Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Wilson K.W. Luk"'
Autor:
Vicky P. Chen, Wilson K.W. Luk, Wallace K.B. Chan, K. Wing eLeung, Ava J.Y. Guo, Gallant K.L. Chan, Sherry L. Xu, Roy C.Y. Choi, Karl W.K. Tsim
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 4 (2011)
Acetylcholinesterase (AChE) is responsible for the hydrolysis of the neurotransmitter, acetylcholine, in the nervous system. The functional localization and oligomerization of AChE T variant are depending primarily on the association of their anchori
Externí odkaz:
https://doaj.org/article/5314fdbd7ea04d30a3351726db1f49a4
Autor:
Ping Yao, Etta Y. L. Liu, Miranda L. Xu, Karl Wah Keung Tsim, Tina T. X. Dong, Wilson K.W. Luk, Kevin Qiyun Wu, Cathy W. C. Bi
Publikováno v:
Journal of Neurochemistry. 146:390-402
Acetylcholinesterase (AChE; EC 3.1.1.7) is known to hydrolyze acetylcholine at cholinergic synapses. In mammalian erythrocyte, AChE exists as a dimer (G2 ) and is proposed to play role in erythropoiesis. To reveal the regulation of AChE during differ
Autor:
Karl Wah Keung Tsim, Qi Y. Wu, Miranda L. Xu, Ying J. Xia, Tina T. X. Dong, Wilson K.W. Luk, Etta Y. L. Liu, Xiang P. Kong
Publikováno v:
Chemico-biological interactions. 308
Acetylcholinesterase (AChE) hydrolyzes acetylcholine at cholinergic synapses, and which has various isoforms of AChE, i.e. AChER, AChEH and AChET, deriving from single gene. AChEH exists as a glycophosphatidylinositol (GPI)-linked dimer (G2), present
Autor:
Ping Yao, Wilson K.W. Luk, Anthony W.M. Cheng, Lily K. W. Cheng, Cathy W. C. Bi, Miranda L. Xu, Karl Wah Keung Tsim, Shinghung Mak, Kitty K.M. Lau
Publikováno v:
Journal of Molecular Neuroscience. 57:446-451
ATP is co-stored and co-released with acetylcholine (ACh) at the pre-synaptic vesicles in vertebrate neuromuscular junction (nmj). Several lines of studies demonstrated that binding of ATP to its corresponding P2Y1 and P2Y2 receptors in the muscle re
Autor:
Karl Wah Keung Tsim, Maria-Letizia Campanari, María-Salud García-Ayllón, Lidia Blazquez-Llorca, Wilson K.W. Luk, Javier Sáez-Valero
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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Acetylcholinesterase (AChE) is a key enzyme in the cholinergic nervous system and is one of the most studied proteins in the field of Alzheimer's disease (AD). Moreover, alternative functions of AChE unrelated with the hydrolysis of acetylcholine are
Autor:
Sun Yanjie, Wilson K.W. Luk, Heidi Qunhui Xie, Yuzhong Zheng, Tina T. X. Dong, Guangcai Zha, Roy Chi Yan Choi, Karl Wah Keung Tsim, Vicky Ping Chen, Xianghui Zou
Publikováno v:
Journal of Molecular Neuroscience. 53:424-428
Cholinesterases (ChEs) have been identified in vertebrates and invertebrates. Inhibition of ChE activity in invertebrates, such as bivalve molluscs, has been used to evaluate the exposure of organophosphates, carbamate pesticides, and heavy metals in
Autor:
Roy Chi Yan Choi, Guangcai Zha, Wilson K.W. Luk, Xianghui Zou, Vicky Ping Chen, Karl Wah Keung Tsim
Publikováno v:
Chemico-Biological Interactions. 203:277-281
Acetylcholinesterase (AChE) activity has been used to evaluate the exposure of mollusk bivalves to organophosphates, carbamate pesticides, and heavy metals. Crassostrea hongkongensis is a Hong Kong endemic oyster, and has a high commercial value alon
Publikováno v:
FEBS Journal. 279:3229-3239
Acetylcholinesterase (AChE) is well-known for its cholinergic functions in the nervous system; however, this enzyme is also found in other tissues where its function is still not understood. AChE is synthesized through alternative splicing as splicin
Publikováno v:
Neuroscience Letters. 523:71-75
Acetylcholinesterase (AChE) is organized into globular tetramers (G4) by a structural protein called p roline- ri ch m embrane a nchor (PRiMA), anchoring it into the cell membrane of neurons in the brain. The assembly of AChE tetramers with PRiMA req
Autor:
Yuen H. Liu, Wilson K.W. Luk, Maria-Letizia Campanari, Cathy W. C. Bi, Roy Chi Yan Choi, Karl Wah Keung Tsim, Kei M. Lau, Javier Sáez-Valero, Li Xu, Miranda L. Xu
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
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Acetylcholinesterase (AChE) is encoded by a single gene, and the alternative splicing at the 3′ end produces different isoforms, including tailed (AChET), read-through (AChER), and hydrophobic (AChEH). Different forms of this enzyme exist in differ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b11e0946514789183088ce920dddbfc
http://hdl.handle.net/10261/123011
http://hdl.handle.net/10261/123011