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Alteration in ion channel function of mouse nicotinic acetylcholine receptor by mutations in the M4 transmembrane domain (vol 170, pg 157, 1999)
被引:0
|
作者
:
Tamamizu, S
论文数:
0
引用数:
0
h-index:
0
Tamamizu, S
Lee, YH
论文数:
0
引用数:
0
h-index:
0
Lee, YH
Hung, B
论文数:
0
引用数:
0
h-index:
0
Hung, B
McNamee, MG
论文数:
0
引用数:
0
h-index:
0
McNamee, MG
Lasalde-Dominicci, JA
论文数:
0
引用数:
0
h-index:
0
Lasalde-Dominicci, JA
机构
:
来源
:
JOURNAL OF MEMBRANE BIOLOGY
|
1999年
/ 172卷
/ 01期
关键词
:
D O I
:
暂无
中图分类号
:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号
:
071010 ;
081704 ;
摘要
:
引用
收藏
页码:89 / 89
页数:1
相关论文
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Subunit-selective role of the M3 transmembrane domain of the nicotinic acetylcholine receptor in channel gating
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Univ Nacl Sur, CONICET, Inst Invest Bioquim, Bahia Blanca, Buenos Aires, Argentina
Univ Nacl Sur, CONICET, Inst Invest Bioquim, Bahia Blanca, Buenos Aires, Argentina
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Corradi, Jeremias
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0
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Univ Nacl Sur, CONICET, Inst Invest Bioquim, Bahia Blanca, Buenos Aires, Argentina
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Corradi, Jeremias
Bouzat, Cecilia
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0
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0
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Univ Nacl Sur, CONICET, Inst Invest Bioquim, Bahia Blanca, Buenos Aires, Argentina
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Slow channel mutations in the center of the M1 transmembrane domain of acetylcholine receptor (AChR) α subunit
Ohno, K
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Ohno, K
Wang, HL
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Wang, HL
Shen, XM
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Milone, M
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Milone, M
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Bernasconi, L
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Engel, AG
NEUROLOGY,
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Slow-channel mutation in acetylcholine receptor αM4 domain and its efficient knockdown
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Mayo Clin, Dept Neurol & Neuromusc Res Lab, Rochester, MN 55905 USA
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Engel, Andrew G.
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Mayo Clin, Dept Neurol & Neuromusc Res Lab, Rochester, MN 55905 USA
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Engel, Andrew G.
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[24]
The functional role of the αM4 transmembrane helix in the muscle nicotinic acetylcholine receptor probed through mutagenesis and coevolutionary analyses
Thompson, Mackenzie J.
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机构:
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Univ Ottawa, Dept Biochem Microbiol & Immunol, Ottawa, ON, Canada
Thompson, Mackenzie J.
Domville, Jaimee A.
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Univ Ottawa, Dept Biochem Microbiol & Immunol, Ottawa, ON, Canada
Univ Ottawa, Dept Biochem Microbiol & Immunol, Ottawa, ON, Canada
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Baenziger, John E.
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Baenziger, John E.
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The Role of Transmembrane Domain 3 in the Actions of Orthosteric, Allosteric, and Atypical Agonists of the M4 Muscarinic Acetylcholine Receptor
Leach, Katie
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Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
Monash Univ, Dept Pharmacol, Parkville, Vic 3052, Australia
Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
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Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
Monash Univ, Dept Pharmacol, Parkville, Vic 3052, Australia
Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
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Christopoulos, Arthur
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Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
Monash Univ, Dept Pharmacol, Parkville, Vic 3052, Australia
Monash Univ, Monash Inst Pharmaceut Sci, Parkville, Vic 3052, Australia
Christopoulos, Arthur
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Acetylcholine receptor M3 domain: stereochemical and volume contributions to channel gating (vol 2, pg 226, 1999)
Wang, HL
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Tonali, P
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MUTATIONS OF CYS451 IN THE M4 HELIX OF THE GAMMA-SUBUNIT OF ACETYLCHOLINE-RECEPTOR DECREASE THE ION CHANNEL ACTIVITY
LI, L
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UNIV CALIF DAVIS,DEPT BIOCHEM & BIOPHYS,DAVIS,CA 95616
LI, L
PALMA, A
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PALMA, A
PAPPONE, P
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UNIV CALIF DAVIS,DEPT BIOCHEM & BIOPHYS,DAVIS,CA 95616
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MCNAMEE, M
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Tryptophan substitutions in the alpha M3 domain of the muscle-type nicotinic acetylcholine receptor alter ion channel function
Navedo, MF
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Univ Puerto Rico, San Juan, PR 00931 USA
Navedo, MF
Nieves, M
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Univ Puerto Rico, San Juan, PR 00931 USA
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Charged amino acid motifs flanking each extreme of the αM4 transmembrane domain are involved in assembly and cell-surface targeting of the muscle nicotinic acetylcholine receptor
Roccamo, A. M.
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Inst Invest Bioquim, Bahia Blanca, Argentina
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