Browse
Submit Data
Databases
API
Help

Dataset Information

339 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

LC-MS/MS Data for Identification of ChREBP O-GlcNAcylation

ABSTRACT: LC-MS/MS analysis of O-GlcNAcylated ChREBP proteins, which were overexpressed in HEK293T cells and purified via affinity purification using Ni-NTA agarose

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: An-Qi Yang

LAB HEAD: Xin-Shan Ye

PROVIDER: PXD004286 | Pride | 2017-05-04

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	ChREBP-H.pep.xml	Pepxml
	ChREBP-H.prot.xml	Xml
	ChREBP-H.raw	Raw
	ChREBP-L.pep.xml	Pepxml
	ChREBP-L.prot.xml	Xml

Items per page:

1 - 5 of 9

Publications

Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).

Yang An-Qi AQ Li Daoyuan D Chi Lianli L Ye Xin-Shan XS

Molecular & cellular proteomics : MCP 20170427 7

O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far. Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively. Moreover, for the first time, we identify O< ...[more]

PMID: 28450420

Similar Datasets

Human Breast Milk TMT labeled Rescored with Prosit

Project description:We Have human breast milk dataset in this project. We predict all spectra in the datasets via Prosit then rescore. We have 100% FDR maxquant search results, and using percolator we get 1%FDR filtered results with andromeda Scores and another with features extracted from Prosit predictions.

2022-05-26 | PXD030339 | Pride

ChIP-MS reveals the local chromatin composition by label-free quantitative proteomics

Project description:Chromatin immunoprecipitation (ChIP) has been a cornerstone for epigenetic analyses over the last decades, but even coupled to sequencing approaches (ChIP-seq), it is ultimately limited to one protein at a time. In a complementary effort, we here combined ChIP with label-free quantitative (LFQ) mass spectrometry (ChIP-MS) to interrogate local chromatin compositions. We demonstrate the versality of our approach at telomeres, with transcription factors, in tissue and by dCas9-driven locus-specific enrichment.

2024-03-05 | PXD039701 | Pride

circRIG-I associated proteins in HEK293T

Project description:We use Proximity biotinylation to find circRIG-I associated proteins in HEK293T.

2022-11-16 | PXD037928 | Pride

DDX3X associated proteins with or without circRIG-I

Project description:We use FLAG pulldown assay to find DDX3X associated proteins with or without circRIG-I in HEK293T.

2022-11-16 | PXD037929 | Pride

Urine Proteomics for Noninvasive Monitoring of Biomarkers in Bronchopulmonary Dysplasia

Project description:Current techniques to diagnose and/or monitor critically ill neonates with bronchopulmonary dysplasia (BPD) require invasive sampling of body fluids, which can affect the health status of these frail neonate. We tested our hypotheses 1) it is feasible to use early urine samples from extremely low gestational age newborns at risk for bronchopulmonary dysplasia for proteomics, and 2) urine proteomics can confirm previously identified proteins and biomarkers associated with BPD without invasive sample collection. We developed a robust high throughput urine proteomics methodology that requires only 50 microliters of urine. We validated the methodology on urine collected within 72 hours of birth. Urine samples were collected from extremely low gestational age newborns (ELGANS) (gestational age (26 + 1.2) weeks) admitted to a single Neonatal Intensive Care Unit(NICU); half of whom eventually developed BPD, while the other half served as controls. Our high throughput urine proteomics approach clearly identified several BPD-associated changes in the urine proteome recapitulating expected blood proteome changes. Interestingly, sixteen identified urinary proteins are known targets of drugs approved by the Food and Drug Administration (FDA). Urine proteomics can be used for prediction of BPD risk. In addition to identifying numerous proteins implicated in BPD pathophysiology, previously found in invasively collected blood, tracheal aspirate, and broncho-alveolar lavage, urine proteomics also suggested novel potential therapeutic targets. Ease of access to urine for sequential proteomic evaluations could also allow for longitudinal monitoring of disease progression and impact of therapeutic intervention.

2022-04-04 | PXD028895 | Pride

AMPK activation induces RALDH+ tolerogenic dendritic cells by rewiring glucose and lipid metabolism

Project description:Dendritic cell (DC) activation and function are underpinned by profound changes in cellular metabolism. Several studies indicate that the ability of DCs to promote tolerance is dependent on catabolic metabolism. Yet the contribution of AMP-activated kinase (AMPK), a central energy sensor promoting catabolism, to DC tolerogenicity remains unknown. Here, we show that AMPK activation renders human monocyte-derived DCs tolerogenic as evidenced by an enhanced ability to drive differentiation of regulatory T cells, a process dependent on increased RALDH activity. This is accompanied by a several metabolic changes, including increased breakdown of glycerophospholipids, enhanced mitochondrial fission-dependent fatty acid oxidation, and upregulated glucose catabolism. This metabolic rewiring is functionally important as we found interference with these metabolic processes to reduce to various degrees AMPK-induced RALDH activity as well as the tolerogenic capacity of moDCs. Altogether, our findings reveal a key role for AMPK signaling in shaping DC tolerogenicity, and suggest AMPK as target to direct DC-driven tolerogenic responses in therapeutic settings.

2024-07-16 | PXD053979 | Pride

Quantitative proteomics analysis of Angiostrongylus vasorum-induced alterations in dog serum

Project description:Blood contains hundreds of proteins, reflecting ongoing cellular processes and immune reactions. Angiostrongylus vasorum infection is associated with a perturbed blood protein profile in dogs. However, the literature currently available lacks the necessary depth of analysis in order to resolve the observed pathologies in A. vasorum infections, including bleeding disorders. Using sera from 8 experimentally-infected dogs (i) before infection with A. vasorum, (ii) 34 days post-infection (p.i.; immature infection), and (iii) 75 days p.i. (mature patent infection), serum proteins were measured using liquid chromatography, tandem mass spectrometry (LC-MS/MS). For 2 dogs, serum was analyzed at days 104 and 230 p.i. additionally. A data-independent acquisition workflow was employed in order to generate quantitative data. Following computational analysis, we identified 139 up- and down-regulated proteins following infection (log2 ratio cutoff ≥ 1.0; q-value ≤ 0.05). Differences in serum profiles were most pronounced at day 75 p.i. compared to before infection. Among up-regulated proteins, chitinase 3, several saposin-like proteins, and heat shock proteins were found greatly increased (log2 fold-changes ≥ 5). Levels of pulmonary surfactant protein B were elevated on day 34 p.i. already, in the prepatent phase. Pathway enrichment revealed that complement (especially the lectin pathway) and coagulation cascades as significantly affected upon analysis of down-regulated proteins. Among them were mannan-binding lectin serine peptidases, ficolin, and coagulation factors. These results reflect the ongoing immune response and stress imposed to the lungs by the parasite. In addition, they bring new elements towards understanding the coagulopathies observed in some A. vasorum-infected dogs.

2021-01-12 | PXD016881 | Pride

Identification of DX2 ubiquitination site

Project description:Although ubiquitination of DX2, novel oncogene, is significant on its protein stability, but DX2 ubiquitination sites are not unveiled. In this study, we identified ubiquitination sites of DX2 upon treatment with DX2 protein inhibitor, SDL01, via LC-MSMS technique. Lysine 90 of DX2 was revealed as a ubiquitination site and was validated as a real ubiquitination site via molecular biology

2024-05-30 | PXD051772 | Pride

Human Yeast Dilution TMT labelled Rescored with Prosit.

Project description:We Have a human yeast dilution dataset in this project. We predict all spectra in the datasets via Prosit then rescore. We have 100% FDR max quant search results using percolator. In addition, we get 1%FDR filtered results with andromeda Scores and another with features extracted from Prosit predictions.

2022-06-09 | PXD030340 | Pride

Splicing factors control triple-negative breast cancer cell mitosis through SUN2 interaction and sororin intron retention

Project description:Triple negative breast cancer (TNBC) is an aggressive subtype of breast cancer with limited therapeutic opportunities. Recently, splicing factors have gained attention as potential targets for cancer treatment. We performed an RNAi screen targeting 244 individual splicing factors to systematically evaluate their role in TNBC cell proliferation. We identified nine splicing factors, including SNRPD2, SNRPD3 and NHP2L1, of which depletion inhibited proliferation in two TNBC cell lines by deregulation of sister chromatid cohesion (SCC) via increased sororin intron 1 retention and down-regulation of SMC1, MAU2 and ESPL1. Protein-protein interaction analysis of SNRPD2, SNRPD3 and NHP2L1 identified that seven out of the nine identified splicing factors belong to the same spliceosome complex including novel componentSUN2 that was also critical for efficient sororin splicing. Finally, sororin transcript levels are highly correlated to various proliferation markers in BC patients, suggesting that deregulating sororin levels through targeting of the relevant splicing factors might be a potential strategy to treat TNBC

2021-03-07 | PXD013968 | Pride