Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure (Q44899476)

7 December 2017

title

Monoglucosylated glycans in the secreted human complement component C3: implications for protein biosynthesis and structure (English)

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7

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5

Ian A Wilson

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Gayle E Ritchie

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Alison J Critchley

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B Paul Morgan

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Raymond A Dwek

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Pauline M Rudd

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language of work or name

English

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publication date

1 May 2004

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volume

566

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issue

1-3

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page(s)

270-274

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Protein glucosylation and its role in protein folding

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cites work

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Processing of N-linked carbohydrate chains in a patient with glucosidase I deficiency (CDG type IIb)

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Structure and biology of complement protein C3, a connecting link between innate and acquired immunity

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Immunoaffinity purification of human complement component C9 using monoclonal antibodies

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Sequencing of N-Linked Oligosaccharides Directly from Protein Gels: In-Gel Deglycosylation Followed by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry and Normal-Phase High-Performance Liquid Chromatography

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Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis

21 January 2018

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Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid

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Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57.

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Structural determination of the N-glycans of a lepidopteran arylphorin reveals the presence of a monoglucosylated oligosaccharide in the storage protein

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Partially glucose-capped oligosaccharides are found on the hemoglobins of the deep-sea tube worm Riftia pachyptila

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N-glycan structures of pigeon IgG: a major serum glycoprotein containing Galalpha1-4 Gal termini..

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Site-specific N-glycosylation of chicken serum IgG.

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Contrasting IgG Structures Reveal Extreme Asymmetry and Flexibility

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Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity

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The crystal structure of IgE Fc reveals an asymmetrically bent conformation

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The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions

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Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc

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The role of constant region carbohydrate in the assembly and secretion of human IgD and IgA1

21 January 2018

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Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

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A unique, terminally glucosylated oligosaccharide is a common feature on Leishmania cell surfaces

21 January 2018

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Identifiers

DOI

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7 December 2017

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