Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA516249 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:To investigate the pathogenesis of malignant phyllodes tumors of the breast, we used lncRNA+mRNA microarray expression profiling as a platform to investigate lncRNAs that play a key role in the malignant progression of phyllodes tumors of the breast.A total of 4 cases of breast fibroadenomas, 6 cases of benign phyllodes tumors and 6 cases of malignant phyllodes tumors were included. Fibroadenomas and benign phyllodes tumors were used as controls to screen out significantly differentially expressed lncrnas in malignant phyllodes tumors.
2024-06-20 | GSE235267 | GEO
Project description:WG-DASL expression of breast fibroepithelial lesions Breast fibroepithelial lesions are biphasic tumors and include fibroadenomas and phyllodes tumors. Fibroadenomas are clinically benign while phyllodes tumors are more unpredictable in biological behavior, with potential for recurrence. Differentiating the tumors may be challeneging when they have overlapping clinical and histological features especially on the core biopsies
2016-04-29 | GSE78071 | GEO
Project description:Classification of fibroadenomas and phyllodes tumors
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Project description:Genome wide DNA methylation profiling of phyllodes tumour, fibroadenoma and metaplastic breast cancer samples. The Illumina Infinium Methylation EPIC v1.0 BeadChip Array was used to obtain DNA methylation profiles across approximately 866,000 CpGs from primary tumours. Samples included a range of grades of phyllodes tumours (n=29), fibroadenoma (n=2), and metaplastic breast cancer (n=2).
2023-12-15 | GSE231574 | GEO
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Project description:Targeted sequencing of phyllodes tumors of the breast
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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
Project description:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.
2019-07-31 | GSE114179 | GEO