English Journal

Gluten exacerbates IgA nephropathy in humanized mice through gliadin-CD89 interaction.

Papista C1, Lechner S1, Ben Mkaddem S1, LeStang MB1, Abbad L1, Bex-Coudrat J1, Pillebout E2, Chemouny JM1, Jablonski M3, Flamant M4, Daugas E5, Vrtovsnik F5, Yiangou M6, Berthelot L1, Monteiro RC7.
Kidney international.Kidney Int.2015 Aug;88(2):276-285. doi: 10.1038/ki.2015.94. Epub 2015 Mar 25.
IgA1 complexes containing deglycosylated IgA1, IgG autoantibodies, and a soluble form of the IgA receptor (sCD89), are hallmarks of IgA nephropathy (IgAN). Food antigens, notably gluten, are associated with increased mucosal response and IgAN onset, but their implication in the pathology remains unk
PMID 25807036

Electrostatic Interactions between OmpG Nanopore and Analyte Protein Surface Can Distinguish between Glycosylated Isoforms.

Fahie MA1, Chen M1.
The journal of physical chemistry. B.J Phys Chem B.2015 Jul 30. [Epub ahead of print]
The flexible loops decorating the entrance of OmpG nanopore move dynamically during ionic current recording. The gating caused by these flexible loops changes when a target protein is bound. The gating is characterized by parameters including frequency, duration, and open-pore current, and these fea
PMID 26181080

Stateva SR1, Villalobo A.
Organic & biomolecular chemistry.Org Biomol Chem.2015 Jul 22;13(30):8196-204. doi: 10.1039/c5ob00443h.
The reversible O-linked attachment of single β-d-N-acetylglucosamine (GlcNAc) moieties to serine/threonine residues in target proteins is a frequently occurring post-translational modification affecting the functionality of many cellular systems. In this report we present experimental evidence sugg
PMID 26108188

Japanese Journal

Label-Free Analysis of O-Glycosylation Site-Occupancy Based on the Signal Intensity of Glycopeptide/Peptide Ions

Simultaneous Enrichment of Deglycosylated Ginsenosides and Monacolin K in Red Ginseng by Fermentation with Monascus pilosus

名古屋学院大学論集　人文・自然科学篇 = THE NAGOYA GAKUIN DAIGAKU RONSHU; Journal of Nagoya Gakuin University; HUMANITIES and NATURAL SCIENCES 47(2), 47-50, 2011-01-31
NAID 120005662346