Zobrazeno 1 - 10
of 449
pro vyhledávání: '"S. Brimijoin"'
Publikováno v:
Neurobiology of Disease, Vol 24, Iss 2, Pp 326-333 (2006)
Butyrylcholinesterase (BuChE) is increased in the cerebral cortex of Alzheimer's disease (AD) patients, particularly those carrying ε4 allele of the apolipoprotein E gene (ApoE) and certain BuChE variants that predict increased AD risk and poor resp
Externí odkaz:
https://doaj.org/article/f4639436b3b64dc28477255d2a5155ea
Autor:
V. Murthy, S. Brimijoin
This chapter briefly describes the promise of mutated versions of butyrylcholinesterase (BChE), a metabolic enzyme altered to treat cocaine addiction. BChE has been engineered into a highly efficient cocaine hydrolase (CocH) that inactivates cocaine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2893a4f549ea875d7e0c706094be418d
https://doi.org/10.1016/b978-0-12-803750-8.00068-3
https://doi.org/10.1016/b978-0-12-803750-8.00068-3
Autor:
C.J. Alves, P. Anglard, K. Anier, R.A. Armstrong, R.K. Bachtell, K. Bakshi, P. Barbanti, P. Barrio, A. Batalla, J.B. Becker, A. Bekker, C. Benkelfat, J. Bergman, P. Bhattacharya, Veronica Bisagno, S. Brimijoin, Z.J. Brown, D. Buffalari, K.-M. Bühler, L. Caffino, G. Cafforio, R. Camarini, V.M. Carvalho, L.C.S. Cepko, C.-C. Chen, X.-P. Chu, L.H. Corbit, E.J. Crofton, C.L. Crunelle, P.J. Cunha, T. Cunha-Oliveira, P.J. Currie, M. D’Ascenzo, L.H.J. Dieckmann, L. von Diemen, E.C. Dumont, A.L. Eagle, B.A. Eipper, J.E. Eipper-Mains, M. Engeln, S. Erb, A. Farré, M. Farré, A.S. Felts, L. Fofi, J.D. Foster, H.C. Fox, M. Frankfurt, M. Freissmuth, R.A. Fuchs, F. Fumagalli, P.A. Gajewski, E. Galaj, J.C.F. Galduróz, E.E. Garling, T.A. Gentile, G. Giannotti, J.-A. Girault, J.D. Glass, P.D. Goncalves, A. González-Duarte, V. Gonzalez-Nunez, R.W. Gould, C. Grassi, T.A. Green, T. Green-Sadan, H.H. Gu, Xiaowei Guan, B. Halbout, D.D. Han, L.K. Henry, J.L. Pérez de Heredia, J.A. Higginbotham, T. Hofmaier, M. Holy, K.-S. Hsu, C.-C. Huang, J. James, A.W. Jones, C.K. Jones, A. Kalda, D.N. Kearns, H.N. Kerver, F. Kessler, S.J. Kohut, K. Krnjević, P. Kucab, O. Kudlacek, D.A. Kupferschmidt, E.V. Kuzhikandathil, M.R. Lee, L. Leggio, J.R. Lever, S.Z. Lever, M. Leyton, J.-X. Li, D.R. Lima, M.K. Lobo, J.A. López-Moreno, H. López-Pelayo, D.A. Lovejoy, A. Luf, M.D.M.V. Lugon, C.E. Lyons, A. Magalhães, P.V.S. Magalhães, M. Mainardi, R.E. Mains, J.R. Mantsch, T. Marcourakis, R. Marhe, F. Matthys, S. El Mestikawy, V. Milivojevic, D.K. Miller, M.O. Min, S. Minnes, M.R. Mitchell, P.R. Monteiro, V. Murthy, J.W. Muschamp, C. Nagy, E.M. Nakamura-Palacios, J.C.M. Narvaez, C.P. Normandeau, F. Ornell, C.A. Orsini, S.B. Ostlund, J. Otkins, V.B. Patel, F.S. Pelição, S.P. Pereira, M.D. Peres, M.N. Potenza, V.R. Preedy, R.A. Prosser, B.B. Quednow, R. Rajendram, A.C. Ramos, R. Ranaldi, C. Rangel-Barajas, G.V. Rebec, A.J. Robison, R.E. Rodríguez, M.C.H. Rohn, I. Roth-Deri, S.G. Scala, C. Scavone, A. Schellekens, J. Scherer, R. Schmid, R.D. Scurlock, B. Setlow, S.J. Simmons, L.T. Singer, R. Sinha, H.H. Sitte, K. Smart, T. Stockner, T. Summavielle, K.K. Szumlinski, G. Tanda, M. Torrens, B.J. Tunstall, F.J. Urbano, R.A. Vaughan, M. Verhaeghe, M. Vonmoos, J.J. Wagner, Y. Wang, Z.-X. Xi, Y. Xu, G. Yadid, J.-H. Ye, S. Yoon, L.J. Zallar, Chang-Guo Zhan, H.-Y. Zhang, Y. Zhang, Fang Zheng, W. Zuo, J. Zwiller
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d02bdbc4a23e14ca18c8f4820ead3f26
https://doi.org/10.1016/b978-0-12-803750-8.00078-6
https://doi.org/10.1016/b978-0-12-803750-8.00078-6
Publikováno v:
Journal of neuroscience research. 63(2)
Acetylcholinesterase (AChE) can promote neurite outgrowth through a mechanism that is independent of its role in hydrolyzing the neurotransmitter acetylcholine. It has been proposed that this neuritogenic capacity of AChE may result from its intrinsi
Autor:
S. Brimijoin, E. Atanasova
Publikováno v:
Structure and Function of Cholinesterases and Related Proteins ISBN: 9781489915429
Evidence is accumulating to suggest more than one functional promoter in the gene for murine acetylcholinesterase (Ache). Previously, we detected moderately strong activity (12.5 times background) when a DNA sequence upstream of the established promo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c444704083fedc50a2350191a152e259
https://doi.org/10.1007/978-1-4899-1540-5_17
https://doi.org/10.1007/978-1-4899-1540-5_17
Autor:
S. Chiappa, S. Brimijoin
Publikováno v:
Structure and Function of Cholinesterases and Related Proteins ISBN: 9781489915429
Possible “non classical” roles for acetylcholinesterase (AChE) have attracted attention because of the enzyme’s widespread distribution and striking ontogenetic regulation, with bursts of expression that coincide in space and time with neurite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::643d0b5aa3f1519ec1d098fe2c174368
https://doi.org/10.1007/978-1-4899-1540-5_156
https://doi.org/10.1007/978-1-4899-1540-5_156
Publikováno v:
The Journal of biological chemistry. 271(39)
We report highly potent, selective, and low cost bifunctional acetylcholinesterase (AChE) inhibitors developed by our two-step prototype optimization strategy utilizing computer modeling of ligand docking with target proteins: 1) identify low affinit
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 277(2)
Monoclonal antibodies to acetylcholinesterase are known to destroy preganglionic sympathetic terminals in rats. To investigate resulting changes in sympathetic tone, turnover of norepinephrine (NE) was examined in five adrenergically innervated tissu
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 261(2)
The emulsifier for cyclosporin in clinical i.v. formulations, Cremophor EL, has recently come into question as a possible source of neurotoxic side effects in immunosuppressant therapy. To address this issue we tested Cremophor EL and cyclosporin on
Autor:
S, Brimijoin, V A, Lennon
Publikováno v:
Journal of neural transmission. Supplementum. 34
Systemic injection of monoclonal antibodies to neural acetylcholinesterase in rats causes permanent, complement-mediated destruction of presynaptic fibers in sympathetic ganglia and adrenal medulla. Ptosis, hypotension, bradycardia, and postural sync