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

Chromosome 14 open reading frame 169

Top mentioned proteins: Histone, demethylase, C22, V1a, fibrillin-1
Papers on NO66
Epigenetic Control of the Bone-master Runx2 Gene during Osteoblast-lineage Commitment by the Histone Demethylase JARID1B/KDM5B.
Montecino et al., Santiago, Chile. In J Biol Chem, Dec 2015
Importantly, knockdown of the H3K4me2/3 demethylase JARID1B, but not of the demethylases UTX and NO66, prevents repression of the Runx2 P1 promoter during myogenic differentiation of mesenchymal cells.
Expression of histone methyltransferases as novel biomarkers for renal cell tumor diagnosis and prognostication.
Jerónimo et al., Porto, Portugal. In Epigenetics, Dec 2015
We found that the expression levels of 3 genes-SMYD2, SETD3, and NO66-was significantly altered in a set of RCTs, which was further validated in a large independent cohort.
Mesenchymal Deletion of Histone Demethylase NO66 in Mice Promotes Bone Formation.
de Crombrugghe et al., Houston, United States. In J Bone Miner Res, Sep 2015
Our previous studies indicated that the Jumonji C (JmjC)-domain-containing NO66 is a histone demethylase with specificity for methylated histone H3K4 and H3K36.
Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.
Zang et al., Hefei, China. In Acta Crystallogr D Biol Crystallogr, Sep 2015
Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase.
Mesenchyme-specific overexpression of nucleolar protein 66 in mice inhibits skeletal growth and bone formation.
Krahe et al., Houston, United States. In Faseb J, Jun 2015
Previous studies showed that nucleolar protein 66 (NO66), the Jumonji C-domain-containing histone demethylase for methylated histone H3K4 and H3K36 (H3K36me), negatively regulates osteoblast differentiation in vitro by inhibiting the activity of transcription factor osterix (Osx).
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Schofield et al., Oxford, United Kingdom. In Nature, 2014
In Escherichia coli, YcfD catalyses arginine hydroxylation in the ribosomal protein L16; in humans, MYC-induced nuclear antigen (MINA53; also known as MINA) and nucleolar protein 66 (NO66) catalyse histidine hydroxylation in the ribosomal proteins RPL27A and RPL8, respectively.
Osterix and NO66 histone demethylase control the chromatin of Osterix target genes during osteoblast differentiation.
deCrombrugghe et al., Houston, United States. In J Bone Miner Res, 2014
In contrast, occupancy of the transcriptional repressors HP1 and the nucleolar protein 66 (NO66), a histone demethylase previously identified as an Osx-interacting protein, was increased at the Bsp gene in Osx-null calvarial cells.
The conserved PBAF nucleosome-remodeling complex mediates the response to stress in Caenorhabditis elegans.
Fay et al., Laramie, United States. In Mol Cell Biol, 2014
In addition, we show that PBAF cooperates with the histone demethylase, JMJC-1/NO66, to promote expression of ESRE genes following stress.
Structural insights into histone demethylase NO66 in interaction with osteoblast-specific transcription factor osterix and gene repression.
Zang et al., Hefei, China. In J Biol Chem, 2013
A JmjC domain-containing protein NO66 was previously found to participate in regulation of Osx transcriptional activity and plays an important role in osteoblast differentiation through interaction with Osx.
Genetic and molecular control of osterix in skeletal formation.
Zhou et al., Houston, United States. In J Cell Biochem, 2013
In particular, the identification of the histone demethylase NO66 as an Osx-interacting protein, which negatively regulates Osx activity opens further avenues in studying epigenetic control of Osx target genes during differentiation and maturation of osteoblasts.
Polycomb PHF19 binds H3K36me3 and recruits PRC2 and demethylase NO66 to embryonic stem cell genes during differentiation.
Bracken et al., Dublin, Ireland. In Nat Struct Mol Biol, 2012
PHF19 associates with the H3K36me3 demethylase NO66, and it is required to recruit the PRC2 complex and NO66 to stem cell genes during differentiation, leading to PRC2-mediated trimethylation of histone H3 Lys27 (H3K27), loss of H3K36me3 and transcriptional silencing.
Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.
Schofield et al., Oxford, United Kingdom. In Nat Chem Biol, 2012
Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively.
Purification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 from Homo sapiens.
Zang et al., Hefei, China. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012
NO66 crystallized in space group P3(1) or P3(2), with unit-cell parameters a = 89.35, b = 89.35, c = 304.86 A, alpha = beta = 90, gamma = 120 degrees , and the crystal is likely to contain four molecules in the asymmetric unit
Proteomics analyses of activated human optic nerve head lamina cribrosa cells following biomechanical strain.
Flanagan et al., Toronto, Canada. In Invest Ophthalmol Vis Sci, 2012
Among proteins of particular interest, also found in multiple stretch/time conditions, were bcl-2-associated athanogene 5 (BAG5), nucleolar protein 66 (NO66), and eukaryotic translation initiation factor 5A (eIF-5A).
Regulation of the osteoblast-specific transcription factor Osterix by NO66, a Jumonji family histone demethylase.
de Crombrugghe et al., Houston, United States. In Embo J, 2010
interactions between NO66 and Osx regulate Osx-target genes in osteoblasts by modulating histone methylation states
NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin.
Schmidt-Zachmann et al., Heidelberg, Germany. In Mol Biol Cell, 2004
NO66 has functions in ribosome biogenesis and in the replication or remodeling of certain heterochromatic regions
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