(Q38615372)

4 September 2017

title

Structural mechanism of high affinity FcγRI recognition of immunoglobulin G. (English)

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4 September 2017

Jinghua Lu

1

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4 September 2017

Peter D Sun

series ordinal

2

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4 September 2017

publication date

1 November 2015

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4 September 2017

published in

Immunological Reviews

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4 September 2017

volume

268

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4 September 2017

issue

1

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4 September 2017

page(s)

192-200

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Pentraxins at the crossroads between innate immunity, inflammation, matrix deposition, and female fertility

4 September 2017

cites work

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Fcgamma receptor IIa, IIIa, and IIIb polymorphisms in German patients with systemic lupus erythematosus: association with clinical symptoms

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On the interaction of IgG subclasses with the low affinity Fc gamma RIIa (CD32) on human monocytes, neutrophils, and platelets. Analysis of a functional polymorphism to human IgG2

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The structure of a human type III Fcgamma receptor in complex with Fc

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The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex

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Engineered antibody Fc variant with selectively enhanced Fc RIIb binding over both Fc RIIaR131 and Fc RIIaH131

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Structure of FcγRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding.

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Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG

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Recognition of IgG by Fcgamma receptor. The role of Fc glycosylation and the binding of peptide inhibitors

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Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha

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Structure of the murine unglycosylated IgG1 Fc fragment

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Crystal Structure of Fc Receptor I and Its Implication in High Affinity -Immunoglobulin Binding

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IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation

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A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs.

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Terminal sugars of Fc glycans influence antibody effector functions of IgGs

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A protein structural change in aglycosylated IgG3 correlates with loss of huFc gamma R1 and huFc gamma R111 binding and/or activation

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Specific binding of non-glycosylated IgE to Fcε, receptor☆

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Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity

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The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity

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Structural basis for binding of human IgG1 to its high-affinity human receptor FcγRI.

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Structural analysis of Fc/FcγR complexes: a blueprint for antibody design.

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Glycoengineering in cancer therapeutics: a review with fucose-depleted trastuzumab as the model

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Obinutuzumab (GA101) for the treatment of chronic lymphocytic leukemia and other B-cell non-hodgkin's lymphomas: a glycoengineered type II CD20 antibody

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Preclinical pharmacokinetics, pharmacodynamics, and efficacy of RG7116: a novel humanized, glycoengineered anti-HER3 antibody

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Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation

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21 January 2018

Identifiers

DOI

10.1111/IMR.12346

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4 September 2017

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