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Molecular Chaperones

Known as: Chaperone, Chaperone, Molecular, Molecular Chaperones [Chemical/Ingredient] 
Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport… Expand
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2019
Review
2019
Background: Glucose‐Regulated Protein 78 (GRP78) is a chaperone heat shock protein that has been intensely studied in the last… Expand
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Review
2019
Review
2019
The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein… Expand
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Review
2019
Review
2019
BACKGROUND As molecular chaperones, Heat Shock Proteins (HSPs) not only play key roles in protein folding and maintaining protein… Expand
Review
2019
Review
2019
Titin has long been recognized as a mechanical protein in muscle cells that has a main function as a molecular spring in the… Expand
Review
2019
Review
2019
Macroautophagy (hereafter referred to as autophagy) involves an intracellular degradation and recycling system that, in a context… Expand
Review
2019
Review
2019
Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis) and prevent the accumulation of… Expand
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Review
2018
Review
2018
Abiotic stresses, such as low or high temperature, deficient or excessive water, high salinity, heavy metals, and ultraviolet… Expand
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Review
2018
Review
2018
Abstract The hypothalamic–pituitary–adrenal (HPA) axis is the major neuroendocrine axis regulating homeostasis in mammals… Expand
Review
2018
Review
2018
Polyphosphate (polyP) consists of a linear arrangement of inorganic phosphates and defies its structural simplicity with an… Expand
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Review
2018
Review
2018
Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-dependent molecular chaperones that fold… Expand
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