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Results: 1-9 |
Results: 9
Characterization of recombinant, soluble beta-secretase from an insect cell expression system
Authors: Mallender, WD Yager, D Onstead, L Nichols, MR Eckman, C Sambamurti, K Kopcho, LM Marcinkeviciene, J Copeland, RA Rosenberry, TL
Citation: Wd. Mallender et al., Characterization of recombinant, soluble beta-secretase from an insect cell expression system, MOLEC PHARM, 59(3), 2001, pp. 619-626
Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheralsite that reveals conformational interactions between the peripheral and acylation sites
Authors: De Ferrari, GV Mallender, WD Inestrosa, NC Rosenberry, TL
Citation: Gv. De Ferrari et al., Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheralsite that reveals conformational interactions between the peripheral and acylation sites, J BIOL CHEM, 276(26), 2001, pp. 23282-23287
Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors
Authors: Harel, M Kryger, G Rosenberry, TL Mallender, WD Lewis, T Fletcher, RJ Guss, JM Silman, I Sussman, JL
Citation: M. Harel et al., Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors, PROTEIN SCI, 9(6), 2000, pp. 1063-1072
Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease
Authors: Camps, P Cusack, B Mallender, WD El Achab, R Morral, J Munoz-Torrero, D Rosenberry, TL
Citation: P. Camps et al., Huprine X is a novel high-affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease, MOLEC PHARM, 57(2), 2000, pp. 409-417
Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway
Authors: Mallender, WD Szegletes, T Rosenberry, TL
Citation: Wd. Mallender et al., Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway, BIOCHEM, 39(26), 2000, pp. 7753-7763
In vitro transport of active alpha(1)-antitrypsin to the apical surface ofepithelia by targeting the polymeric immunoglobulin receptor
Authors: Eckman, EA Mallender, WD Szegletes, T Silski, CL Schreiber, JR Davis, PB Ferkol, TW
Citation: Ea. Eckman et al., In vitro transport of active alpha(1)-antitrypsin to the apical surface ofepithelia by targeting the polymeric immunoglobulin receptor, AM J RESP C, 21(2), 1999, pp. 246-252
Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands - Distinct effects of propidium and fasciculin
Authors: Mallender, WD Szegletes, T Rosenberry, TL
Citation: Wd. Mallender et al., Organophosphorylation of acetylcholinesterase in the presence of peripheral site ligands - Distinct effects of propidium and fasciculin, J BIOL CHEM, 274(13), 1999, pp. 8491-8499
A steric blockade model for inhibition of acetylcholinesterase by peripheral site ligands and substrate
Authors: Rosenberry, TL Mallender, WD Thomas, PJ Szegletes, T
Citation: Tl. Rosenberry et al., A steric blockade model for inhibition of acetylcholinesterase by peripheral site ligands and substrate, CHEM-BIO IN, 120, 1999, pp. 85-97
Substrate binding to the peripheral site of acetylcholinesterase initiatesenzymatic catalysis. Substrate inhibition arises as a secondary effect
Authors: Szegletes, T Mallender, WD Thomas, PJ Rosenberry, TL
Citation: T. Szegletes et al., Substrate binding to the peripheral site of acetylcholinesterase initiatesenzymatic catalysis. Substrate inhibition arises as a secondary effect, BIOCHEM, 38(1), 1999, pp. 122-133
Risultati: 1-9 |