Glycomics and Proteomics

Glycomic Analysis

Glycomic analysis increases the diversity of the proteome to a level unmatched by any other post-translational modification. Glycosidases catalyze the hydrolysis of glycosidic bonds to remove sugars from proteins. These enzymes are critical for glycan processing in the ER and Golgi, and each enzyme shows specificity for removing a particular sugar (e.g., mannosidase). Both membrane proteins and the ECM are highly glycosylated, and O-glycans are essential for proper ECM function and communication between cells and the ECM. Several Glycoepitomics forms of CMD are known to result from dysfunctional O-glycosylation of membrane and ECM proteins; however, one-third of CMDs arise from an unknown genetic etiology.

Relevant Conferences

International Conference on Structural Biology, June 23-24, 2016 New Orleans, USA; World Congress on Amino Acids and Proteins, December 08-09, 2016 Baltimore, USA; 6^th International Conference on Bioinformatics, March 29-30, 2016 Valencia, Spain; International Conference on Nucleic Acids, August 04-06, 2016 Seattle, USA; 7^th International Conference on Proteomics, October 24-26, 2016 Rome, Italy; International Conference on Obesity & Chronic Diseases, July 25-27, 2016 Las Vegas USA; International Conference on New Therapeutics for Diabetes and Obesity, April 17-20, 2016 La Jolla, USA; Conference on Plasma Spectrochemistry, January 10-16, 2016 Tucson, USA; Euro Fed Lipid Congress, September 18-21, 2016 Gent, Belgium; Society for Glycobiology, 2016; International Obesity and Adipose Tissue Biology Conference, February 15-19, 2016 Banff, Canada