Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Homo sapiens

ABSTRACT: SKBR3 48h Lapatinib+JQ1

PROVIDER: PRJNA278881 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR1925284.fastq.gz	Fastqsanger.gz
	SRR1925286.fastq.gz	Fastqsanger.gz
	SRR1925326.fastq.gz	Fastqsanger.gz
	SRR1925328.fastq.gz	Fastqsanger.gz

Items per page:

1 - 4 of 4

Similar Datasets

Homo sapiens

Project description:BT474 48h Lapatinib+JQ1 transcriptome response

| PRJNA278887 | ENA

Homo sapiens

Project description:Lapatinib-resistant SKBR3 + JQ1 + I-BET151 for 8 days

| PRJNA278888 | ENA

Adaptive responses of the HER2+ SKBR-3 and BT474m1 cell lines to lapatinib and JQ1

Project description:SKBR-3 or BT474m1 HER2+ breast cancer cells were treated with either DMSO, 300nM lapatinib, 300nM JQ1, or lapatinib and JQ1 in combination for 48h.

2020-10-26 | GSE160018 | GEO

Acquired resistance to lapatinib

Project description:These studies are aimed at understanding gene expression chnages in a Her2 positive breast cancer cell line that has developed acquired resistance to lapatinib. Samples include SKBR3 parental and resistant (SKBR3-R) under basal conditions and in response to 0.1 and 1uM lapatinib treatment after 24 hours.

2012-06-30 | GSE38376 | GEO

ERRalpha mediates metabolic adaptations that drive lapatinib resistance in breast cancer (ERRalpha binding profiles in breast cancer cells by ChIP-seq)

2016-06-15 | E-GEOD-81651 | biostudies-arrayexpress

A novel miRNA fingerprint inversely associated with breast cancer progression in SKBR3 cells challenged with all-trans retinoic acid and lapatinib

Project description:In SKBR3 cells, simultaneous targeting of RARM-kM-1 with all-trans retinoic acid (ATRA) and HER2 with lapatinib results in synergistic anti-tumor responses. SKBR3 cells were treated with vehicle (DMSO), lapatinib (100 nM), ATRA (100 nM) or lapatinib+ATRA for 36 hours and miRNA expression profile was determined by one-color Agilent microarray experiments.

2015-04-30 | E-MTAB-3097 | biostudies-arrayexpress

Enhancer analysis of HER2+ cell lines SKBR-3 (ER-) and BT474m1 (ER+) in response to lapatinib and JQ1 and analysis of FOXA1 chromatin binding in SKBR-3 cells in response to lapatinib and JQ1 and impact of FOXA1 knockdown on BRD4 and MED1

Project description:SKBR-3 and BT474m1 HER2+ breast cancer cell lines were treated with lapatinib, JQ1, or lapatinib and JQ1 or (for SKBR-3) treated with siRNA pools (non-targeting control or FOXA1) prior to drug treatment before being used for ChIPseq (BRD4, MED1, H3K27Ac, or FOXA1 (for SKBR-3))

2020-11-03 | GSE160667 | GEO

ERRalpha mediates metabolic adaptations that drive lapatinib resistance in breast cancer (gene expression profiles)

Project description:Ablation of ERRalpha significantly delays ERBB2-induced mammary tumorigenesis and ERRalpha regulates genes of the ERBB2 amplicon. To further investigate the relationship between ERRalpha activity and RTK signaling, we depleted ERRalpha in SKBr3 cells upon serum starvation, EGF treatment or heregulin treatment. Inhibition of ERBB2 signaling using the RTK inhibitor lapatinib impacts on ERRalpha stability. Since we have shown that the development of lapatinib-resistance restaures the expression of ERRalpha in breast cancer cells, we performed depletion of ERRalpha in SKBr3 cells that have developped resistance to lapatinib treatment in order to identify a potential reprogramming of ERRa transcriptional activity associated to lapatinib resistance, For the study of growth factor effec on ERRalpha activity, total RNA was obtained from human SKBr3 breast cancer cells cultured in DMEM deprived of FBS (starved) for 24 hours and treated with PBS, EGF (100uM) or Heregulin (100uM) for an additional 24h. Cells were transfected with siRNA against ERRalpha or with siControl for 60 hours prior to harvesting. For the effect of ERRalpha in lapatinib resistance cells, parental SKBr3 cells (pSKBr3) and Lapatinib-resistant cells (LRSKBr3, maintained in 2uM lapatinib) were transfected with siControl (siC) or siERRalpha for 60 hours prior to harvesting and RNA extraction

2016-06-15 | E-GEOD-81546 | biostudies-arrayexpress

ERRalpha mediates metabolic adaptations that drive lapatinib resistance in breast cancer (gene expression profiles)

2016-06-15 | GSE81546 | GEO

Crystal structure of Homo sapiens kynureninase.

Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.

| S-EPMC2531291 | 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