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R2TP complex

Known as: R2TP complex location 
A highly conserved protein complex comprised of two ATP-dependent DNA helicases (Rvb1p and Rvb2p in yeast, Pontin52 and Reptin52 in humans), Pih1p in… Expand
National Institutes of Health

Papers overview

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2017
2017
Summary The R2TP complex, comprising the Rvb1p-Rvb2p AAA-ATPases, Tah1p, and Pih1p in yeast, is a specialized Hsp90 co-chaperone… Expand
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2017
2017
Pontin (Ruvbl1) and Reptin (Ruvbl2) are closely related AAA ATPases. They are components of the Ruvbl1-Ruvbl2-Tah1-Pih1 (R2TP… Expand
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Review
2017
Review
2017
ABSTRACT Box C/D and box H/ACA snoRNAs are abundant non-coding RNAs that localize in the nucleolus and mostly function as guides… Expand
Review
2015
Review
2015
The R2TP complex is a HSP90 co-chaperone, which consists of four subunits: PIH1D1, RPAP3, RUVBL1, and RUVBL2. It is involved in… Expand
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2014
2014
BackgroundBox C/D snoRNPs, which are typically composed of box C/D snoRNA and the four core protein components Nop1, Nop56, Nop58… Expand
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2013
2013
The ubiquitous Hsp90 chaperone participates in snoRNP and RNA polymerase assembly through interaction with the R2TP complex. This… Expand
Review
2012
Review
2012
The two closely related AAA+family ATPases Rvb1 and Rvb2 are part of several critical multiprotein complexes, and, thus, are… Expand
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Highly Cited
2010
Highly Cited
2010
TEL2 interacts with and is essential for the stability of all phosphatidylinositol 3-kinase-related kinases (PIKKs), but its… Expand
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2010
2010
We have previously reported that the two components of R2TP complex, RNA polymerase II-associated protein 3 (RPAP3), and Reptin… Expand
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Highly Cited
2008
Highly Cited
2008
Hsp90 is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes. In this study… Expand
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