Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteins that directly interact with the full-length LINC01198, with EGFP as a control, in vemurafenib-resistant melanoma cells.

ABSTRACT: Using EGFP RNA as a control, the full-length LINC01198 pull-down was performed to identify proteins that directly interact with LINC01198 in vemurafenib-resistant melanoma cells.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Melanocyte, Skin

SUBMITTER: Jieyu Liu

LAB HEAD: Jieyu Liu

PROVIDER: PXD056757 | Pride | 2025-11-10

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	EGFP_VS_LINC01198.xlsx	Xlsx
	L_81.msf	Msf
	L_81.raw	Raw
	L_82.msf	Msf
	L_82.raw	Raw

Items per page:

1 - 5 of 8

Publications

LINC01198 activates Hippo signaling to stimulate IL-1β autocrine for driving vemurafenib resistance by associating with TAOK1/2 in melanoma.

Liu Jieyu J Liang Xiaoting X Wang Ke K Zhang Chunting C Li Can C Zhao Lei L Kuang Yanjie Y Wang Min M Liu Jun J Zhou Liang L Ma Li L

Cell death discovery 20251027 1

Vemurafenib (VEM) is an important targeted drug for treating melanoma harboring BRAF-V600E mutation. Despite its remarkable curative efficacy in early clinical treatment, most patients developed drug resistance within one year. Nevertheless, the critical factors driving vemurafenib resistance and mechanisms leading to treatment failure in melanoma are debating and inconclusive. In this study, we established vemurafenib-resistance melanoma cell strain together with acute vemurafenib treatment and ...[more]

PMID: 41145465

Similar Datasets

LncRNA LINC00622 directly bingding proteins in melanoma cells

Project description:We conducted an RNA pulldown assay in melanoma cell line SK-MEL-28 using in vitro-transcribed full-length LINC00622 RNA accompanied with a control EGFP RNA. The specific binding proteins of LINC00622 was identified using high-performance liquid chromatography-mass spectrometry (HPLC-MS).

2025-07-21 | PXD055040 | Pride

Transcriptome analysis of Mapt-EGFP+ and Mapt-EGFP- myenteric cells

Project description:Transcriptome analysis of Mapt-EGFP+ and Mapt-EGFP- myenteric cells

| PRJNA822404 | ENA

Interaction protein of Ptc1::eGFP and Ptc2::eGFP in Aspergillus flavus

Project description:There are the Mass spectrum original data of Ptc1 and Ptc2. The immunoprecipitated proteins from Ptc1::eGFP and Ptc2::eGFP stains in Aspergillus flavus were detected with SDS-PAGE. Next, in-gel tryptic digestion, and the peptides were obtained and detected by liquid chromatog-raphy coupled with tandem mass spectrometry (LC-MS/MS) on a Q-Exactive (QE) mass spectrometer (Thermo Fisher Scientific)

2023-07-06 | PXD038079 |

Immunoprecipitated proteins associated with foci-forming Eno2p-EGFP-FLAG or non-forming Eno2V22Ap-EGFP-FLAG in yeast Saccharomyces cerevisiae under hypoxia

Project description:Yeast enolase (Eno2p) conjugated with EGFP and Flag-tag (Eno2p-EGFP-FLAG) and Eno2p with V22A substitution (Eno2V22Ap) conjugated with EGFP and Flag-tag (Eno2V22Ap-EGFP-FLAG) were produced in baker's yeast S. cerevisiae. After semi-anaerobic culture at 30 ˚C for 12h, cells producing Eno2p-EGFP-FLAG formed fluorescent foci, while cells producing Eno2V22Ap-EGFP-FLAG did not. The cells were collected and lysed, and proteins Eno2p-EGFP-FLAG or Eno2V22Ap-EGFP-FLAG and the associated proteins were coimmunoprecipitated using ANTI-FLAG M2 affinity gel and analyzed. Data contain two biological replicates and two technical replicates (n = 4). As the results, 96 proteins were detected with both recombinant Eno2p-EGFP-FLAG and Eno2V22Ap-EGFP-FLAG protein, 29 proteins were detected only with recombinant Eno2p-EGFP-FLAG protein, and 16 proteins were detected only with recombinant Eno2V22Ap-EGFP-FLAG protein. Data Processing/Data Analysis: The separated analytes were detected on an LTQ Velos linear ion trap mass spectrometer (Thermo Scientific). For data-dependent acquisition, the method was set to automatically analyze the five most intense ions observed in the MS scan. The mass spectrometry data were used for protein identification by the Mascot search engine on Protein Discoverer software (ver. 1.2, Thermo Scientific) against the information in the Saccharomyces Genome Database (SGD; http://www.yeastgenome.org). Search parameters for peptide identification included a precursor mass tolerance of 1.2 Da, a fragment mass tolerance of 0.8 Da, a minimum of one tryptic terminus, and a maximum of one internal trypsin cleavage site. Cysteine carbamidomethylation (+57.021 Da) and methionine oxidation (+15.995 Da) were set as a differential amino acid modification. The data were then filtered at a q value ≤ 0.01 corresponding to 1% FDR at the spectral level.

2014-02-25 | PXD000173 | Pride

ATAC seq from EGFP+ and EGFP- cells from postnatal day 3 striatum from GENSAT Nr4a1-EGFP mice

Project description:ATAC seq from EGFP+ and EGFP- cells from postnatal day 3 striatum from GENSAT Nr4a1-EGFP mice

| PRJNA601456 | ENA

BM-eGFP+ MSC expression arrays

Project description:original population (oMSC) and highly migrative subpopulation (sMSC) of murine eGFP+ bone marrow MSC

| EGAD00010001265 | EGA

ZHBTc4 ES cells stably expressing EGFP vs Nr5a2-EGFP or Oct4-EGFP vs Nr5a2-EGFP

Project description:Gene expression profiles of ZHBTc4 ES cells expressing EGFP, Oct4-EGFP, Nr5a2-EGFP under CAG promoter. Monoclonal cell lines selected by Puromycin were used for analysis. Each of the cell lines was cultured in doxycycline containing media for endogenous Oct4 knock-down. Pupose of this experiment is to investigate the possibility that forced expression of Nr5a2 can replace Oct4 function in the self-renewal of ES cells. Monoclonal ZHBTc4 ES cells expressing EGFP vs Nr5a2-EGFP, Oct4-EGFP vs Nr5a2-EGFP, no replication

2013-11-05 | E-GEOD-52034 | biostudies-arrayexpress

N-terminal modification of eGFP by LC-MSMS

Project description:We used an in-depth analysis of the characteristics of eGFP as a proof-of-principle analyte to establish a robust assay for the determination of degradation rates on the single-cell level using microinjection and live-cell microscopy. We aimed to determine the influence of the exposed n-terminal aminoacid on the proteins degradation. The high sensitivity of our single-cell analysis in combination with the controlled starting conditions of microinjection provides an unique advantage to examine differences in rates with an improved resolution and to compare the influence of different n-terminal aminoacids on eGFP-degradation without accounting for differences during translation. We produced XS-eGFP, with X being substituted by different proteinogenic amino acids, from E.coli and extensively purified it by a three column process. We could show pronounced differences in degradation rates for the constructs with differing N-terminal aminoacids. We also chemically acetylated the N-terminal α amino groups of methionine, alanine, threonine, valine and serine that would normally occur co translationally, in vitro before, microinjection to analyze the influence of acetylation on target degradation. Acetylation at the N-terminus was confirmed by LC-MS-MS. Acetylation reduced degradation of the respective construct. Finally we purified eGFP by anion-exchange from eGFP expressing HEK293 cells to elucidate modifications of eGFP after eukaryotic expression. We could show that eGFP is likely cleaved during HEK293 expression and n-terminally acetylated, which leads to a starkly reduced degradation rate. The degradation rate was similarly reduced for a N-terminally shortened eGFP produced in E.coli and acetylated in-vitro.

2025-05-06 | PXD042569 | Pride

RNAseq analysis of CD4+EGFP+ and CD8+EGFP+ regulatory T cells

Project description:RNAseq analysis of CD4+EGFP+ and CD8+EGFP+ regulatory T cells

| PRJNA784567 | ENA

Transcriptome analysis of HT1080 cells expressing HA-hZFAT-EGFP and EGFP

Project description:Transcriptome analysis of HT1080 cells expressing HA-hZFAT-EGFP and EGFP

| PRJNA607801 | ENA