Ribosomal oxygenases are structurally conserved from prokaryotes to humans - Test2 - elhamkhani - TriplyDB

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

http://www.wikidata.org/entity/Q27683705

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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 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 Proteomic Characterization of the World Trade Center dust-activated mdig and c-myc signaling circuit linked to multiple myeloma The proteomic investigation reveals interaction of mdig protein with the machinery of DNA double-strand break repair Systematic discovery of genetic modulation by Jumonji histone demethylases in Drosophila The Succinated Proteome of FH-Mutant Tumours Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases Protein Hydroxylation Catalyzed by 2-Oxoglutarate-dependent Oxygenases.Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases.Mina: a Th2 response regulator meets TGFβ.novPTMenzy: a database for enzymes involved in novel post-translational modifications.Oxygen and glucose deprivation induces widespread alterations in mRNA translation within 20 minutes Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily Signaling hypoxia by hypoxia-inducible factor protein hydroxylases: a historical overview and future perspectives Oxygen sensing by protozoans: how they catch their breath.Modifying the maker: Oxygenases target ribosome biology.Inhibitors of Protein Methyltransferases and Demethylases.New horizons in hypoxia signaling pathways.A SNP uncoupling Mina expression from the TGFβ signaling pathway.Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding.Inhibitors of both the N-methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases.YcfDRM is a thermophilic oxygen-dependent ribosomal protein uL16 oxygenase.JMJD5 is a human arginyl C-3 hydroxylase.Phylogenetic and genomic analyses of the ribosomal oxygenases Riox1 (No66) and Riox2 (Mina53) provide new insights into their evolution.The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases The emerging roles of ribosomal histidyl hydroxylases in cell biology, physiology and disease Loss of mdig expression enhances DNA and histone methylation and metastasis of aggressive breast cancer

P2860

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P2860

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

http://www.wikidata.org/entity/Q27683705

description

2014 nî lūn-bûn

@nan

2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@ast

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@en

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@nl

type

label

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@ast

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@en

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@nl

prefLabel

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@ast

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@en

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

@nl

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Ribosomal oxygenases are structurally conserved from prokaryotes to humans

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P2093

Aiden J Doherty

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

Chia-Hua Ho

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

Claire Phillips

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

Ewa S Pilka

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

Gavin C Fox

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

Ian J Clifton

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

Kathryn L Kavanagh

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

Melanie Vollmar

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

Rok Sekirnik

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

Stanley S Ng

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

P2860

phyloXML: XML for evolutionary biology and comparative genomics

Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases

Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

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

Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains

Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy

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422-426

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scholarly article

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2590827

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10.1038/NATURE13263

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7505

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510

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Christopher J. Schofield

Rasheduzzaman Chowdhury

Nadia J Kershaw

Michael A McDonough

Frank von Delft

João R C Muniz

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2014-05-11T00:00:00Z

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262230817

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1012441101

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24814345

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4066111

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