메뉴 건너뛰기




Volumn 12, Issue 4, 2014, Pages 285-290

Low molecular weight precursor applicable for Alzheimer disease drugs synthesis (AChE and BChE inhibition, BACE inhibition, antioxidant properties and in silico modulation)

Author keywords

Acetylcholinesterase; Alzheimer disease; Betasecretase; Inhibition; Neurodegeneration

Indexed keywords

7 METHOXYTACRINE; ACETYLCHOLINESTERASE; ACETYLCYSTEINE; ACRIDINE; BETA SECRETASE; BETA SECRETASE INHIBITOR; CHINOLINE; CHOLINESTERASE INHIBITOR; DONEPEZIL; GALANTAMINE; HUPERZINE A; INDOLE; ISOQUINOLINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; PIPERIDINE; PYRIDINE; PYRIDOXINE B6; RIVASTIGMINE; TACRINE; TROLOX C; TRYPTAMINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 84925988858     PISSN: 1214021X     EISSN: 12140287     Source Type: Journal    
DOI: 10.1016/j.jab.2014.01.010     Document Type: Article
Times cited : (11)

References (29)
  • 3
    • 34247581682 scopus 로고    scopus 로고
    • Development of huperzine A and B for treatment of Alzheimer's disease
    • Bai, D., 2007. Development of huperzine A and B for treatment of Alzheimer's disease. Pure Appl. Chem. 79, 469-479.
    • (2007) Pure Appl. Chem , vol.79 , pp. 469-479
    • Bai, D.1
  • 4
    • 79960676808 scopus 로고    scopus 로고
    • Rivastigmine lowers Ab and increases sAPPa levels, which parallel elevated synaptic markers and metabolic activity in degenerating primary rat neurons
    • Bailey, J., Ray, B., Greig, N., Lahiri, D., 2011. Rivastigmine lowers Ab and increases sAPPa levels, which parallel elevated synaptic markers and metabolic activity in degenerating primary rat neurons. PLOS ONE 6, e21954.
    • (2011) PLOS ONE , vol.6 , pp. e21954
    • Bailey, J.1    Ray, B.2    Greig, N.3    Lahiri, D.4
  • 10
    • 0037375876 scopus 로고    scopus 로고
    • Cholineterases: New roles in brain function and in Azheimer's disease
    • Giacobini, E., 2003. Cholineterases: new roles in brain function and in Azheimer's disease. Neurochem. Res. 28, 515-522.
    • (2003) Neurochem. Res , vol.28 , pp. 515-522
    • Giacobini, E.1
  • 12
    • 0034681279 scopus 로고    scopus 로고
    • Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo Californica
    • Koellner, G., Kryger, G., Millard, C.B., Silman, I., Sussman, J.L., Steiner, T., 2000. Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo Californica. J. Mol. Biol. 296, 713-735.
    • (2000) J. Mol. Biol , vol.296 , pp. 713-735
    • Koellner, G.1    Kryger, G.2    Millard, C.B.3    Silman, I.4    Sussman, J.L.5    Steiner, T.6
  • 13
    • 11144328091 scopus 로고    scopus 로고
    • The Lycopodium alkaloids
    • Ma, X., Gang, D.R., 2004. The Lycopodium alkaloids. Nat. Prod. Rep. 21, 752-772.
    • (2004) Nat. Prod. Rep , vol.21 , pp. 752-772
    • Ma, X.1    Gang, D.R.2
  • 14
    • 34547333504 scopus 로고    scopus 로고
    • Multiwell fluorometric a colorimetric microassays for the evaluation of β-secretase (BACE-1) inhibitors
    • Mancini, F., Naldi, M., Cavrini, V., Andrisano, V., 2007. Multiwell fluorometric a colorimetric microassays for the evaluation of β-secretase (BACE-1) inhibitors. Anal. Bioanal. Chem. 388, 1175-1183.
    • (2007) Anal. Bioanal. Chem , vol.388 , pp. 1175-1183
    • Mancini, F.1    Naldi, M.2    Cavrini, V.3    Andrisano, V.4
  • 15
    • 0027973241 scopus 로고
    • Butyrylcholinesterase reactivity differentiates the amyloid plaques of aging from those of dementia
    • Mesulam, M., Geula, C., 1994. Butyrylcholinesterase reactivity differentiates the amyloid plaques of aging from those of dementia. Am. Neurol. 36, 722-727.
    • (1994) Am. Neurol , vol.36 , pp. 722-727
    • Mesulam, M.1    Geula, C.2
  • 18
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicholet, Y., Lockridge, O., Masson, P., Fontecilla-Camps, J.C., Nachon, F., 2003. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem. 278, 41141-41147.
    • (2003) J. Biol. Chem , vol.278 , pp. 41141-41147
    • Nicholet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 19
    • 77953495128 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors in Alzheimer's disease: Further comments on their mechanisms of action and therapeutic consequences
    • Nieoullon, A., 2010. Acetylcholinesterase inhibitors in Alzheimer's disease: further comments on their mechanisms of action and therapeutic consequences. Psychol. Neurosychiatr. Vieil. 8, 123-131.
    • (2010) Psychol. Neurosychiatr. Vieil , vol.8 , pp. 123-131
    • Nieoullon, A.1
  • 20
    • 80054096801 scopus 로고    scopus 로고
    • Cholinesterases, a target of pharmacology and toxicology
    • Pohanka, M., 2011. Cholinesterases, a target of pharmacology and toxicology. Biomed. Pap. 155, 219-223.
    • (2011) Biomed. Pap , vol.155 , pp. 219-223
    • Pohanka, M.1
  • 21
    • 84864213744 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibitors: A patent review ( 2008-present)
    • Pohanka, M., 2012. Acetylcholinesterase inhibitors: a patent review (2008-present). Expert Opin. Ther. Pat. 22, 871-886.
    • (2012) Expert Opin. Ther. Pat , vol.22 , pp. 871-886
    • Pohanka, M.1
  • 22
    • 84893306847 scopus 로고    scopus 로고
    • Alzheimer's disease and oxidative stress: A review
    • Pohanka, M., 2013. Alzheimer's disease and oxidative stress: a review. Curr. Med. Chem. 21, 356-364.
    • (2013) Curr. Med. Chem , vol.21 , pp. 356-364
    • Pohanka, M.1
  • 23
    • 84880932391 scopus 로고    scopus 로고
    • Spectrophotometric methods based on 2,6-dichloroindophenol acetate and indoxylacetate for butyrylcholinesterase activity assay in plasma
    • Pohanka, M., Drtinova, L., 2013. Spectrophotometric methods based on 2,6-dichloroindophenol acetate and indoxylacetate for butyrylcholinesterase activity assay in plasma. Talanta 106, 281-285.
    • (2013) Talanta , vol.106 , pp. 281-285
    • Pohanka, M.1    Drtinova, L.2
  • 24
    • 0034701238 scopus 로고    scopus 로고
    • The origins of Alzheimer disease: A is for amyloid
    • Selkoe, D.J., 2000. The origins of Alzheimer disease: a is for amyloid. JAMA 283, 1615-1617.
    • (2000) JAMA , vol.283 , pp. 1615-1617
    • Selkoe, D.J.1
  • 25
    • 0028823072 scopus 로고
    • Synthesis and structure-activity relationships of aceylcholinesterase inhibitors: 1-benzyl-4-[( 5,6-dimethoxy-1-oxoindan-2-yl)methyl]piperidine hydrochloride and related compounds
    • Sugimoto, H., Iimura, Y., Yamanishi, Y., Yamatsu, K., 1995. Synthesis and structure-activity relationships of aceylcholinesterase inhibitors: 1-benzyl-4-[(5,6-dimethoxy-1-oxoindan-2-yl)methyl]piperidine hydrochloride and related compounds. J. Med. Chem. 38, 4821-4829.
    • (1995) J. Med. Chem , vol.38 , pp. 4821-4829
    • Sugimoto, H.1    Iimura, Y.2    Yamanishi, Y.3    Yamatsu, K.4
  • 26
    • 20944446415 scopus 로고    scopus 로고
    • Neuroprotective effects of huperzine A
    • Wang, R., Tang, X.C., 2005. Neuroprotective effects of huperzine A. Neurosignals 14, 71-82.
    • (2005) Neurosignals , vol.14 , pp. 71-82
    • Wang, R.1    Tang, X.C.2
  • 27
    • 84862789255 scopus 로고    scopus 로고
    • Quantitative structure and bioactivity relationship study on human acetylcholinesterase inhibitors
    • Yan, A., Wang, K., 2012. Quantitative structure and bioactivity relationship study on human acetylcholinesterase inhibitors. Bioorg. Med. Chem. Lett. 22, 3336-3342.
    • (2012) Bioorg. Med. Chem. Lett , vol.22 , pp. 3336-3342
    • Yan, A.1    Wang, K.2
  • 29
    • 39149123780 scopus 로고    scopus 로고
    • Non-cholinergic effects of huperzine A: Beyond inhibition of acetylcholinesterase
    • Zhang, H.Y., Yan, H., Tang, X.C., 2008. Non-cholinergic effects of huperzine A: beyond inhibition of acetylcholinesterase. Cell. Mol. Neurobiol. 28, 173-183.
    • (2008) Cell. Mol. Neurobiol , vol.28 , pp. 173-183
    • Zhang, H.Y.1    Yan, H.2    Tang, X.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.