Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Shelley Camp"'
Publikováno v:
Protein & Peptide Letters. 19:173-179
The α/β hydrolase fold family is perhaps the largest group of proteins presenting significant structural homology with divergent functions, ranging from catalytic hydrolysis to heterophilic cell adhesive interactions to chaperones in hormone produc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ece4d0cc730066857a06219a616150c5
https://doi.org/10.2174/092986612799080103
https://doi.org/10.2174/092986612799080103
Contributions of selective knockout studies to understanding cholinesterase disposition and function
Autor:
Oksana Lockridge, Shelley Camp, Véronique Bernard, Palmer Taylor, Antonella De Jaco, Ellen G. Duysen, Limin Zhang, Emmanuelle Girard, Alexandre Dobbertin, Eric Krejci
Publikováno v:
Chemico-Biological Interactions
Chemico-Biological Interactions, Elsevier, 2010, 187 (1-3), pp.72-77. ⟨10.1016/j.cbi.2010.02.008⟩
Chemico-Biological Interactions, Elsevier, 2010, 187 (1-3), pp.72-77. ⟨10.1016/j.cbi.2010.02.008⟩
International audience; The complete knockout of the acetylcholinesterase gene (AChE) in the mouse yielded a surprising phenotype that could not have been predicted from deletion of the cholinesterase genes in Drosophila, that of a living, but functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::865f641f1adaf8a10ddc7237b1979ebc
https://doi.org/10.1016/j.cbi.2010.02.008
https://doi.org/10.1016/j.cbi.2010.02.008
Autor:
Goran Bucht, Limin Zhang, Michael Marquez, Shelley Camp, Brian de la Torre, Jeffery M. Long, Palmer Taylor
Publikováno v:
Chemico-Biological Interactions. :79-86
AChE is an alternatively spliced gene. Exons 2, 3 and 4 are invariantly spliced, and this sequence is responsible for catalytic function. The 3' alternatively spliced exons, 5 and 6, are responsible for AChE disposition in tissue [J. Massoulie, The o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::876374257b1b8540e2ea3af4b4884e14
https://doi.org/10.1016/j.cbi.2005.10.012
https://doi.org/10.1016/j.cbi.2005.10.012
Autor:
Claudine N. Prowse, Elizabeth J. Ackermann, Pierre E. Bougis, Shelley Camp, Zoran Radić, Joan R. Kanter, Palmer Taylor, Pascale Marchot
Publikováno v:
Journal of Biological Chemistry. 272:3502-3510
Fasciculin, a selective peptidic inhibitor of acetylcholinesterase, is a member of the three-fingered peptide toxin superfamily isolated from snake venoms. The availability of a crystal structure of a fasciculin 2 (Fas2)-acetylcholinesterase complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff742d31463e30610dc975934573f8f3
https://doi.org/10.1074/jbc.272.6.3502
https://doi.org/10.1074/jbc.272.6.3502
Autor:
Joan R. Kanter, Joel L. Sussman, Palmer Taylor, Pascale Marchot, Raimond B. G. Ravelli, Shelley Camp, Mia L. Raves, Daniel C. Vellom, Yves Bourne
Publikováno v:
Protein Science. 5:672-679
A soluble, monomeric form of acetylcholinesterase from mouse (mAChE), truncated at its carboxyl-terminal end, was generated from a cDNA encoding the glycophospholipid-linked form of the mouse enzyme by insertion of an early stop codon at position 549
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5a6a0f1a95331c22343dd5875b9bad07
https://doi.org/10.1002/pro.5560050411
https://doi.org/10.1002/pro.5560050411
Publikováno v:
Journal of Biological Chemistry. 270:1866-1872
The increase in acetylcholinesterase expression during muscle differentiation from myoblasts to myotubes was shown previously to reflect primarily a greater stability of the messenger RNA (mRNA). Here, we investigate the regulation of the acetylcholi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01b8359dcb0e94a903c33fdd7e574510
https://doi.org/10.1074/jbc.270.4.1866
https://doi.org/10.1074/jbc.270.4.1866
Publikováno v:
FEBS Journal
FEBS Journal, Wiley, 2012, 279 (23), pp.4293-305. ⟨10.1111/febs.12019⟩
FEBS Journal, Wiley, 2012, 279 (23), pp.4293-305. ⟨10.1111/febs.12019⟩
The α/β-hydrolase fold superfamily of proteins is composed of structurally related members that, despite great diversity in their catalytic, recognition, adhesion and chaperone functions, share a common fold governed by homologous residues and cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::125cb891849d7cc7cab7b8e2b78915ac
http://hdl.handle.net/11573/485497
http://hdl.handle.net/11573/485497
Publikováno v:
Biochemistry. 32:12074-12084
By examining inhibitor interactions with single and multiple site-specific mutants of mouse acetylcholinesterase, we have identified three distinct domains in the cholinesterase structure that are responsible for conferring selectivity for acetyl- an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c701ae3c9ac4cc43af4a0b4ad171fed5
https://doi.org/10.1021/bi00096a018
https://doi.org/10.1021/bi00096a018
Autor:
C. M. Harper, David O. Hutchinson, T. J. Walls, S. Nakano, Palmer Taylor, Shelley Camp, Andrew G. Engel, Joan M. Brengman
Publikováno v:
Annals of the New York Academy of Sciences. 681:469-486
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebeb5c8bba6a16211ca89c0c3ff888de
https://doi.org/10.1111/j.1749-6632.1993.tb22931.x
https://doi.org/10.1111/j.1749-6632.1993.tb22931.x
Publikováno v:
Journal of Biological Chemistry. 268:5790-5797
This study examines the tissue specificity and the gene products arising from alternative mRNA processing of the mammalian acetylcholinesterase gene. By splicing either alternative exons 5 or 6 in the mouse and human genes directly to the invariant e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5954e1377ecc2874783076bcea6a1abd
https://doi.org/10.1016/s0021-9258(18)53388-3
https://doi.org/10.1016/s0021-9258(18)53388-3