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Homo sapiens

ABSTRACT: Global DNA Hypermethylation in Down Syndrome Placenta [RNA-Seq]

PROVIDER: PRJNA179205 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR611842_1.fastq.gz	Fastqsanger.gz
	SRR611842_2.fastq.gz	Fastqsanger.gz
	SRR611843_1.fastq.gz	Fastqsanger.gz
	SRR611843_2.fastq.gz	Fastqsanger.gz
	SRR611844_1.fastq.gz	Fastqsanger.gz

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Homo sapiens

Project description:Global DNA Hypermethylation in Down Syndrome Placenta [Bisulfite-Seq]

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Project description:Global DNA Hypermethylation in Down Syndrome Placenta

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Project description:Analysis of astrocyte precursor cells in Down syndrome (RNA-seq)

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Project description:Tumor hypoxia causes DNA hypermethylation by reducing TET activity (RNA-Seq)

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Global DNA Hypermethylation in Down Syndrome Placenta [RNA-Seq]

Project description:We have performed genome-wide DNA methylation analysis at single base resolution and gene expression analysis, resulted in hypermethylation in all autosomes in DS samples, mediated by down-regulation of all three TET family genes, and down-regulation of REST/NRSF. Genes located on chr21 were up-regulated by a median of 45% in DS compared to normal villi, while genes with promoter hypermethylation were down regulated. Comparison of RNA expression in human placenta between 5 normal and 4 Trisomy 21 samples.

2013-08-06 | E-GEOD-42142 | biostudies-arrayexpress

Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

| S-EPMC2531291 | biostudies-literature

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