The impact of glycosylation on the biological function and structure of human immunoglobulins.

By J. N. Arnold, M. Wormald, Robert B Sim, P. Rudd, R. Dwek. Annual Review of Immunology, 2007

1,312 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/b1aad03deccb85e32c5a7de36ab5f268dcf531a6

How researchers see this paper

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

In Immunology

1. F. Nimmerjahn
2. R. Jefferis
3. J. Ravetch
4. Gabriel A. Rabinovich
5. Y. Kooyk

In Molecular Biology

1. R. Jefferis
2. F. Nimmerjahn
3. J. Ravetch
4. Gabriel A. Rabinovich
5. Y. Kooyk
6. A. Chan
7. P. Carter

In Radiology, Nuclear Medicine and Imaging

1. F. Nimmerjahn
2. R. Jefferis
3. J. Ravetch
4. Gabriel A. Rabinovich
5. A. Chan
6. P. Carter

Citations in the corpus

• Protein-glycan interactions in the control of innate and adaptive immune responses (2008, background): “In addition, aberrant glycosylation of immunoglobulins has been linked to the pathogenesis of diseases such as rheumatoid arthritis and immunoglobulin A nephropath”
• A systematic approach to protein glycosylation analysis: a path through the maze. (2010, background): “Macro- and microheterogeneity of glycoproteins Glycosylation of proteins is the most common post-translational modification, strongly influencing many of their functional aspects, including cellular localization, turnover and protein quality contro”
• Fcγ receptors as regulators of immune responses (2008, background): “This sugar side chain consists of a conserved biantennary heptasaccharide core structure containing mannose and N-acetylglucosamine (GlcNac) with varying additions of terminal and branching residues such as fucose, GlcNac, galactose and sialic aci”
• Antibody-Based Sensors: Principles, Problems and Potential for Detection of Pathogens and Associated Toxins (2009, background): “A more in-depth discussion of antibody glycosylation is provided in reference [30].”
• Structure and Function of Immunoglobulins (2010, positive): “Adapted from Arnold et al.(28) J ALLERGY CLIN IMMUNOL”
• Glycosylation as a strategy to improve antibody-based therapeutics (2009, background): “It is generally reported that IgG Fc oligosaccharides of normal human IgG are predominantly devoid of terminal sialic acid residue”