Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA337913 | ENA |
REPOSITORIES: ENA
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Project description:Targeted FAIRE-sequencing of breast cancer risk regions in two breast cancer cell lines
| PRJNA337965 | ENA
Project description:Purpose: The goal of this study was to identify allele-specific open chromatin regions in breast cancer cell lines, focusing on the fraction of the genome that has been previously associated to breast-cancer risk. Methods: DNA obtained from Angilent SureSelect solution-based sequence capture was subjected to Illumina HiSeq 2500 paired-end sequencing (Illumina). We performed targeted sequencing of 3 replicated FAIRE samples per cell-line and the correspondent genomic DNA controls in two breast cancer cell lines (T47D and MDAMB134). Allele-specific analysis was performed with BaalChIP R package (version 0.1.9) with the default parameters and options. Results: Using targeted sequencing, we investigated 69 genomic loci that have been previously associated to breast cancer risk. We identified a total of 21 allele-specific SNPs in MDAMB134 and allele-specific 9 SNPs in T-47D cell lines (see processed files).
2017-01-26 | GSE85261 | GEO
Project description:Expression data from two breast cancer cell lines
| PRJNA221364 | ENA
Project description:We report the application of FAIRE seq in Human Mammary Epithelial Cells for identifying the breast cancer risk functional SNPs in enhancer region. Examination of FAIRE assay in HMEC
2013-05-10 | E-GEOD-46074 | biostudies-arrayexpress
Project description:We report the application of FAIRE seq in Human Mammary Epithelial Cells for identifying the breast cancer risk functional SNPs in enhancer region.
2013-05-10 | GSE46074 | GEO
Project description:RNA-seq in two ER+ breast cancer cell lines with and without progestins
| PRJNA282505 | ENA
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