Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans - Wikidata - wikimedia - TriplyDB

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

http://www.wikidata.org/entity/Q34308602

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OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy Oncoprotein mdig contributes to silica-induced pulmonary fibrosis by altering balance between Th17 and Treg T cells Histone demethylases in chromatin biology and beyond Current understanding of mdig/MINA in human cancers Ascorbate as a co-factor for fe- and 2-oxoglutarate dependent dioxygenases: physiological activity in tumor growth and progression Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases as a novel regulatory mechanism in bacteria Growing with the wind. Ribosomal protein hydroxylation and cell growth Ribosomal oxygenases are structurally conserved from prokaryotes to humans NDUFAF5 Hydroxylates NDUFS7 at an Early Stage in the Assembly of Human Complex I Mdig de-represses H19 large intergenic non-coding RNA (lincRNA) by down-regulating H3K9me3 and heterochromatin The proteomic investigation reveals interaction of mdig protein with the machinery of DNA double-strand break repair Structural insights into histone demethylase NO66 in interaction with osteoblast-specific transcription factor osterix and gene repression.Systematic discovery of genetic modulation by Jumonji histone demethylases in Drosophila Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation Oncometabolites: linking altered metabolism with cancer.Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.Mina: a Th2 response regulator meets TGFβ.novPTMenzy: a database for enzymes involved in novel post-translational modifications.Hydroxylated histidine of human ribosomal protein uL2 is involved in maintaining the local structure of 28S rRNA in the ribosomal peptidyl transferase center.High-resolution structure of the Escherichia coli ribosome.A cell-permeable ester derivative of the JmjC histone demethylase inhibitor IOX1 Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.Striking Oxygen Sensitivity of the Peptidylglycine α-Amidating Monooxygenase (PAM) in Neuroendocrine Cells.Global gene expression profiling of JMJD6- and JMJD4-depleted mouse NIH3T3 fibroblasts.Post-translational modifications near the quinone binding site of mammalian complex I.Post-translational modifications are enriched within protein functional groups important to bacterial adaptation within a deep-sea hydrothermal vent environment Signaling hypoxia by hypoxia-inducible factor protein hydroxylases: a historical overview and future perspectives Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth.Carcinogenic metalloid arsenic induces expression of mdig oncogene through JNK and STAT3 activation.Increased expression of mdig predicts poorer survival of the breast cancer patients.Jmjd6, a JmjC Dioxygenase with Many Interaction Partners and Pleiotropic Functions Optimal translational termination requires C4 lysyl hydroxylation of eRF1.Specialization from synthesis: how ribosome diversity can customize protein function.Histone H3 lysine 4 methyltransferases and demethylases in self-renewal and differentiation of stem cells.The roles of Jumonji-type oxygenases in human disease.Adding a functional handle to nature's building blocks: the asymmetric synthesis of β-hydroxy-α-amino acids.Oncometabolites-driven tumorigenesis: From genetics to targeted therapy.The oxygenase Jmjd6--a case study in conflicting assignments.

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

http://www.wikidata.org/entity/Q34308602

description

2012 nî lūn-bûn

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2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2012 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2012年の論文

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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name

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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type

label

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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Nature Chemical Biology

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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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P2093

Adam P Hardy

http://www.w3.org/2001/XMLSchema#string

Adam Zayer

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Armin Thalhammer

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Atsushi Yamamoto

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Chia-Hua Ho

http://www.w3.org/2001/XMLSchema#string

David C Trudgian

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Lingzhi Gong

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Marion Schmidt-Zachmann

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Miao Jiang

http://www.w3.org/2001/XMLSchema#string

Ming Yang

http://www.w3.org/2001/XMLSchema#string

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Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection

The human mineral dust-induced gene, mdig, is a cell growth regulating gene associated with lung cancer

Expanding role of the jumonji C domain as an RNA hydroxylase

Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing

Regulation of the osteoblast-specific transcription factor Osterix by NO66, a Jumonji family histone demethylase

NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin

The AlkB domain of mammalian ABH8 catalyzes hydroxylation of 5-methoxycarbonylmethyluridine at the wobble position of tRNA

Increased expression of a Myc target gene Mina53 in human colon cancer

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Genetically-defined metabolic reprogramming in cancer

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960-962

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scholarly article

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10.1038/NCHEMBIO.1093

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12

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8

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Peter J. Ratcliffe

Christopher J. Schofield

Rasheduzzaman Chowdhury

Benedikt M. Kessler

Christoph Loenarz

Refaat B. Hamed

Mathew L Coleman

James S. McCullagh

P577

2012-10-28T00:00:00Z

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232720430

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23103944

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4972389

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