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The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

ABSTRACT: The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

PROVIDER: PRJNA1186555 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31361217_1.fastq.gz	Fastqsanger.gz
	SRR31361217_2.fastq.gz	Fastqsanger.gz
	SRR31361218_1.fastq.gz	Fastqsanger.gz
	SRR31361218_2.fastq.gz	Fastqsanger.gz
	SRR31361219_1.fastq.gz	Fastqsanger.gz

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The effects of wild-type Usp24 or catalytically inactive USP24 on EgfrL858R-driven lung tumor specimens.

Project description:Ubiquitin-specific peptidase 24 (USP24), a cysteine protease, functions as deubiquitinating enzyme that recognizes and removes ubiquitin from the target protein. USP24 is overexpressed in various cancers and regulates the stability of proteins involved in cancer metastasis, cancer stemness, and drug resistance. While the expression profile alteration in tumor microenvironment upon USP24 inhibition is unrevealed. Through RNA-seq, we have characterized that USP24 catalytically inactivation upregulates activation of immune response and lymphocyte activation-related genes in lung tumors from EgfrL858RUsp24C1695A mice

2025-04-22 | GSE281983 | GEO

Mouse ES cells expressing catalytically inactive Ring1B display impaired Ring1B and H3K27me3 deposition.

Project description:ChIP-seq for H3K27me3 and Ring1B was performed in WT mESCs and mESCs containing catalytically inactive Ring1B (I53A mutant). Cells expressing catalytically inactive Ring1B maintain the spatial distribution of Ring1B and H3K27me3 but at reduced levels. These findings support the notion that PRC2 recruitment is, in part, dependent on H2A ubiquitination (H2AK119ub). Two biological replicates were performed for Ring1B and H3K27me3 ChIPs in WT and Ring1B I53A/I53A mouse ESCs. Input chromatin was sequenced for each replicate as a control for ChIP enrichment.

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Mouse ES cells expressing catalytically inactive Ring1B display impaired Ring1B and H3K27me3 deposition.

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Transcriptome profile of oocytes expressing a catalytically inactive knock-in allele of Ago2

Project description:The RNase III enzyme DICER generates both microRNAs (miRNAs) and endogenous short interfering RNAs (endo-siRNAs). Dicer deletion in mouse oocytes leads to female infertility due to defects during meiosis I. Because miRNA function is suppressed in mouse oocytes, it has been proposed that endo-siRNAs may have a role during female meiosis. By utilizing a catalytically inactive knock-in allele of AGO2 specifically in oocytes, we disrupt the function of siRNAs and analyze the transcriptome of these oocytes in comparison with Ago2 null, and Dicer null oocytes. Germinal vesicle-intact, full-grown oocytes were collected from eCG-primed females expressing a catalytically inactive knock-in allele of Ago2 (Ago2 ADH) specifically in oocytes. Oocytes were also collected from Ago2 null and Ago2 fl/fl oocytes, as well as Dicer wild-type and null mice. Oocytes were freed of attached cumulus cells by pipetting. Twenty oocytes collected from 3 different mice were used for high-throughput RNA sequencing. Three replicates for all genotypes except Ago2 null (two). The mouse background strain is "mostly" C57BL6, i.e., it is a cross between 3 different transgenic mice of different strains.

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NSUN7 is an RNA:m5C catalytically inactive protein that regulates sperm flagellum assembly

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Catalytically inactive Ring1B maintains near wildtype levels of gene expression in mESCs

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NSUN7 is an RNA:m5C catalytically inactive protein that regulates sperm flagellum assembly [scRNA-seq]

Project description:NSUN7 is an RNA:m5C catalytically inactive protein that regulates sperm flagellum assembly [scRNA-seq]

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Catalytically inactive Ring1B maintains near wildtype levels of gene expression in mESCs

Project description:This experiment was designed to determine the extent of gene misregulation in mESCs containing catalytically dead Ring1B in comparison to mESCs lacking Ring1B.

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