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… (More)
National Institutes of Health

Topic mentions per year

Topic mentions per year

1993-2017
05010019932017

Papers overview

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Review
2015
Review
2015
Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis… (More)
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2013
2013
The mechanisms through which iron-dependent enzymes receive their metal cofactors are largely unknown. Poly r(C)-binding protein… (More)
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2013
2013
Structurally and sequence-wise, the Hsp110s belong to a subfamily of the Hsp70 chaperones. Like the classical Hsp70s, members of… (More)
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2013
2013
Fragments of proteins containing an expanded polyglutamine (polyQ) tract are thought to initiate aggregation and toxicity in at… (More)
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2010
2010
The epithelial sodium channel (ENaC) is composed of a single copy of an alpha-, beta-, and gamma-subunit and plays an essential… (More)
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2010
2010
The major protein of bovine seminal plasma, PDC-109, binds to choline phospholipids on the sperm plasma membrane and induces the… (More)
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2008
2008
Plants often respond to abiotic stresses by the increased expression of LEA (late embryogenesis abundant) proteins, so called… (More)
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Highly Cited
2004
Highly Cited
2004
The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, Faculty of Agricultural, Food and Environmental… (More)
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Highly Cited
2002
Highly Cited
2002
The highly coordinated interactions of several molecular chaperones, including hsp70 and hsp90, are required for the folding and… (More)
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2002
2002
Protein disulfide isomerase (PDI) is a multifunctional protein catalysing the formation of disulfide bonds, acting as a molecular… (More)
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