Electrostatic determinants of the ion channel control of the nicotinic acetylcholine receptor of Torpedo californica

Andreas Kukol; E. Neumann

doi:10.1007/s002490050173

Electrostatic determinants of the ion channel control of the nicotinic acetylcholine receptor of Torpedo californica

European Biophysics Journal ◽

10.1007/s002490050173 ◽

1998 ◽

Vol 27 (6) ◽

pp. 618-625 ◽

Cited By ~ 6

Author(s):

Andreas Kukol ◽

E. Neumann

Keyword(s):

Ion Channel ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine ◽

Torpedo Californica ◽

Channel Control

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Biophysical and Ion Channel Functional Characterization of the Torpedo californica Nicotinic Acetylcholine Receptor in Varying Detergent–Lipid Environments

The Journal of Membrane Biology ◽

10.1007/s00232-008-9107-7 ◽

2008 ◽

Vol 223 (1) ◽

pp. 13-26 ◽

Cited By ~ 14

Author(s):

Guillermo A. Asmar-Rovira ◽

Aloysha M. Asseo-García ◽

Orestes Quesada ◽

Michael A. Hanson ◽

Anchi Cheng ◽

...

Keyword(s):

Ion Channel ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Functional Characterization ◽

Nicotinic Acetylcholine ◽

Torpedo Californica

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Effects of lipids and detergents on the conformation of the nicotinic acetylcholine receptor from Torpedo californica.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)42565-3 ◽

1992 ◽

Vol 267 (11) ◽

pp. 7655-7663

Author(s):

M.P. McCarthy ◽

M.A. Moore

Keyword(s):

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine ◽

Torpedo Californica

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Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 2. Membrane fluidity and ligand-mediated alteration in the accessibility of .gamma. subunit cysteine residues to cholesterol

Biochemistry ◽

10.1021/bi00097a021 ◽

1993 ◽

Vol 32 (46) ◽

pp. 12420-12427 ◽

Cited By ~ 39

Author(s):

Vasanthy Narayanaswami ◽

Mark G. McNamee

Keyword(s):

Membrane Fluidity ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Cysteine Residues ◽

Receptor Function ◽

Nicotinic Acetylcholine ◽

Torpedo Californica ◽

Gamma Subunit ◽

Lipid Interactions

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Protein-lipid interactions and Torpedo californica nicotinic acetylcholine receptor function. 1. Spatial disposition of cysteine residues in the .gamma. subunit analyzed by fluorescence-quenching and energy-transfer measurements

Biochemistry ◽

10.1021/bi00097a020 ◽

1993 ◽

Vol 32 (46) ◽

pp. 12413-12419 ◽

Cited By ~ 20

Author(s):

Vasanthy Narayanaswami ◽

Jeongah Kim ◽

Mark G. McNamee

Keyword(s):

Energy Transfer ◽

Fluorescence Quenching ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Cysteine Residues ◽

Receptor Function ◽

Nicotinic Acetylcholine ◽

Torpedo Californica ◽

Gamma Subunit ◽

Lipid Interactions

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Mapping the lipid-exposed regions in the Torpedo californica nicotinic acetylcholine receptor

Biochemistry ◽

10.1021/bi00130a003 ◽

1992 ◽

Vol 31 (15) ◽

pp. 3738-3750 ◽

Cited By ~ 104

Author(s):

Michael P. Blanton ◽

Jonathan B. Cohen

Keyword(s):

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine ◽

Torpedo Californica

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Interaction of MK-801 with the nicotinic acetylcholine receptor-associated ion channel from electroplax

European Journal of Pharmacology ◽

10.1016/0014-2999(89)90487-1 ◽

1989 ◽

Vol 164 (2) ◽

pp. 397-398 ◽

Cited By ~ 15

Author(s):

M.P. Kavanaugh ◽

B.A.C. Tester ◽

E. Weber

Keyword(s):

Ion Channel ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine ◽

Mk 801

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The ion channel of the nicotinic acetylcholine receptor is formed by the homologous helices M II of the receptor subunits

FEBS Letters ◽

10.1016/0014-5793(86)80881-x ◽

1986 ◽

Vol 205 (1) ◽

pp. 137-142 ◽

Cited By ~ 221

Author(s):

Ferdinand Hucho ◽

Walter Oberthür ◽

Friedrich Lottspeich

Keyword(s):

Ion Channel ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine

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Identification of Amino Acids in the Nicotinic Acetylcholine Receptor Agonist Binding Site and Ion Channel Photolabeled by 4-[(3-Trifluoromethyl)-3H-Diazirin-3-yl]Benzoylcholine, a Novel Photoaffinity Antagonist†

Biochemistry ◽

10.1021/bi0269815 ◽

2003 ◽

Vol 42 (2) ◽

pp. 271-283 ◽

Cited By ~ 14

Author(s):

David C. Chiara ◽

Jonathan C. Trinidad ◽

Dong Wang ◽

Michael R. Ziebell ◽

Deirdre Sullivan ◽

...

Keyword(s):

Amino Acids ◽

Ion Channel ◽

Binding Site ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Receptor Agonist ◽

Agonist Binding ◽

Nicotinic Acetylcholine

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The ion channel of the nicotinic acetylcholine receptor

Trends in Neurosciences ◽

10.1016/0166-2236(87)90087-7 ◽

1987 ◽

Vol 10 (8) ◽

pp. 318-321 ◽

Cited By ~ 65

Author(s):

H.Robert Guy ◽

Ferdinand Hucho

Keyword(s):

Ion Channel ◽

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine

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A model for short α-neurotoxin bound to nicotinic acetylcholine receptor from Torpedo californica: Comparison with long-chain α-neurotoxins and α-conotoxins

Computational Biology and Chemistry ◽

10.1016/j.compbiolchem.2005.08.007 ◽

2005 ◽

Vol 29 (6) ◽

pp. 398-411 ◽

Cited By ~ 26

Author(s):

D.Yu. Mordvintsev ◽

Ya.L. Polyak ◽

O.V. Levtsova ◽

Ye.V. Tourleigh ◽

I.E. Kasheverov ◽

...

Keyword(s):

Acetylcholine Receptor ◽

Nicotinic Acetylcholine Receptor ◽

Nicotinic Acetylcholine ◽

Torpedo Californica ◽

Long Chain

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