Results 131 to 140 of about 12,358,109 (167)

X-ray Structures of Torpedo californica Acetylcholinesterase Complexed with (+)-Huperzine A and (−)-Huperzine B:  Structural Evidence for an Active Site Rearrangement^,

Biochemistry, 2002
Kinetic and structural data are presented on the interaction with Torpedo californica acetylcholinesterase (TcAChE) of (+)-huperzine A, a synthetic enantiomer of the anti-Alzheimer drug, (-)-huperzine A, and of its natural homologue (-)-huperzine B.
H, Dvir, H L, Jiang, D M, Wong, M, Harel, M, Chetrit, X C, He, G Y, Jin, G L, Yu, X C, Tang, I, Silman, D L, Bai, J L, Sussman   +11 more
openaire   +2 more sources

Preparative isolation of huperzines A and B from Huperzia serrata by displacement centrifugal partition chromatography

Journal of Chromatography A, 2007
The pH-zone refining centrifugal partition chromatography technique was used to separate the two acetylcholinesterase inhibitors huperzines A and B from a crude alkaloid extract of the club moss Huperzia serrata. Complete co-elution of huperzines A and B was initially observed with the well-known methyl tert-butyl ether-acetonitrile-water (4:1:5, v/v/v)
Toribio, Alix, Delannay, Eldra, Richard, Bernard, Zèches, Monique, Nuzillard, Jean-Marc, Renault, Jean-Hugues, Plé, Karen   +6 more
openaire   +3 more sources

Molecular Interaction of Human Brain Acetylcholinesterase with a Natural Inhibitor Huperzine-B: An Enzoinformatics Approach

CNS & Neurological Disorders - Drug Targets, 2014
The present study emphasizes the molecular interactions between human brain acetylcholinesterase (AChE) and the natural ligand Huperzine-B and its comparison to 'AChE-Tolserine interactions'. Docking between Huperzine-B and AChE was performed using 'Autodock4.2'.
Aftab, Alam, Sibhghatulla, Shaikh, Syed S, Ahmad, Mohammad A, Ansari, Shahnawaz, Shakil, Syed M D, Rizvi, Shazi, Shakil, Mohammad, Imran, Mohammad, Haneef, Adel M, Abuzenadah, Mohammad A, Kamal   +10 more
openaire   +2 more sources

The structures of huperzine A and B, two new alkaloids exhibiting marked anticholinesterase activity

Canadian Journal of Chemistry, 1986
Huperzine A and B, two new Lycopodium alkaloids isolated from Huperziaserrata (Thunb.) Trev., are shown to possess structures 1 and 3, respectively, on the basis of chemical and spectroscopic data.
Jia-Sen Liu, Yuan-Long Zhu, Chao-Mei Yu, You-Zuo Zhou, Yan-Yi Han, Feng-Wu Wu, Bao-Feng Qi   +6 more
openaire   +1 more source

Study on dual-site inhibitors of acetylcholinesterase: Highly potent derivatives of bis- and bifunctional huperzine B

Bioorganic & Medicinal Chemistry, 2007
Natural (-)-huperzine B (HupB), isolated from Chinese medicinal herb, displayed moderate inhibitory activity of acetylcholinesterase (AChE). Based on the active dual-site of AChE, a series of novel derivatives of bis- and bifunctional HupB were designed and synthesized.
Xu-Chang, He, Song, Feng, Zhi-Fei, Wang, Yufang, Shi, Suxin, Zheng, Yu, Xia, Hualiang, Jiang, Xi-can, Tang, Donglu, Bai   +8 more
openaire   +2 more sources

Huperzine B, a novel acetylcholinesterase inhibitor, attenuates hydrogen peroxide induced injury in PC12 cells

Neuroscience Letters, 2000
A number of studies indicate that free radicals are involved in the neurodegeneration in Alzheimer's disease (AD). The present study was mainly conducted to examine the effect of Huperzine B on H(2)O(2) induced toxicity in rat pheochromocytoma line PC12 by measuring cell lesion, level of lipid peroxidation and antioxidant enzyme activities. Following a
H Y, Zhang, X C, Tang
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In silico study of Huperzine B against Alzheimer's Disease

Journal of Advances in Developmental Research
Alzheimer’s disease (AD) is a progressive neurodegenerative disorder characterized by memory loss, cognitive decline, and neuronal damage. One of the major therapeutic approaches for AD involves inhibiting enzymes associated with disease progression, particularly acetylcholinesterase (AChE), which degrades acetylcholine in the brain.
Divyani Vilas Bankar -, Syeda Afifa -
openaire   +1 more source

STRUCTURAL FEATURE OF AChE INHIBITOR HUPERZINE B IN NATURE AND IN THE BINDING SITE OF AChE: DENSITY FUNCTIONAL THEORY STUDY COMBINED WITH IR DETERMINATION

Journal of Theoretical and Computational Chemistry, 2002
Quantum chemical DFT-B3LYP/6-31G* method and IR spectrometry have been used to investigate the natural and binding structures of Huperzine B (HupB) in order to better understand the interaction nature between acetylcholinesterase (AChE) and its inhibitor, with the view of designing new AChE inhibitors.
XIAOMIN LUO, CHENG FENG, XIAO-JIAN TAN, CHANGHENG TAN, DAYUAN ZHU, JIANHUA SHEN, XIAOQIN HUANG, TONG LIU, KAIXIAN CHEN, HUALIANG JIANG, WEILIANG ZHU, CHUM MOK PUAH, HAY DVIR, MICHAL HAREL, JOEL L. SUSSMAN, ISRAEL SILMAN   +15 more
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Inhibitory effects of huperzine B on cholinesterase activity in mice.

Zhongguo yao li xue bao = Acta pharmacologica Sinica, 1999
To determine the anticholinesterase properties of huperzine B (Hup B) and compare with tacrine in vitro and in vivo.Spectrophotometry was used to determine ChE activity.Hup B showed much more selective inhibition to acetylcholinesterase (AChE) than tacrine. The IC50 ratios of Hup B and tacrine for butyrylcholinesterase (BuChE): AChE were 65.8 and 0.54,
J, Liu, H Y, Zhang, L M, Wang, X C, Tang
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[Detection of Huperzine A and Huperzine B in fermentation broth of endophytic fungus Colletotrichum gloesporioides from Huperzia serrate by HPLC].

Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 2019
In this study, we established a rapid and efficient HPLC method to determine the accumulation of Huperzine A and Huperzine B in the fermentation broth of endophytic fungus Colletotrichum gloesporioides from Huperzia serrate. The chloroform extracts of fermentation broth were dissolved in methanol and filtered before injection for HPLC analysis.
Liqin, Hu, Xincong, Kang, Pengyuan, Shen, Tian, Chen, Jiayin, Zhang, Dongbo, Liu   +5 more
openaire   +1 more source