saibil. Nature reviews. Molecular cell biology, 2013

1,055 citations recorded by the source corpus.

Molecular chaperones are diverse families of multidomain proteins that have evolved to assist nascent proteins to reach their native fold, protect subunits from heat shock during the assembly of complexes, prevent protein aggregation or mediate targeted unfolding and disassembly. Their increased expression in response to stress is a key factor in the health of the cell and longevity of an organism. Unlike enzymes with their precise and finely tuned active sites, chaperones are heavy-duty molecular machines that operate on a wide range of substrates. The structural basis of their mechanism of action is being unravelled (in particular for the heat shock proteins HSP60, HSP70, HSP90 and HSP100) and typically involves massive displacements of 20–30 kDa domains over distances of 20–50 Å and rotations of up to 100°.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d12c5780417f9c53da78d5f3b0d3f7069ddff0a1

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Donna D. Zhang

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Citations in the corpus

NRF2 and the Hallmarks of Cancer. (2018, background): “Heat shock factor 1 (HSF1) is the main transcription factor regulating the expression of HSPs (Dayalan Naidu and Dinkova-Kostova, 2017, Anckar and Sistonen, 2011, Whitesell and Lindquist, 2009).”
Epigenetically facilitated mutational assimilation: epigenetics as a hub within the inclusive evolutionary synthesis (2018, background): “, 2017) and chaperone molecules (Halfmann & Lindquist, 2010; Lindquist, 2011; Halfmann et al., 2012; Saibil, 2013) that constitute other forms of molecular memory.”