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PGRC Cancer Proteome Study of Gastric Tissue

ABSTRACT: The goal of the project is to analyze different layers of proteome information including protein abundance and post-translational modifications of PGRC gastric tissue samples. Three pairs of human gastric cancer and adjacent normal tissues were extensively characterized by serial enrichments of phosphorylation and N-glycosylation (SEPG) coupled to LC-MS/MS method.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Stomach

DISEASE(S): Stomach Cancer

SUBMITTER: Dong-Gi Mun

LAB HEAD: Sang-Won Lee

PROVIDER: PXD003115 | Pride | 2016-03-18

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	FN01_N179T180_180min_10ug_C1_032714.raw	Raw
	FN01_N179T180_180min_10ug_C1_032714_PEMMR.mgf	Mgf
	FN01_N179T180_180min_10ug_C1_032714_PEMMR.pepXML	Pepxml
	FN01_N181T182_180min_10ug_C2_033114.raw	Raw
	FN01_N181T182_180min_10ug_C2_033114_PEMMR.mgf	Mgf

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Publications

Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease-related protein networks.

Park Jong-Moon JM Park Ji-Hwan JH Mun Dong-Gi DG Bae Jingi J Jung Jae Hun JH Back Seunghoon S Lee Hangyeore H Kim Hokeun H Jung Hee-Jung HJ Kim Hark Kyun HK Lee Hookeun H Kim Kwang Pyo KP Hwang Daehee D Lee Sang-Won SW

Scientific reports 20151211

Multi-dimensional proteomic analyses provide different layers of protein information, including protein abundance and post-translational modifications. Here, we report an integrated analysis of protein expression, phosphorylation, and N-glycosylation by serial enrichments of phosphorylation and N-glycosylation (SEPG) from the same tissue samples. On average, the SEPG identified 142,106 unmodified peptides of 8,625 protein groups, 18,846 phosphopeptides (15,647 phosphosites), and 4,019 N-glycopep ...[more]

PMID: 26657352

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