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Marios Zouridakis

Researcher at Pasteur Institute

Publications -  22
Citations -  780

Marios Zouridakis is an academic researcher from Pasteur Institute. The author has contributed to research in topics: Nicotinic agonist & Acetylcholine receptor. The author has an hindex of 14, co-authored 20 publications receiving 678 citations. Previous affiliations of Marios Zouridakis include University of Patras & University of Utah.

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Muscle and neuronal nicotinic acetylcholine receptors

TL;DR: Nicotinic acetylcholine receptors (nAChRs) as mentioned in this paper are integral membrane proteins and prototypic members of the ligand-gated ion-channel superfamily, which has precursors in the prokaryotic world.
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Crystal structures of free and antagonist-bound states of human α9 nicotinic receptor extracellular domain

TL;DR: The X-ray crystal structures of the α9 ECD revealed a functionally important β7-β10 strand interaction in α9-containing nAChRs, involving their unique Thr147, a hydration pocket similar to that of mouse α1 ECD and a membrane-facing network coordinated by the invariant Arg210.
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Recent advances in understanding the structure of nicotinic acetylcholine receptors

TL;DR: Important progress has been made mainly based on electron microscopy studies of Torpedo nAChR and the high‐resolution X‐ray crystal structures of the homologous molluscan acetylcholine‐binding proteins, the extracellular domain of the mouse nA ChR α1 subunit, and two prokaryotic pentameric LGICs.
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α7 Nicotinic acetylcholine receptor-specific antibody induces inflammation and amyloid β42 accumulation in the mouse brain to impair memory.

TL;DR: Data demonstrate that neuroinflammation is sufficient to provoke the decrease of α7 and α4β2 nAChRs, Aβ42 accumulation and memory impairment in mice and α7(1-208) nA ChR-specific antibodies can cause inflammation within the brain resulting in the symptoms typical for Alzheimer disease.
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Molecular Interaction of α-Conotoxin RgIA with the Rat α9α10 Nicotinic Acetylcholine Receptor

TL;DR: The data support the interaction of α-CTx RgIA at the α10/α9 rather than the α9/α10 nAChR subunit interface, and may facilitate the development of selective ligands with therapeutic potential.