MALDI / Pasadena / Bradford / Frederick / London / St. Louis / /
Company
Kodak / IgG / Novagen Inc. / Pedersen L. C. / Protein Chemistry Laboratory / Acta Pharm / Hsieh-Wilson L. C. / Glycan / B Galtransferase / Mei / Bio-Rad / Dojindo Laboratories / Amersham Biosciences / B Gal / Masibay A. S. / /
Country
United States / United Kingdom / / /
Facility
Howard Hughes Medical Institute / National Cancer Institute / R-LA complex / California Institute of Technology / / /
IndustryTerm
pharmaceutical agents / centrifugal filter device / filter device / blood / pharmaceutical settings / cleavage site / glycosylation site / chemical handle / antigen binding site / model systems / metal binding sites / software residing / /
Organization
National Cancer Institute / California Institute of Technology / National Institute of Health / U.S. Government / Chemical Engineering and Howard Hughes Medical Institute / Center for Cancer Research / Department of Health and Human Services / Division of Chemistry and Chemical Engineering / /
Person
Wing / Yang Feng / Maria Manzoni / Linda C. Hsieh-Wilson / Elizabeth Boeggeman / Harvey / Nelly Khidekel / Dimiter S. Dimitrov / Sharon / Yun Zhang / John T. Simpson / / /
Position
D. J. / Corresponding author / Governor / /
Product
GalNAc / /
ProvinceOrState
Maryland / California / /
PublishedMedium
Cancer Research / /
Technology
Alpha / electrophoresis / X-ray / antibodies / UDP / MRI / laser / rational drug design / drug delivery system / glycomics / /
Bioconjugate Chem. 2007, 18, 806−[removed]Direct Identification of Nonreducing GlcNAc Residues on N-Glycans of Glycoproteins Using a Novel Chemoenzymatic Method