Asset Details
Do you wish to reserve the book?
Integrated analysis of global proteome, phosphoproteome and glycoproteome enables complementary interpretation of disease-related protein networks
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Integrated analysis of global proteome, phosphoproteome and glycoproteome enables complementary interpretation of disease-related protein networks
Do you wish to request the book?
Integrated analysis of global proteome, phosphoproteome and glycoproteome enables complementary interpretation of disease-related protein networks
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Integrated analysis of global proteome, phosphoproteome and glycoproteome enables complementary interpretation of disease-related protein networks
2015
Overview
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-glycopeptides (2,634 N-glycosites) in tumor and adjacent normal tissues from three gastric cancer patients. The combined analysis of these data showed that the integrated analysis additively improved the coverages of gastric cancer-related protein networks; phosphoproteome and N-glycoproteome captured predominantly low abundant signal proteins and membranous or secreted proteins, respectively, while global proteome provided abundances for general population of the proteome. Therefore, our results demonstrate that the SEPG can serve as an effective approach for multi-dimensional proteome analyses and the holistic profiles of protein expression and PTMs enabled improved interpretation of disease-related networks by providing complementary information.
Publisher
Springer Science and Business Media LLC,Nature Publishing Group UK,Nature Publishing Group
