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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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N-Methyl-D-aspartate receptor mediated toxicity in nonneuronal cell lines: characterization using fluorescent measures of cell viability and reactive oxygen species production.

TL;DR: Using co-transfection with green fluorescent protein and cell counting of viable cells with a fluorescence activated cells sorter, the subunit-specific profile of NMDA receptor-mediated cell death in cells transfected with NMDA receptors was confirmed.
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Optical studies of nicotinic acetylcholine receptor subtypes in the guinea-pig enteric nervous system.

TL;DR: The range of activity patterns that follows sequential pharmacological elimination of individual subtypes suggests that nAChRs may be capable of regulating the activity of both excitatory and inhibitory pathways, in a manner similar to that described in the central nervous system.
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Expression of lynx1 in developing lung and its modulation by prenatal nicotine exposure

TL;DR: Lynx1 expression was first observed in 71-day fetal lungs and increased with age, and immunohistochemistry, Western analysis, and realtime PCR analysis showed increased lynX1 expression in lungs following prenatal nicotine exposure, suggesting lynx1 is co-expressed with nAChR in the lung.
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α-Conotoxin PeIA[S9H,V10A,E14N] Potently and Selectively Blocks α6β2β3 versus α6β4 Nicotinic Acetylcholine Receptors

TL;DR: Novel analogs of a recently described α-conotoxin, PeIA, are synthesized and it is demonstrated that ligands can be developed to discriminate between α6β2 and α6 β4 nAChRs.
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Isoform-specific mechanisms of α3β4*-nicotinic acetylcholine receptor modulation by the prototoxin lynx1

TL;DR: The exquisite isoform selectivity of lynx1 interactions provides new insights into the mechanisms and allosteric sites [α(−)‐interface containing] by which prototoxins can modulate nAChR function.