Results 331 to 340 of about 176,114 (393)

Oxidase-mimicking activity of ultrathin MnO2 nanosheets in colorimetric assay of acetylcholinesterase activity.

Nanoscale, 2017
In the present study, a novel colorimetric sensing platform was constructed for quantitative detection of acetylcholinesterase (AChE) activity and its inhibitor.
Xu Yan, Yang Song, Xiaoli Wu, Chengzhou Zhu, X. Su, Dan Du, Yuehe Lin   +6 more
semanticscholar   +1 more source

ACETYLCHOLINESTERASE

Canadian Journal of Biochemistry, 1964
The general characteristics of acetylcholinesterase are described. The mechanism of action of the enzyme is considered primarily in relation to the two steps in the hydrolysis of acetylcholine, the acetylation and deacetylation reactions. Competitive and non-competitive inhibition, and inhibitions by hydrogen ion and by substrate, are explained in ...
openaire   +2 more sources

Acetylcholinesterase: A Primary Target for Drugs and Insecticides.

Mini-Reviews in Medical Chemistry, 2017
BACKGROUND Acetylcholinesterase is a serine hydrolase that terminates the action of the neurotransmitter acetylcholine by hydrolyzing it into acetic acid and choline.
Sunita Thapa, M. Lv, Hui Xu
semanticscholar   +1 more source

The thermal inactivation of acetylcholinesterase

Biochimica et Biophysica Acta, 1963
Abstract Thermal inactivation of acetylcholinesterase (Acetylcholine acetyl-hydrolase, EC, 3.1.1.7) from mammalian erythrocytes is accompanied by a decrease in the Michaelis constant K8, while the substrate inhibition constant K32 remains unchanged. The time course involves two first-order processes, suggesting (a) the presence of two enzymes, or (b)
M.H. Coleman, D.D. Eley
openaire   +3 more sources

Immunoenzymology of acetylcholinesterase—I

Immunochemistry, 1969
Abstract Antibodies to bovine erthrocyte acetylcholinesterase were obtained from rabbits following immunization with the enzyme. The combination of the enzyme with antibodies did not affect its enzymatic activity as measured by K m values and substrate specificity. However, whereas the enzyme was found to lose activity upon heating at 60°C for a
D Michaeli, J.D Pinto, F.D de Buren, E Benjamini   +3 more
openaire   +3 more sources

Structures of human acetylcholinesterase in complex with pharmacologically important ligands.

Journal of Medicinal Chemistry, 2012
Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to ...
J. Cheung, M. Rudolph, F. Burshteyn, M. Cassidy, E. Gary, J. Love, M. Franklin, J. Height   +7 more
semanticscholar   +1 more source

Molecular Dynamics of Acetylcholinesterase

Accounts of Chemical Research, 2002
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Shen, Tongye, Tai, Kaihsu, Henchman, Richard H., McCammon, J. Andrew   +3 more
openaire   +4 more sources

Breathing Without Acetylcholinesterase

2004
Acetylcholine (ACh) mediates neurotransmission at the neuromuscular junction and is involved in respiratory control1, notably chemosensitivity2 of central and peripheral origin. The level of ACh at the synaptic cleft and neuromuscular junction is regulated by the enzyme acetylcholinesterase (AChE).
Chatonnet, Fabrice, Boudinot, Eliane, Chatonnet, Arnaud, Champagnat, Jean, Foutz, Arthur   +4 more
openaire   +5 more sources

Toward an Artificial Acetylcholinesterase

Chemistry - A European Journal, 2000
The methanolysis of choline p-nitrophenylcarbonate in chloroform containing 1% methanol is catalyzed with turnover by ditopic receptors 1 and 2, consisting of a calix[6]arene connected to a bicyclic guanidinium by means of a short spacer. The calix[6]arene subunit strongly binds to the trimethylammonium head group through cation-pi interactions ...
CUEVAS F., DI STEFANO, Stefano, MAGRANS J. O., PRADOS P., MANDOLINI, Luigi, DE MENDOZA J.   +5 more
openaire   +4 more sources

Hysteresis of insect acetylcholinesterase

Chemico-Biological Interactions, 2008
Pre-steady-state catalytic properties of insect acetylcholinesterase (AChE, EC 3.1.1.7) were studied with the neutral substrate N-methylindoxylacetate. Kinetics of soluble Apis mellifera and Drosophila melanogaster AChE forms showed lags (v(i)=0) before reaching the steady-state.
Badiou, Alexandra, Froment, M.T., Fournier, Dominique, Masson, P., Belzunces, Luc   +4 more
openaire   +4 more sources