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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

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Review
2018
Review
2018
Carotenoids are lipophilic isoprenoid compounds synthesized by all photosynthetic organisms and some non-photosynthetic… Expand
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Review
2018
Review
2018
Both acute proteotoxic stresses that unfold proteins and expression of disease-causing mutant proteins that expose aggregation… Expand
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Review
2018
Review
2018
Rab proteins are the major regulators of vesicular trafficking in eukaryotic cells. Their activity can be tightly controlled… Expand
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Review
2018
Review
2018
Skeletal muscle is the most abundant tissue in the human body and can adapt its mass as a consequence of physical activity… Expand
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Review
2017
Review
2017
This review deals with the adaptive mechanisms that plants can implement to cope with the challenge of salt stress. Plants… Expand
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Review
2017
Review
2017
Gradual degeneration and loss of dopaminergic neurons in the substantia nigra, pars compacta and subsequent reduction of dopamine… Expand
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Review
2017
Review
2017
Aging is the inevitable time-dependent decline in physiological organ function and is a major risk factor for cancer development… Expand
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Review
2017
Review
2017
The association of histones with specific chaperone complexes is important for their folding, oligomerization, post-translational… Expand
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Review
2016
Review
2016
Heat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This… Expand
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Review
2015
Review
2015
This Review discusses new developments in understanding the basis of chylomicronaemia—a challenging metabolic disorder for which… Expand
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