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Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1646, Issue 1-2, 2003, Pages 119-130

Different degree of cooperativity in adult, embryonic and mutated mouse muscle nicotinic receptors

(2) Krusek J a Vyskocil F a,b

a INSTITUTE OF PHYSIOLOGY (Czech Republic)

b CHARLES UNIVERSITY (Czech Republic)

Author keywords

Affinity; Allostery; Binding site difference; Efficacy; Hill coefficient; Nicotinic ACh receptor; Site mutation

Indexed keywords

ACETYLCHOLINE; AMINO ACID; NICOTINIC RECEPTOR; RECEPTOR SUBUNIT;

AGONIST; ANIMAL CELL; ARTICLE; CELL STRAIN COS1; CHANNEL GATING; CONTROLLED STUDY; GENE MUTATION; HILL REACTION; MOLECULAR INTERACTION; MOUSE; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; RECEPTOR AFFINITY; STRAIN DIFFERENCE; WILD TYPE; ANIMAL; BINDING SITE; BIOSYNTHESIS; CHEMICAL MODEL; CHEMISTRY; COMPARATIVE STUDY; GENE VECTOR; METABOLISM; MOLECULAR CLONING; POINT MUTATION; PRENATAL DEVELOPMENT; SKELETAL MUSCLE;

ACETYLCHOLINE; ANIMALS; BINDING SITES; CLONING, MOLECULAR; COS CELLS; GENETIC VECTORS; MICE; MODELS, CHEMICAL; MUSCLE, SKELETAL; POINT MUTATION; RECEPTORS, NICOTINIC;

EID: 0043123446 PISSN: 15709639 EISSN: None Source Type: Journal
DOI: 10.1016/S1570-9639(02)00552-6 Document Type: Article

Times cited : (12)

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