ZUO1 protein, S cerevisiae

Known as: YGR285C protein, S cerevisiae, Zuotin, zuotin protein, S cerevisiae 
Identified in yeast, Zuotin, containing one J domain, is a Z-DNA-binding protein and ribosomal chaperone that may be involved in chromosome… (More)
National Institutes of Health

Papers overview

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Review
2012
Review
2012
Chirality is absolutely central in chemistry and biology. The recent findings of chiral self-assembling peptides' remarkable… (More)
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Highly Cited
2006
Highly Cited
2006
GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the… (More)
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Highly Cited
2002
Highly Cited
2002
The chaperones RAC (ribosome-associated complex), consisting of Ssz1p and zuotin, and Ssb1/2p are associated with ribosomes of… (More)
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Highly Cited
2001
Highly Cited
2001
The yeast cytosol contains multiple homologs of the DnaK and DnaJ chaperone family. Our current understanding of which homologs… (More)
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2001
2001
Proteins are often characterized by the presence of multiple domains, which make specific contributions to their cellular… (More)
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1999
1999
Id proteins not only regulate cell differentiation negatively, but they also promote growth, immortalization, and apoptosis. To… (More)
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Highly Cited
1998
Highly Cited
1998
Correct folding of newly synthesized polypeptides is thought to be facilitated by Hsp70 molecular chaperones in conjunction with… (More)
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1995
1995
We have isolated cDNA clone encoding a protein that can associate with Id, a helix-loop-helix (HLH) protein. This protein is… (More)
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1993
1993
We here isolated and characterized a cDNA clone encoding 40-kDa heat-shock protein hsp40 from cDNA expression library of human… (More)
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Highly Cited
1992
Highly Cited
1992
A putative Z-DNA binding protein, named zuotin, was purified from a yeast nuclear extract by means of a Z-DNA binding assay using… (More)
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