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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

PIH1 Pih1p

NOP17, Pih1, Pih1p
Top mentioned proteins: Hsp90, Nop58p, POLYMERASE, NUFIP, ATPase
Papers on NOP17
Structure/Function Analysis of Protein-Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP Assembly.
Manival et al., Vandœuvre-lès-Nancy, France. In J Mol Biol, Sep 2015
They contain one guide RNA and four core proteins and their in vivo assembly requires numerous factors including (HUMAN/Yeast) BCD1/Bcd1p, NUFIP1/Rsa1p, ZNHIT3/Hit1p, the R2TP complex composed of protein PIH1D1/Pih1p and RPAP3/Tah1p that bridges the R2TP complex to the HSP90/Hsp82 chaperone and two AAA+ ATPases.
(1)H, (15)N and (13)C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complex.
Quinternet et al., Vandœuvre-lès-Nancy, France. In Biomol Nmr Assign, Apr 2015
We report the nearly complete (1)H, (15)N and (13)C resonance assignment of the complex formed by the C-terminal domains of Pih1 and Tah1 from S. cerevisiae and evidence the folding ability of Tah1 under complex formation.
Nop17 is a key R2TP factor for the assembly and maturation of box C/D snoRNP complex.
Oliveira et al., São Paulo, Brazil. In Bmc Mol Biol, 2014
Nop17, also known as Pih1, has been shown to be a constituent of the R(2)TP (Rvb1, Rvb2, Tah1, Pih1) and to participate in box C/D snoRNP assembly by its interaction with Nop58.
The R2TP chaperone complex: its involvement in snoRNP assembly and tumorigenesis.
Saeki et al., In Biomol Concepts, 2014
R2TP was originally identified in yeast Saccharomyces cerevisiae as Hsp90 interacting complex, and is composed of four different proteins: Rvb1, Rvb2, Tah1, and Pih1.
Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
Prodromou et al., Brighton, United Kingdom. In Structure, 2014
Hsp90 involvement in the assembly of snoRNPs, RNA polymerases, PI3-kinase-like kinases, and chromatin remodeling complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90.
Nutritional status modulates box C/D snoRNP biogenesis by regulated subcellular relocalization of the R2TP complex.
Houry et al., In Genome Biol, 2013
The highly conserved R2TP complex, comprising the proteins Rvb1, Rvb2, Tah1, and Pih1, has been shown to be required for box C/D snoRNP biogenesis and assembly; however, the molecular basis of R2TP chaperone-like activity is not yet known.
Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.
Charpentier et al., Vandœuvre-lès-Nancy, France. In Nucleic Acids Res, 2013
In yeast, protein Rsa1 acts as a platform, interacting with both the RNA-binding core protein Snu13 and protein Pih1 of the Hsp82-R2TP chaperone complex.
Identification of R2TP complex of Leishmania donovani and Plasmodium falciparum using genome wide in-silico analysis.
Tuteja et al., New Delhi, India. In Commun Integr Biol, 2013
Within R2TP complex, Pih1 tightly interacts with Rvb1/Rvb2 and with Tah1 to form R2TP macromolecular complex.
High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.
Manival et al., Vandœuvre-lès-Nancy, France. In Structure, 2013
This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2.
The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminus.
Zhao et al., Toronto, Canada. In J Biol Chem, 2013
Pih1 is an unstable protein and a subunit of the R2TP complex that, in yeast Saccharomyces cerevisiae, also contains the helicases Rvb1, Rvb2, and the Hsp90 cofactor Tah1.
Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90.
Houry et al., Valencia, Spain. In J Biol Chem, 2012
Tah1 and Pih1 are novel Hsp90 interactors.
The R2TP complex: discovery and functions.
Houry et al., Toronto, Canada. In Biochim Biophys Acta, 2012
It was found that Rvb1 and Rvb2 form a tight functional complex with Pih1 (Protein interacting with Hsp90) and Tah1 (TPR-containing protein associated with Hsp90), which are two Hsp90 interactors.
PIH1D1, a subunit of R2TP complex, inhibits doxorubicin-induced apoptosis.
Kamisaki et al., Suita, Japan. In Biochem Biophys Res Commun, 2011
These results suggest that PIH1D1 may also function as a novel modulator of apoptosis pathway.
The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activity.
Moréra et al., Gif-sur-Yvette, France. In J Biol Chem, 2010
a role for the Pih1-Tah1 cochaperone complex in the recruitment of client proteins such as core RNP proteins to Hsp90
[Effect of PIH1D1 on the degradation of its binding protein SNF5].
Shen et al., Beijing, China. In Zhongguo Yi Xue Ke Xue Yuan Xue Bao, 2009
PIH1D1 may stabilize SNF5 by attenuating its proteasome degradation pathway.
High-resolution mapping of the protein interaction network for the human transcription machinery and affinity purification of RNA polymerase II-associated complexes.
Coulombe et al., Montréal, Canada. In Methods, 2009
Is part of an RNA polymerase II-associated complex with possible chaperone activity.
Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex activity that regulates snoRNA accumulation.
Houry et al., Toronto, Canada. In J Cell Biol, 2008
We identify a function for the chaperone in RNA processing and maintenance. This functionality of Hsp90 involves two recently identified interactors of the chaperone: Tah1 and Pih1/Nop17.
Hsp90: a chaperone for protein folding and gene regulation.
Houry et al., Toronto, Canada. In Biochem Cell Biol, 2005
We identified 2 highly conserved novel Hsp90 cofactors, termed Tah1 and Pih1, that bind to the chaperone and that also associate physically and functionally with the essential DNA helicases Rvb1 and Rvb2.
Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone.
Houry et al., Toronto, Canada. In Cell, 2005
Two novel Hsp90 cofactors, Tah1 (YCR060W) and Pih1 (YHR034C), were also identified.
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