Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (bulkRNA-Seq and Exome-Seq)

ABSTRACT: Divergent resistance mechanisms to HER2-targeted therapies in breast cancer

ORGANISM(S): Homo sapiens

PROVIDER: GSE161420 | GEO | 2021/04/21

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (scRNA-Seq)

Project description:Divergent resistance mechanisms to HER2-targeted therapies in breast cancer

2021-04-21 | GSE161422 | GEO

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (bulkRNA-Seq and Exome-Seq)

Project description:Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (bulkRNA-Seq and Exome-Seq)

| PRJNA678282 | ENA

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer

Project description:Divergent resistance mechanisms to HER2-targeted therapies in breast cancer

| PRJNA678280 | ENA

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (scRNA-Seq)

Project description:Divergent resistance mechanisms to HER2-targeted therapies in breast cancer (scRNA-Seq)

| PRJNA678283 | ENA

Divergent resistance mechanisms to HER2-targeted therapies in breast cancer

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

2021-04-21 | GSE161423 | GEO

Mechanisms of tumor resistance to EGFR-targeted therapies.

Project description:Much effort has been devoted to development of cancer therapies targeting EGFR, based on its role in regulating cell growth. Small-molecule and antibody EGFR inhibitors have clinical roles based on their efficacy in a subset of cancers, generally as components of combination therapies. Many cancers are either initially resistant to EGFR inhibitors or become resistant during treatment, limiting the efficacy of these reagents.To review cellular resistance mechanisms to EGFR-targeted therapies.The best validated of these mechanisms include activation of classic ATP-binding casette (ABC) multidrug transporters; activation or mutation of EGFR; and overexpression or activation of signaling proteins operating in relation to EGFR. We discuss current efforts and potential strategies to override these sources of resistance. We describe emerging systems-biology-based concepts of alternative resistance to EGFR-targeted therapies, and discuss their implications for use of EGFR-targeted and other targeted therapies.

| S-EPMC2670612 | biostudies-other

Cancer-stromal cell interactions in breast cancer brain metastases induce glycocalyx-mediated resistance to HER2-targeting therapies [ATAC-seq]

Project description:In a 3D coculture with stroma cells derived from breast cancer patients’ brain metastasis, HER2+ breast cancer cells were protected from HER2-targeted therapies, particularly the EGFR/HER2 small molecule inhibitor neratinib. To get insight into how this protection arises, ATAC-seq on coculture cells with or without neratinib as performed.

2024-04-24 | GSE249459 | GEO

Cancer-stromal cell interactions in breast cancer brain metastases induce glycocalyx-mediated resistance to HER2-targeting therapies [RNA-seq]

Project description:In a 3D coculture with stroma cells derived from breast cancer patients’ brain metastasis, HER2+ breast cancer cells were protected from HER2-targeted therapies, particularly the EGFR/HER2 small molecule inhibitor neratinib. To get insight into how this protection arises, a Synthetic Notch (SynNotch) reporter model allowed to study the effect of direct contact between stroma and cancer cells.

2024-04-24 | GSE249573 | GEO

Identification of resistance mechanisms to anti-HER2 antibody in breast cancer cell line BT-474

Project description:Background: The addition of the anti-HER2 antibody pertuzumab to trastuzumab/chemotherapy treatment in HER2+ breast cancer significantly improves clinical outcome. Concomitantly, the drug-antibody conjugate T-DM1 (trastuzumab-emantasine) has demonstrated efficacy, at least equal, to the combination of trastuzumab/chemotherapy. Scientific, economic and health challenges emerge from the clinical use of these novel anti-HER2 antibodies, aimed to identify new resistance mechanisms and to select the target breast cancer population. Objectives: (1) To identify primary resistance mechanisms to anti-HER2 antibodies trastuzumab, pertuzumab, and to the combined trastuzumab/pertuzumab or pertuzumab/T-DM1 therapy, (2) To identify acquired resistance mechanisms to anti-HER2 antibodies trastuzumab, pertuzumab, and to the combined trastuzumab/pertuzumab or pertuzumab/T-DM1 therapy, (3) To develop new combinations of anti-HER2 antibodies with other targeted therapies.

2019-12-31 | GSE89216 | GEO

JNK Pathway Activation Modulates Acquired Resistance to EGFR/HER2-Targeted Therapies.

Project description:Resistance limits the effectiveness of receptor tyrosine kinase (RTK)-targeted therapies. Combination therapies targeting resistance mechanisms can considerably improve response, but will require an improved understanding of when particular combinations will be effective. One common form of resistance is bypass signaling, wherein RTKs not targeted by an inhibitor can direct reactivation of pathways essential for survival. Although this mechanism of resistance is well appreciated, it is unclear which downstream signaling events are responsible. Here, we apply a combined experimental- and statistical modeling-based approach to identify a set of pathway reactivation essential for RTK-mediated bypass resistance. Differences in the downstream pathway activation provided by particular RTKs lead to qualitative differences in the capacity of each receptor to drive therapeutic resistance. We identify and validate that the JNK pathway is activated during and strongly modulates bypass resistance. These results identify effective therapeutic combinations that block bypass-mediated resistance and provide a basic understanding of this network-level change in kinase dependence that will inform the design of prognostic assays for identifying effective therapeutic combinations in individual patients. Cancer Res; 76(18); 5219-28. ©2016 AACR.

| S-EPMC5026573 | 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