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Volumn 16, Issue 22, 2008, Pages 9729-9740

Synthesis, structure-activity relationships and molecular modeling studies of new indole inhibitors of monoamine oxidases A and B

Author keywords

Amine oxidase; Indole; Molecular dynamics; Molecular modeling; Monoamine oxidase type A; Monoamine oxidase type B; Structure activity relationships

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; MONOAMINE OXIDASE A INHIBITOR; MONOAMINE OXIDASE B INHIBITOR; N METHYL N (3 PHENYLPROPYL) 1H INDOLE 2 CARBOXAMIDE; UNCLASSIFIED DRUG;

EID: 84954358613     PISSN: 09680896     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmc.2008.09.072     Document Type: Article
Times cited : (37)

References (55)
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    • Database searching (SWISS-PROT), sequence alignment, and analysis of rat, bovine and human MAO sequences were carried out using FASTA. Pearson W.R. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 2444-2448
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2444-2448
    • Pearson, W.R.1
  • 24
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    • and BLAST programs. Wang S., and Pak Y.J. Phys. Chem. B 104 (2000) 354-359
    • (2000) Phys. Chem. B , vol.104 , pp. 354-359
    • Wang, S.1    Pak, Y.J.2
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    • GOLD 3.1; CCDC Software Limited: Cambridge, UK, 2004.
    • GOLD 3.1; CCDC Software Limited: Cambridge, UK, 2004.
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    • Molecular Operating Environment (MOE), version 2005.06; Chemical Computing Group, Inc.: Montreal, Canada, 2005.
    • Molecular Operating Environment (MOE), version 2005.06; Chemical Computing Group, Inc.: Montreal, Canada, 2005.
  • 53
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    • note
    • Authors demonstrated that the binding of two inhibitors, rasagiline and isatin, to human MAO B I199F mutant enzyme is identical to that of WT enzyme. In both cases, the side chain of Phe199 extends into the entrance cavity with essentially identical conformations rather than the 'open/closed' conformations seen with Ile199. In the same paper, the authors pointed out that the presence of this bulky residue in the entrance cavity does not appear to alter the kinetic properties of the enzyme or the binding affinity of a small competitive inhibitor.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.