J
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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Journal ArticleDOI
A comparative non-radioactive in situ hybridization and immunohistochemical study of the distribution of α7 and α8 subunits of the nicotinic acetylcholine receptors in visual areas of the chick brain
Tânia H.O Lohmann,Andréa da Silva Torrão,Luiz R.G. Britto,Jon Lindstrom,Dânia E. Hamassaki-Britto +4 more
TL;DR: The results indicated that the alpha7 and alpha8 nAChR transcripts are widely distributed in the brain, exhibiting differential expression in some structures but also some degree of co-localization.
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Leukoplasmapheresis for Myasthenia Gravis: Acetylcholine Receptor Antibody Production
TL;DR: Acetylcholine receptor antibody and IgG were studied in vivo and in vitro in a patient with myasthenia gravis, who was undergoing multiple leukoplasmaphereses, indicating that AChR-ab production in this patient was not the result of detectable loss of suppressor-cell activity.
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Differential co-localization of nicotinic acetylcholine receptor subunits with calcium-binding proteins in retinal ganglion cells
Cláudia Marie Araki,R. S. Pires,Luiz R.G. Britto,Jon Lindstrom,Harvey J. Karten,Dania Emi Hamassaki-Britto +5 more
TL;DR: In this paper, the co-occurrence of nicotinic acetylcholine receptor subunits with calcium-binding proteins in ganglion cells of the chick retina was examined.
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Determinants of channel gating located in the N-terminal extracellular domain of nicotinic α7 receptor
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Extracellular Domain Nicotinic Acetylcholine Receptors Formed by α4 and β2 Subunits
TL;DR: It is suggested that M1 domains on both α4 and β2 play an important role for efficient expression of extracellular domain α4 β2 nAChRs that are high fidelity structural models of full-length α4β2 n aChRs.