Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds.

By R. Spiro. Glycobiology, 2002

1,321 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. (2005, background): “Of the 12 structures, 8 were of recombinant proteins expressed in Escherichia coli, and they can therefore not carry any mucin-type glycans (Spiro, 2002).”
A systematic approach to protein glycosylation analysis: a path through the maze. (2010, background): “A range of monosaccharides attached to serine and threonine have been found, most commonly N -acetylgalactosamine (GalNAc), N -acetylglucosamine (GlcNAc), xylose, mannose and fucos”
Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry (2003, background): “In addition, changes in the extent of glycosylation and the carbohydrate structure of proteins on the cell surface and in body fluids have been shown to correlate with cancer and other disease states, highlighting the clinical importance of this modification as an indicator or effector of ”