Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation

ABSTRACT: LiP-MS experiment was performed HEK293 cells which are expressing eGFP +mRFP-HTTQ74 or eGFP-SPP+mRFP-HTTQ74 to analyze structural changes in proteome level between these two conditions.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Prerana Wagle

LAB HEAD: David Vilchez

PROVIDER: PXD044409 | Pride | 2023-08-11

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	3488_GFP_report.tsv	Tabular
	3488_lipMSsequences.fasta	Fasta
	E2_ColID567_3488_01.raw	Raw
	E2_ColID567_3488_02.raw	Raw
	E2_ColID567_3488_03.raw	Raw

Items per page:

1 - 5 of 25

Similar Datasets

In planta expression of human polyQ-expanded huntingtin fragment reveals mechanisms to prevent disease-related protein aggregation.

Project description:We overexpressed eGFP, eGFP-SPP and pmRFP-Q74 construct in HEK93 cells. We made immunoprecipitation of GFP. We compare the interactome of eGFP and eGFP-SPP.

2023-08-11 | PXD044408 | Pride

Epstein-Barr Virus (EBV)-positive B-cell strain, 28-2: Low v. High latent membrane protein 1 (LMP1)-mRFP expression (miRNA)

Project description:Expression of miRNAs in an EBV-positive B-cell strain, 28-2. 28-2 are infected with a derivative of the B-958 strain of EBV, which expresses eGFP constitutively and LMP1 fused to mRFP from its native promoter. Single cells were sorted by flow cytometry for their levels of LMP1-mRFP (5% expressing the lowest levels of LMP1-mRFP or 5% expressing the highest levels of LMP1-mRFP) Two-condition experiment: Low v. High LMP1-mRFP expression. Biological replicates: 3 Low LMP1-mRFP, 3 High LMP1-mRFP. Samples were normalized to the expression of miRNAs in a pool of unsorted 28-2 cells.

2012-02-01 | E-GEOD-33972 | biostudies-arrayexpress

Epstein-Barr Virus (EBV)-positive B-cell strain, 28-2: Low v. High latent membrane protein 1 (LMP1)-mRFP expression

Project description:Expression of mRNAs in an EBV-positive B-cell strain, 28-2. 28-2 are infected with a derivative of the B-958 strain of EBV, which expresses eGFP constitutively and LMP1 fused to mRFP from its native promoter. Single cells were sorted by flow cytometry for their levels of LMP1-mRFP (5% expressing the lowest levels of LMP1-mRFP or 5% expressing the highest levels of LMP1-mRFP) Two-condition experiment: Low v. High LMP1-mRFP expression. Biological replicates: 3 Low LMP1-mRFP, 3 High LMP1-mRFP. Samples were normalized to the expression of mRNAs in a pool of unsorted 28-2 cells.

2012-02-01 | E-GEOD-33673 | biostudies-arrayexpress

LiP-MS on Purified CAMKK1 treated with Staurosporine

Project description:Limited proteolysis coupled to mass spectrometry (LiP-MS) is a structural proteomics technique that can be used to identify the targets of small molecules. This is achieved by incubating protein with the drug of interest, which induces structural changes such as occupation of the binding site or changes and protein-protein interactions. This is followed by a limited proteolysis step in which the unspecific protease proteinase K is added to the treated protein sample. The protease preferentially cleaves accessible and flexible regions of the protein, thus generating peptides that reflect the changes in surface accessibility caused by the treatment with the small molecule. Here we treated affinity-purified CAMKK1 kinase inhibitor Staurosporine. The data were generated as part of the IMI EUbOPEN project.

2023-04-26 | PXD041089 | Pride

Epstein-Barr Virus (EBV)-positive B-cell strain, 28-2: Low v. High latent membrane protein 1 (LMP1)-mRFP expression (miRNA)

2012-02-01 | GSE33972 | GEO

Epstein-Barr Virus (EBV)-positive B-cell strain, 28-2: Low v. High latent membrane protein 1 (LMP1)-mRFP expression

2012-02-01 | GSE33673 | GEO

LiP-MS on DCLK1 Purified from HEK293 cells treated with DCLK1-IN-1

Project description:Limited proteolysis coupled to mass spectrometry (LiP-MS) is a structural proteomics technique that can be used to identify the targets of small molecules. This is achieved by incubating lysate with the drug of interest, which induces structural changes such as occupation of the binding site or changes and protein-protein interactions. This is followed by a limited proteolysis step in which the unspecific protease proteinase K is added to the treated lysate. The protease preferentially cleaves accessible and flexible regions of the proteins, thus generating peptides that reflect the changes in surface accessibility caused by the treatment with the small molecule. Here we treated DCLK1 Purified from HEK293 cells with the probe DCLK1-IN-1 and staurosporine to profile structural effects. This project is part of the IMI EUbOPEN project.

2025-04-30 | PXD055350 | Pride

LiP-MS on CAMKK2 Purified from HEK293 cells treated with SGC-CAMKK2-1

Project description:Limited proteolysis coupled to mass spectrometry (LiP-MS) is a structural proteomics technique that can be used to identify the targets of small molecules. This is achieved by incubating lysate with the drug of interest, which induces structural changes such as occupation of the binding site or changes and protein-protein interactions. This is followed by a limited proteolysis step in which the unspecific protease proteinase K is added to the treated lysate. The protease preferentially cleaves accessible and flexible regions of the proteins, thus generating peptides that reflect the changes in surface accessibility caused by the treatment with the small molecule. Here we treated CAMKK2 Purified from HEK293 cells with the probe SGC-CAMKK2-1, negative control SGC-CAMKK2-1N and staurosporine to profile structural effects. This project is part of the IMI EUbOPEN project.

2025-04-30 | PXD058369 | Pride

LiP-MS on CASK Purified from HEK293 cells treated with NR162

Project description:Limited proteolysis coupled to mass spectrometry (LiP-MS) is a structural proteomics technique that can be used to identify the targets of small molecules. This is achieved by incubating lysate with the drug of interest, which induces structural changes such as occupation of the binding site or changes and protein-protein interactions. This is followed by a limited proteolysis step in which the unspecific protease proteinase K is added to the treated lysate. The protease preferentially cleaves accessible and flexible regions of the proteins, thus generating peptides that reflect the changes in surface accessibility caused by the treatment with the small molecule. Here we treated CASK Purified from HEK293 cells with the probe NR162, negative control NR187 and staurosporine to profile structural effects. This project is part of the IMI EUbOPEN project.

2025-04-30 | PXD058317 | Pride

LiP-MS on CHEK1 Purified from HEK293 cells treated with Rabusertib

Project description:Limited proteolysis coupled to mass spectrometry (LiP-MS) is a structural proteomics technique that can be used to identify the targets of small molecules. This is achieved by incubating lysate with the drug of interest, which induces structural changes such as occupation of the binding site or changes and protein-protein interactions. This is followed by a limited proteolysis step in which the unspecific protease proteinase K is added to the treated lysate. The protease preferentially cleaves accessible and flexible regions of the proteins, thus generating peptides that reflect the changes in surface accessibility caused by the treatment with the small molecule. Here we treated CHEK1 Purified from HEK293 cells with the probe Rabusertib and staurosporine to profile structural effects. This project is part of the IMI EUbOPEN project.

2025-04-30 | PXD058318 | Pride