M
Michael Remoundos
Researcher at Pasteur Institute
Publications - 5
Citations - 277
Michael Remoundos is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Acetylcholine receptor & Binding site. The author has an hindex of 5, co-authored 5 publications receiving 274 citations.
Papers
More filters
Journal ArticleDOI
The Ser-Arg-Tyr-Asp region of the major surface glycoprotein of Leishmania mimics the Arg-Gly-Asp-Ser cell attachment region of fibronectin.
Ketty Soteriadou,Michael Remoundos,M C Katsikas,Athina K. Tzinia,Vassilios Tsikaris,C. Sakarellos,Socrates J. Tzartos +6 more
TL;DR: The conserved among species sequence SRYD of gp63, with significant hydrophilicity, flexibility, and beta-turn propensity features, mimics antigenically and functionally the RGDS sequence of fibronectin.
Journal ArticleDOI
Fine localization of the major alpha-bungarotoxin binding site to residues alpha 189-195 of the Torpedo acetylcholine receptor. Residues 189, 190, and 195 are indispensable for binding.
TL;DR: The Pepscan systematic peptide synthesis system was used to determine the minimum Torpedo AChR segment required for alpha-bungarotoxin binding and to investigate the role of each residue within this segment, finding that the heptapeptide alpha 189-195 was the minimum sequence with high binding activity.
Journal ArticleDOI
Expression of Soluble Ligand- and Antibody-binding Extracellular Domain of Human Muscle Acetylcholine Receptor α Subunit in Yeast Pichia pastoris: ROLE OF GLYCOSYLATION IN α-BUNGAROTOXIN BINDING
Loukia Psaridi-Linardaki,Avgi Mamalaki,Michael Remoundos,Socrates J. Tzartos,Socrates J. Tzartos +4 more
TL;DR: Results suggest that the extracellular domain of the human AChR α subunit expressed in P. pastoris has an apparently near native conformation, which makes it suitable for structural studies on the nicotinic acetylcholine receptor and for use as an autoantigen in myasthenia gravis studies.
Journal ArticleDOI
Reconstitution of conformationally dependent epitopes on the N-terminal extracellular domain of the human muscle acetylcholine receptor α subunit expressed in Escherichia coli: implications for myasthenia gravis therapeutic approaches
TL;DR: Results show that the conformationally dependent MIR epitopes do not require the participation of the oligosaccharide moiety of the alpha subunit nor the contribution of neighboring subunits for antibody binding, and should prove valuable in the understanding and development of therapeutic approaches for MG.
Journal ArticleDOI
Precise epitope mapping of monoclonal antibodies to the cytoplasmic side of the acetylcholine receptor α subunit
TL;DR: The epitopes for twelve monoclonal antibodies against the cytoplasmic side of the acetylcholine receptor (AChR) α subunit were precisely mapped using over 300 continuously overlapping synthetic peptides attached on poly(ethylene) rods and should prove instructive in searches for VICE-α-like epitopes carrying autoantigens with potential involvement in myasthenia gravis.