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Jon Lindstrom

Researcher at University of Pennsylvania

Publications -  442
Citations -  50369

Jon Lindstrom is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Acetylcholine receptor & Nicotinic agonist. The author has an hindex of 108, co-authored 441 publications receiving 48999 citations. Previous affiliations of Jon Lindstrom include University of California, San Diego & University of California, Riverside.

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Distribution of the alpha 2, alpha 3, and alpha 5 nicotinic acetylcholine receptor subunits in the chick brain.

TL;DR: The patterns of distribution of the different nAChR subunits suggest that neurons in many brain structures may contain several subtypes of nA ChRs and that in a few regions one particular subtype may determine the cholinergic nicotinic responses.
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Response of CD4+T Cells from Myasthenic Patients and Healthy Subjects of Biosynthetic and Synthetic Sequences of the Nicotinic Acetylcholine Receptor

TL;DR: The suitability of pools of overlapping synthetic peptides spanning the complete alpha 1 subunit sequence of the human muscle acetylcholine receptor (AChR) or the extracellular domain, and of biosynthetic alpha 1 constructs from E. coli, as stimulants of human CD4+ cells from myasthenia gravis patients and healthy subjects, is investigated.
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Neurogenesis of cholinoceptive neurons in the chick retina

TL;DR: The data suggest that the time of birth of cholinoceptive neurons in the chick retina follows the general pattern of cell generation in the chicks retina, and that alpha 8-positive cells in the ganglion cell layer start to leave the cell cycle almost one day earlier than the alpha 3-positive Cells in the same layer.
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Myasthenogenicity of the main immunogenic region

TL;DR: It is proposed that an initial autoimmune response directed at the MIR leads to an autoimmune response sustained by muscle AChRs, and that AChR‐like proteins distantly related to muscle AchR can induce EAMG and, potentially, MG.
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Discovery of an intrasubunit nicotinic acetylcholine receptor–binding site for the positive allosteric modulator Br-PBTC

TL;DR: The amino acids Glu-282 and Phe-286 near the extracellular domain on the third transmembrane helix were found to be crucial for Br-PBTC's PAM effect and should prove useful as α subunit–selective nAChR PAMs.