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The functional study of DEK in 786-O cells

ABSTRACT: The functional study of DEK in 786-O cells

PROVIDER: PRJNA1017370 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR26059906_1.fastq.gz	Fastqsanger.gz
	SRR26059906_2.fastq.gz	Fastqsanger.gz
	SRR26059907_1.fastq.gz	Fastqsanger.gz
	SRR26059907_2.fastq.gz	Fastqsanger.gz
	SRR26060212_1.fastq.gz	Fastqsanger.gz

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The functional study of DEK in 786-O cells [RNA]

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The functional study of DEK in 786-O cells [ChIP]

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The functional study of DEK in 786-O cells [ATAC]

Project description:The functional study of DEK in 786-O cells [ATAC]

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The functional study of DEK in 786-O cells [ChIP]

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The functional study of DEK in 786-O cells [RNA]

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786-O and 786-VHL in EMCV study

Project description:786-0 is a cell line derived from a clear cell renal carcinoma. Previous studies have shown that the 786-O cell line harbors an inactivating mutation in the von-Hippel Lindau (VHL) gene. Mutations in the VHL gene occur in the majority of sporadic clear cell renal cell. To determine how inactivation of the VHL affects cellular functions, we created a derivative of 786-0, which we call 786-VHL in which a functional allele of VHL has been introduced back into the 786-O cell line. The renal cell carcinoma cell line 786-0, which harbors a mutated allele of VHL, was compared to a cell line derived from 786-0, termed 786-VHL, that contains a functional allele of VHL. Genes whose expression characteristics were dependent on functional VHL were identified.

2010-06-23 | E-GEOD-22256 | biostudies-arrayexpress

786-O and 786-VHL in EMCV study

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The functional study of DEK in 786-O cells

Project description:This SuperSeries is composed of the SubSeries listed below.

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Structural basis of the DEK-nucleosome complex and its functional implications

Project description:The nuclear factor Dek is notably enriched within chromatin; nevertheless, the precise binding mechanism of Dek to the nucleosome remains elusive. In this study, we employ cryo-electron microscopy (cryo-EM) to elucidate the high-resolution structure of the Dek-Nucleosome Core Particle (NCP) complex. We identify specific domains responsible for DEK interaction with the histone octamer and DNA within the nucleosome. The veracity of these binding domains is confirmed through a series of meticulous biochemical experiments. Subsequently, cellular experiments reveal that Dek lacking nucleosome-binding capacity exhibits a deficiency in chromatin interaction. Remarkably, this impairment induces a shift towards the primitive endoderm fate in mouse embryonic stem cells, underscoring the pivotal role of Dek in determining cell fate through its nucleosomal interactions.

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