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Mechanism of inhibition of cholinesterases by huperzine A

Biochemical and Biophysical Research Communications, 1992
Huperzine A, an alkaloid isolated from Huperzia serrata was found to reversibly inhibit acetylcholinesterases (EC 3.1.1.7) and butyrylcholinesterases (EC 3.1.1.8) with on- and off-rates that depend on both the type and the source of enzyme. Long-term incubation of high concentrations of purified cholinesterases (1-8 microM) with huperzine A did not ...
Y, Ashani, J O, Peggins, B P, Doctor
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ChemInform Abstract: Synthesis of a Hybrid Analogue (I) of the Acetylcholinesterase Inhibitors Huperzine A and Huperzine B.

ChemInform, 2001
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
V. Rajendran   +4 more
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[+]-Huperzine A Protects Against Soman Toxicity in Guinea Pigs

Neurochemical Research, 2011
The chemical warfare nerve agent (CWNA) soman irreversibly inhibits acetylcholinesterase (AChE) causing seizure, neuropathology and neurobehavioral deficits. Pyridostigmine bromide (PB), the currently approved pretreatment for soman, is a reversible AChE inhibitor that does not cross the blood-brain barrier (BBB) to protect against central nervous ...
Ying, Wang   +5 more
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Is There a Better Source of Huperzine A than Huperzia serrata? Huperzine A Content of Huperziaceae Species in China

Journal of Agricultural and Food Chemistry, 2005
A precise and selective reversed phase high-performance liquid chromatographic method was developed for quantifying huperzine A (HupA) in samples of the Huperziaceae in China. This method was used to quantify the levels of HupA in samples of Huperzia serrata collected from a single population at different times of the year, in different organs of the ...
Xiaoqiang, Ma   +3 more
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A convergent approach to huperzine A and analogues

Tetrahedron Letters, 2000
Abstract An aldol reaction between the enolate of cyclohexenone and 3-bromo-6-methoxy-1-formylpyridine, followed by protection of the resultant alcohol and reaction with Pd(0) yielded 5-methoxy-8-tert-butyldimethylsilylanyloxy-6-azatricyclo[7.3.1.02,7]trideca-2,4,6,11-tetraen-13-one, which has the basic skeleton of huperzine A.
Yann Foricher, John Mann
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Bivalent Ligands Derived from Huperzine A as Acetylcholinesterase Inhibitors

Current Topics in Medicinal Chemistry, 2007
The naturally occurring alkaloid Huperzine A (HupA) is an acetylcholinesterase (AChE) inhibitor that has been used for centuries as a Chinese folk medicine in the context of its source plant Huperzia Serrata. The potency and relative safety of HupA rendered it a promising drug for the ameliorative treatment of Alzheimer's disease (AD) vis-à-vis the ...
H, Haviv   +3 more
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ChemInform Abstract: A Formal Synthesis of (+)‐Huperzine A.

ChemInform, 2000
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
Arnaud Haudrechy   +3 more
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A concise and convergent (formal) total synthesis of huperzine A

Org. Biomol. Chem., 2007
The first convergent synthesis of the tricyclic skeleton of huperzine A is described and includes, as the key step, an efficient regioselective intramolecular Heck reaction of 2-(tert-butyldimethylsilyloxymethyl)-6-(2-methoxy-5-bromopyridin-6-yl)methylcyclohex-2-enol.
Mann, John, Lucey, C., Kelly, S.
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Huperzine A

2021
Weaam Ebrahim   +2 more
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Huperzine A: A nootropic agent in the shade [Huperzin A: Gölgede Kalmış bir Nootropik Ajan]

2019
Huperzine A is a sesquiterpene alkaloid found in the chemical composition of the medical plant Huperzia serrata. Huperzine A has attracted the attention of neuroscientists after the discovery of its strong and selective inhibitory activity on the acetylcholinesterase enzyme.
Turan, Yücel, N., Can, Özgür Devrim
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