Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Integrated computational analysis identifies therapeutic targets with dual action in cancer cells and T cells

ABSTRACT: Integrated computational analysis identifies therapeutic targets with dual action in cancer cells and T cells

PROVIDER: PRJNA1089567 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR28387375_1.fastq.gz	Fastqsanger.gz
	SRR28387375_2.fastq.gz	Fastqsanger.gz
	SRR28387376_1.fastq.gz	Fastqsanger.gz
	SRR28387376_2.fastq.gz	Fastqsanger.gz
	SRR28387377_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 42

Similar Datasets

Integrated computational analysis identifies therapeutic targets with dual action in cancer cells and T cells

Project description:Many cancer drugs that target cancer cell pathways have detrimental effects on the immune system. We developed a computational platform for the identification of therapeutic targets with beneficial effects in both cancer and immune cells. ICRAFT (https://icraft.pku-genomics.org/) enables integrated analysis of immune-related CRISPR screen datasets, scRNA-Seq data, and pre-treatment RNA-Seq data from clinical trials. This platform enabled the discovery of a substantial number of targets with dual action in cancer cells and T cells. Among these, TNFAIP3, a ubiquitin-editing enzyme also known as A20, emerged as a leading target. Inactivating TNFAIP3 in cancer cells sensitizes them to immune attacks by activating the NF-κB pathway, while targeting it in T cells significantly enhances their antitumor efficacy.

2024-12-25 | GSE261915 | GEO

Dual-action host-guest chemistry suppresses virulence in Pseudomonas aeruginosa

Project description:Dual-action host-guest chemistry suppresses virulence in Pseudomonas aeruginosa

| PRJNA758067 | ENA

Dual-action host-guest chemistry suppresses virulence in Pseudomonas aeruginosa

Project description:This study describes the influence of selected synthetic macrocycle on the gene expression in Pseudomonas aeruginosa PAO1. In this work, we propose two distinct functionalities responsible for a dual mechanism of action. We identified a water-soluble pillararene whose inner cavity tightly binds to specific homoserine lactones (HSLs) thereby interfering with interbacterial signalling, leading to effective synchronized suppression of exotoxins and biofilms in P. aeruginosa. An additional concerted mechanism of action is suggested that involves the cationic functional side groups on the pillararene that disrupt both the bacterial outer membrane and biofilms, to increase the penetration and efficacy of intracellular antibiotics.

2023-02-27 | GSE182853 | GEO

Dual-action host-guest chemistry suppresses PAO1 virulence in A549 cell line model

Project description:Dual-action host-guest chemistry suppresses PAO1 virulence in A549 cell line model

| PRJNA758054 | ENA

Computational Genomics of Preeclampsia

Project description:Computational Genomics of Preeclampsia

| PRJNA809816 | ENA

Computational Genomics of Preeclampsia

Project description:Computational Genomics of Preeclampsia

| PRJNA809817 | ENA

A covalent PIN1 inhibitor selectively targets cancer cells by a dual mechanism of action.

Project description:The prolyl isomerase PIN1, a critical modifier of multiple signalling pathways, is overexpressed in the majority of cancers and its activity strongly contributes to tumour initiation and progression. Inactivation of PIN1 function conversely curbs tumour growth and cancer stem cell expansion, restores chemosensitivity and blocks metastatic spread, thus providing the rationale for a therapeutic strategy based on PIN1 inhibition. Notwithstanding, potent PIN1 inhibitors are still missing from the arsenal of anti-cancer drugs. By a mechanism-based screening, we have identified a novel covalent PIN1 inhibitor, KPT-6566, able to selectively inhibit PIN1 and target it for degradation. We demonstrate that KPT-6566 covalently binds to the catalytic site of PIN1. This interaction results in the release of a quinone-mimicking drug that generates reactive oxygen species and DNA damage, inducing cell death specifically in cancer cells. Accordingly, KPT-6566 treatment impairs PIN1-dependent cancer phenotypes in vitro and growth of lung metastasis in vivo.

| S-EPMC5472749 | biostudies-literature

Computational identification of clonal cells in single-cell CRISPR screens

Project description:Computational identification of clonal cells in single-cell CRISPR screens

| PRJNA771674 | ENA

Computational map of colon polyps

Project description:Computational map of colon polyps

| PRJNA929038 | ENA

A dual-action niclosamide-based prodrug that targets cancer stem cells and inhibits TNBC metastasis.

Project description:Chemotherapy typically destroys the tumor mass but rarely eradicates the cancer stem cells (CSCs) that can drive metastatic recurrence. A key current challenge is finding ways to eradicate CSCs and suppress their characteristics. Here, we report a prodrug, Nic-A, created by combining a carbonic anhydrase IX (CAIX) inhibitor, acetazolamide, with a signal transducer and transcriptional activator 3 (STAT3) inhibitor, niclosamide. Nic-A was designed to target triple-negative breast cancer (TNBC) CSCs and was found to inhibit both proliferating TNBC cells and CSCs via STAT3 dysregulation and suppression of CSC-like properties. Its use leads to a decrease in aldehyde dehydrogenase 1 activity, CD44high/CD24low stem-like subpopulations, and tumor spheroid-forming ability. TNBC xenograft tumors treated with Nic-A exhibited decreased angiogenesis and tumor growth, as well as decreased Ki-67 expression and increased apoptosis. In addition, distant metastases were suppressed in TNBC allografts derived from a CSC-enriched population. This study thus highlights a potential strategy for addressing CSC-based cancer recurrence.

| S-EPMC10214212 | 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