chaperone activity

OBSOLETE. Assists in the correct non-covalent assembly of polypeptide-containing structures in vivo, but is not a component of these assembled… (More)
National Institutes of Health

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Highly Cited
2010
Highly Cited
2010
Presynaptic nerve terminals release neurotransmitters repeatedly, often at high frequency, and in relative isolation from… (More)
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Highly Cited
2008
Highly Cited
2008
ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to… (More)
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Highly Cited
2003
Highly Cited
2003
ClpB of Escherichia coli is an ATP-dependent ring-forming chaperone that mediates the resolubilization of aggregated proteins in… (More)
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Highly Cited
2001
Highly Cited
2001
Non-LTR retrotransposons such as L1 elements are major components of the mammalian genome, but their mechanism of replication is… (More)
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Highly Cited
2000
Highly Cited
2000
The 70 kDa heat shock proteins (the Hsp70 family) assist refolding of their substrates through ATP-controlled binding. We have… (More)
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Highly Cited
1999
Highly Cited
1999
Small heat shock proteins (sHsps) are a conserved protein family, with members found in all organisms analysed so far. Several… (More)
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Highly Cited
1999
Highly Cited
1999
Heat shock protein 70 (Hsp70) is thought to play a critical role in the thermotolerance of mammalian cells, presumably due to its… (More)
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Review
1998
Review
1998
Retrovirus particles contain a small, basic protein, the nucleocapsid (NC) protein, that possesses 'nucleic acid chaperone… (More)
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Highly Cited
1997
Highly Cited
1997
The 70 kDa heat shock family of molecular chaperones is essential to a variety of cellular processes, yet it is unclear how these… (More)
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Highly Cited
1997
Highly Cited
1997
The BAG-1 protein appears to inhibit cell death by binding to Bcl-2, the Raf-1 protein kinase, and certain growth factor… (More)
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