Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Homo sapiens

ABSTRACT: Genomic Analysis of Nasopharyngeal Carcinoma Reveals TME-based Subtypes

PROVIDER: PRJNA397538 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR5908750.fastq.gz	Fastqsanger.gz
	SRR5908750_1.fastq.gz	Fastqsanger.gz
	SRR5908750_2.fastq.gz	Fastqsanger.gz
	SRR5908760.fastq.gz	Fastqsanger.gz
	SRR5908760_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 339

Similar Datasets

Homo sapiens

Project description:The genomic landscape of nasopharyngeal carcinoma

| PRJNA267603 | ENA

Homo sapiens

Project description:Integrative Transcriptome Analysis Reveals Common Molecular Subtypes of Human Hepatocellular Carcinoma

| PRJNA108343 | ENA

Homo sapiens

Project description:Nasopharyngeal carcinoma cell lines (expression analysis)

| PRJNA123145 | ENA

Homo sapiens

Project description:Integrative Transcriptome Analysis Reveals Common Molecular Subtypes of Human Hepatocellular Carcinoma (HT-HG_U133A)

| PRJNA108143 | ENA

Homo sapiens

Project description:Nasopharyngeal carcinoma cell lines (copy number analysis)

| PRJNA123147 | ENA

Homo sapiens

Project description:Human nasopharyngeal carcinoma

| PRJNA111223 | ENA

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

Homo sapiens

Project description:nasopharyngeal carcinoma versus nasopharyngeal phlogistic tissue reference

| PRJNA106827 | ENA