Proteomics

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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 (ncbitaxon:9606)

SUBMITTER: Sang-Won Lee  

PROVIDER: MSV000080818 | MassIVE | Fri Mar 31 02:28:00 BST 2017

SECONDARY ACCESSION(S): PXD003115

REPOSITORIES: MassIVE

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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]

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