Výsledky vyhledávání - "Bungarotoxins/metabolism"

Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane

Autor: Lambert P. van den Heuvel, Karel J.M. Assmann, H. Dijkman, Thea J. van de Velden, Jacques H. Veerkamp, C.A.F. Buskens, Leo A. H. Monnens, Markus A. Rüegg, Alexander J. Groffen, Jacob van den Born

Publikováno v: Journal of Histochemistry & Cytochemistry, 46(1), 19-27
The Journal of Histochemistry and Cytochemistry, 46(1), 19-27. Histochemical Society Inc.
Groffen, A J, Ruegg, M A, Dijkman, H, Van De Velden, T J, Buskens, C A, Van Den Born, J, Assmann, K J, Monnens, L A, Veerkamp, J H & Van Den Heuvel, L P 1998, ' Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane ', Journal of Histochemistry and Cytochemistry, vol. 46, no. 1, pp. 19-27 . https://doi.org/10.1177/002215549804600104
Journal of Histochemistry and Cytochemistry, 46, pp. 19-27
Journal of the American Society of Nephrology, 8, A2396-A2396. Williams & wilkins
Groffen, A J, Ruegg, M A, Dijkman, H, Van De Velden, T J, Buskens, C A, Van Den Born, J, Assmann, K J, Monnens, L A, Veerkamp, J H & Van Den Heuvel, L P 1998, ' Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane ', The Journal of Histochemistry and Cytochemistry, vol. 46, no. 1, pp. 19-27 . https://doi.org/10.1177/002215549804600104
Journal of Histochemistry and Cytochemistry, 46, 19-27
Journal of Histochemistry and Cytochemistry, 46(1), 19-27. Histochemical Society Inc.
Journal of the American Society of Nephrology, 8, pp. A2396-A2396

Agrin is a heparan sulfate proteoglycan (HSPG) that is highly concentrated in the synaptic basal lamina at the neuromuscular junction (NMJ). Agrin-like immunoreactivity is also detected outside the NMJ. Here we show that agrin is a major HSPG compone

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0df1560e294b76afdd44f950898b0cc8
https://research.rug.nl/en/publications/53e993fe-67b6-4829-bcd6-17100348ffbf

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Interaction of alpha-conotoxin ImII and its analogs with nicotinic receptors and acetylcholine-binding proteins: additional binding sites on Torpedo receptor

Autor: Rustam H. Ziganshin, Daniel Bertrand, Titia K. Sixma, Victor I. Tsetlin, Alexander Fish, Prakash Rucktooa, Alexey V. Osipov, Igor E. Kasheverov, Alexey Yu. Khruschov, Maxim N. Zhmak, August B. Smit, Dieter D’hoedt

Publikováno v: Journal of Neurochemistry, Vol. 111, No 4 (2009) pp. 934-44
Kasheverov, I E, Zhmak, M N, Fish, A, Rucktooa, P, Khruschov, A Y, Osipov, A V, Ziganshin, R H, D'Hoedt, D, Bertrand, D, Sixma, T K, Smit, A B & Tsetlin, V I 2009, ' Interaction of alpha-conotoxin ImII and its analogs with nicotinic receptors and acetylcholine-binding proteins: additional binding sites on Torpedo receptor ', Journal of Neurochemistry, vol. 111, pp. 934-944 . https://doi.org/10.1111/j.1471-4159.2009.06359.x
Journal of Neurochemistry, 111, 934-944. Wiley-Blackwell

alpha-Conotoxins interact with nicotinic acetylcholine receptors (nAChRs) and acetylcholine-binding proteins (AChBPs) at the sites for agonists/competitive antagonists. alpha-Conotoxins blocking muscle-type or alpha7 nAChRs compete with alpha-bungaro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4088b7e0e780a119be9debdb83db1a9
https://archive-ouverte.unige.ch/unige:5107

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[3H]A-585539 [(1S,4S)-2,2-dimethyl-5-(6-phenylpyridazin-3-yl)-5-aza-2-azoniabicyclo[2.2.1]heptane], a novel high-affinity alpha7 neuronal nicotinic receptor agonist: radioligand binding characterization to rat and human brain

Autor: Daniel Bertrand, Anouk Marguerat, David J. Anderson, Eliane Tribollet, Bruce Surber, Murali Gopalakrishnan, Carol S. Surowy, Jia Du, William H. Bunnelle

Publikováno v: Journal of Pharmacology and Experimental Therapeutics, Vol. 324, No 1 (2008) pp. 179-187

Receptor binding was characterized for [(3)H](1S,4S)-2,2-dimethyl-5-(6-phenylpyridazin-3-yl)-5-aza-2-azoniabicycl o[2.2.1]heptane ([(3)H]A-585539), a selective high-affinity alpha7 nicotinic acetylcholine receptor (nAChR) agonist with rapid kinetics,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5b14dfc8eac515f07f229a3f2f2d8f2
https://pubmed.ncbi.nlm.nih.gov/17959745

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Mapping the Main Immunogenic Region and Toxin-Binding Site of the Nicotinic Acetylcholine Receptor

Autor: Christine Alliod, Marc Ballivet, Alex Mauron, SJ Tzartos, T. Barkas, B. Roth

Publikováno v: Science, Vol. 235, No 4784 (1987) pp. 77-80

The alpha-chain of the nicotinic acetylcholine receptor carries the binding sites both for cholinergic ligands and for most experimentally induced or naturally occurring antibodies to the native receptor. By means of expression cloning in Escherichia

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bc31e33071e671c70d75cbfe21b6d70
https://doi.org/10.1126/science.2432658

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Conservation of neural nicotinic acetylcholine receptors from Drosophila to vertebrate central nervous systems

Autor: Pierre Spierer, Marc Ballivet, Blaise Bossy

Publikováno v: EMBO Journal, Vol. 7, No 3 (1988) pp. 611-8

Nicotinic acetylcholine receptors (nAChR) are found both in vertebrate and insect central nervous systems. We have isolated a Drosophila gene by crosshybridization with a vertebrate probe. Structural conservation of domains of the deduced protein and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db02f95b68fb35dc7ef7f6a3497bacf1
https://europepmc.org/articles/PMC454364/

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