Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Trim2b mediates protection against SVCV infection by degrading NLRP12-like and viral SVCV-N/SVCV-G proteins

ABSTRACT: Trim2b mediates protection against SVCV infection by degrading NLRP12-like and viral SVCV-N/SVCV-G proteins

PROVIDER: PRJNA971593 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR24511700_1.fastq.gz	Fastqsanger.gz
	SRR24511700_2.fastq.gz	Fastqsanger.gz
	SRR24511701_1.fastq.gz	Fastqsanger.gz
	SRR24511701_2.fastq.gz	Fastqsanger.gz
	SRR24511702_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 24

Similar Datasets

Trim2b mediates protection against SVCV infection by degrading NLRP12-like and viral SVCV-N/SVCV-G proteins

Project description:In the present study, we report the functional characterization of zebrafish trim2b. we show that zebrafish trim2b plays a protective role in the host defense against SVCV infection. During SVCV infection, the in vivo studies revealed that trim2b overexpression led to the decreased virus loads and increased survival rate. Zebrafish trim2b deficiency led to the increased virus loads and decreased survival rate. In addition, Zebrafish trim2b deficiency leads higher numbers of immune related DEGs and signaling pathways enriched during the SVCV infection or uninfection. Among them, NOD-like receptor signaling pathway was significantly enriched. The present study characterized two NLRs degraded by trim2b plays a negative role in the host defense against SVCV infection.

2024-04-26 | GSE232313 | GEO

RNAseq analysis of gene expression in colorectal tumors of wild-type and Nlrp12-/- mice

Project description:Background: NLRP12 is a cytosolic pattern recognition receptor in the family of NOD-like receptor. NLRP12 has been shown to suppress colorectal tumorigenesis. However, the precise mechansim of NLRP12-mediated regualtion of colorectal cancer is unknown. Results: RNAseq data demonstrate higher expression of oncogenes, matrix degrading enzymes such as matrix metaloproteinases (MMPs), and genes involved in tumor invasion in Nlrp12-/- compared to wild-type tumors. Notably, several of the genes highly induced in Nlrp12-/- tumors are regulated by the Wnt/b-catenin pathway. Conclusion: NLRP12 negatively regualtes the Wnt/b-catenin pathway to suppress colorectal cancer progression and invasion.

2020-10-01 | GSE149769 | GEO

The Nlrp12 inflammasome negatively regulates NOD2-mediated adjuvanticity, endotoxic shock and host defence afforded by an immunomodulatory muropeptide.

Project description:Transcriptional profiling of intestinal response to Citrobacter rodentium in wild-type and Nlrp12-deficient mice Four-conditions experiment, Nlrp12-deficient mouse infected by Citrobacter rodentium at day 7 versus non-infected Nlrp12-deficient mice with two biologicals replicates , Wild-type mouse infected by Citrobacter rodentium at day 7 versus non-infected Wild-type mice with two biologicals replicates and Nlrp12-deficient mouse infected by Citrobacter rodentium versus Control mouse infected by Citrobacter rodentium at 2 differents times ( day 0 and post infection at day 7 ) with three biologicals replicates

2015-07-25 | E-GEOD-59940 | biostudies-arrayexpress

The Nlrp12 inflammasome negatively regulates NOD2-mediated adjuvanticity, endotoxic shock and host defence afforded by an immunomodulatory muropeptide.

Project description:Transcriptional profiling of intestinal response to Citrobacter rodentium in wild-type and Nlrp12-deficient mice

2015-07-25 | GSE59940 | GEO

Autophagy mediates degradation of nuclear lamina

Project description:Autophagy is a catabolic membrane trafficking process involved in degradation of cellular constituents through lysosomes, which maintains cell and tissue homeostasis. While much attention has been focused on autophagic turnover of cytoplasmic materials, little is known regarding the role of autophagy in degrading nuclear components. Here we report that autophagy machinery mediates degradation of nuclear lamina in mammalian cells, a process we term laminophagy. The autophagy protein LC3 is present in the nucleus and directly interacts with the nuclear lamina protein Lamin B1, and associates with lamin-associated domains (LADs) on chromatin. This interaction does not downregulate Lamin B1 during starvation, but mediates nuclear lamina degradation upon tumorigenic insults, such as by oncogenic Ras. Laminophagy is achieved by nucleus-to-cytosol transport that delivers Lamin B1 to lysosome for degradation. Inhibiting autophagy or LC3-Lamin B1 interaction prevents oncogenic Ras-induced Lamin B1 loss and delays oncogene-induced cell cycle arrest. Our study unveils a role of autophagy in degrading nuclear materials, and suggests laminophagy as a guarding mechanism protecting cells from tumorigenesis.

2015-10-08 | GSE63440 | GEO

Biofilms of the PAH-degrading Sphingomonas sp. LH128 on solute stress when actively degrading and growing on phenanthrene

2012-06-18 | GSE38296 | GEO

Nlrp12 expressing heamatopoitic cells maintain the intestinal microbiome symbiosis.

Project description:Nlrp12-/- mice host a dysbiotic microbiome. After performing bone marrow transplantation study, we found mice receiving Nlrp12-/- haematopoitic cells pheno-copied the dysbiotic microbiome in the Nlrp12-/- mice.

| PRJEB18700 | ENA

Tumor Necrosis Factor Associated Factor 2 Mediates Cardiac Protection Through Non-canonical NF-κB Signaling

Project description:Tumor Necrosis Factor Associated Factor 2 Mediates Cardiac Protection Through Non-canonical NF-κB Signaling

| PRJNA420992 | ENA

Biofilms of the PAH-degrading Sphingomonas sp. LH128 on solute stress when actively degrading and growing on phenanthrene

Project description:This study examines the transcriptomic response of biofilms of the PAH-degrading Sphingomonas sp. LH128 on solute stress when actively degrading and growing on the PAH compound. To address the effect of solute stress on bacterial physiology and transcriptomic response, NaCl was used as osmolyte. Both acute and chronic solute stress was invoked to assess differences in short-term and long-term responses. Transcriptomic response of phenanthrene degrading Sphingomonas sp. LH128 biofilms as a response to short-term and long-term solute (NaCl) stress was studied using genome-wide gene expression analysis. For this purpose, the strain was grown in customized continuous glass flow chambers that contain solid phenanthrene as a sole carbon source and that allow easy recovery of biofilm cells for transcriptomic and physiological analysis. A NaCl stress of 450 mM was imposed on LH128 biofilms growing on phenanthrene crystals coated on glass slides either for 4 hours (acute stress) or for 3 days (chronic stress). RNA was extracted from the biofilm and cDNA was synthesized and labeled with Cy3. Transcriptomic response in the stressed biofilms of three replicates per conditions were analyzed and compared with non-stressed

2012-06-18 | E-GEOD-38296 | biostudies-arrayexpress

TRIM35 mediates protection against influenza infection by activating TRAF3 and degrading viral PB2.

Project description:Tripartite motif (TRIM) family proteins are important effectors of innate immunity against viral infections. Here we identified TRIM35 as a regulator of TRAF3 activation. Deficiency in or inhibition of TRIM35 suppressed the production of type I interferon (IFN) in response to viral infection. Trim35-deficient mice were more susceptible to influenza A virus (IAV) infection than were wild-type mice. TRIM35 promoted the RIG-I-mediated signaling by catalyzing Lys63-linked polyubiquitination of TRAF3 and the subsequent formation of a signaling complex with VISA and TBK1. IAV PB2 polymerase countered the innate antiviral immune response by impeding the Lys63-linked polyubiquitination and activation of TRAF3. TRIM35 mediated Lys48-linked polyubiquitination and proteasomal degradation of IAV PB2, thereby antagonizing its suppression of TRAF3 activation. Our in vitro and in vivo findings thus reveal novel roles of TRIM35, through catalyzing Lys63- or Lys48-linked polyubiquitination, in RIG-I antiviral immunity and mechanism of defense against IAV infection.

| S-EPMC7719147 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data