메뉴 건너뛰기




Volumn 70, Issue 12, 2004, Pages 1189-1194

Phosphodiesterase and thymidine phosphorylase-inhibiting salirepin derivatives from Symplocos racemosa

Author keywords

Phosphodiesterase I; Salirepin derivatives; Symplocaceae; Symplocos racemosa; Thymidine phosphorylase; Urease

Indexed keywords

BENZOYSALIREPOSIDE; GLYCOSIDE; PHOSPHODIESTERASE; PHOSPHODIESTERASE I; PLANT EXTRACT; SALIREPIN; SALIREPOSIDE; SYMPLOCOMOSIDE; SYMPLOCOS RACEMOSA EXTRACT; SYMPLOSOSIDE; SYMPLOVEROSIDE; SYMPONOSIDE; THYMIDINE PHOSPHORYLASE; UNCLASSIFIED DRUG;

EID: 11944252342     PISSN: 00320943     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2004-835850     Document Type: Article
Times cited : (31)

References (19)
  • 3
    • 77957008260 scopus 로고
    • Phosphodiesterases
    • Academic Press, Newark
    • Razzell WE. Phosphodiesterases. In: Methods in Enzymology Academic Press, Newark: 1963; Vol. VI: pp 236-42
    • (1963) Methods in Enzymology , vol.6 , pp. 236-242
    • Razzell, W.E.1
  • 4
    • 0035026555 scopus 로고    scopus 로고
    • Up-regulated expression of the phosphodiesterase nucleotide pyrophosphatase family member PC-1 is a marker and pathogenic factor for knee meniscal cartilage matrix calcification
    • Kristen J, Sanshiro H, Martin L, Kenneth P, James G, Robet T. Up-regulated expression of the phosphodiesterase nucleotide pyrophosphatase family member PC-1 is a marker and pathogenic factor for knee meniscal cartilage matrix calcification. Arthr Rheum 2001; 44: 1071-81
    • (2001) Arthr Rheum , vol.44 , pp. 1071-1081
    • Kristen, J.1    Sanshiro, H.2    Martin, L.3    Kenneth, P.4    James, G.5    Robet, T.6
  • 6
    • 0035427998 scopus 로고    scopus 로고
    • Thymidine phosphorylase: A two-faced Janus in anticancer chemotherapy
    • Focher F, Spadari S. Thymidine phosphorylase: A two-faced Janus in anticancer chemotherapy. Curr Cancer Drug Targets 2001; 1: 141-53
    • (2001) Curr Cancer Drug Targets , vol.1 , pp. 141-153
    • Focher, F.1    Spadari, S.2
  • 7
    • 0024514293 scopus 로고
    • Microbial urease: Significance, regulation and molecular characterization
    • Mobley HL, Hausinger RP. Microbial urease: significance, regulation and molecular characterization. Microbial Rev 1989; 53: 85-100
    • (1989) Microbial Rev , vol.53 , pp. 85-100
    • Mobley, H.L.1    Hausinger, R.P.2
  • 8
    • 0036676049 scopus 로고    scopus 로고
    • New alloaromadendrane, cadinene and cyclocopacamphane type sesquiterpene derivatives and bibenzyls from Dendrobium nobile
    • Ye Ci Zhao W. New alloaromadendrane, cadinene and cyclocopacamphane type sesquiterpene derivatives and bibenzyls from Dendrobium nobile. Planta Medica 2002; 68: 723-9
    • (2002) Planta Medica , vol.68 , pp. 723-729
    • Ye, Ci.1    Zhao, W.2
  • 9
    • 0032475892 scopus 로고    scopus 로고
    • Enhancement and inhibition of snake venom phosphodiesterase activity by lysophospholipids
    • Mamillapalli R, Haimovitz R, Ohad M, Shinitzky M. Enhancement and inhibition of snake venom phosphodiesterase activity by lysophospholipids. FEBS Lett 1998; 436: 256-8
    • (1998) FEBS Lett , vol.436 , pp. 256-258
    • Mamillapalli, R.1    Haimovitz, R.2    Ohad, M.3    Shinitzky, M.4
  • 10
    • 0001281157 scopus 로고
    • Studies on polynucleotides
    • Razzell WE, Khorana HG. Studies on polynucleotides. J Biol Chem 1959; 234: 2105-13
    • (1959) J Biol Chem , vol.234 , pp. 2105-2113
    • Razzell, W.E.1    Khorana, H.G.2
  • 11
    • 0028181191 scopus 로고
    • Alkaline phosphodiesterase 1 release from eucaryotic plasma membranes by phosphatidylinositol-specitic phospholipase C-IV. The release from Cacia porcellus organs
    • Nakabayashi T, Matsuoka Y, Ikezawa H, Kimura Y. Alkaline phosphodiesterase 1 release from eucaryotic plasma membranes by phosphatidylinositol-specitic phospholipase C-IV. The release from Cacia porcellus organs. Int J Biochem 1994; 26: 171-9
    • (1994) Int J Biochem , vol.26 , pp. 171-179
    • Nakabayashi, T.1    Matsuoka, Y.2    Ikezawa, H.3    Kimura, Y.4
  • 12
    • 0032472247 scopus 로고    scopus 로고
    • Glycine-enhanced inhibition of rat liver nucleotide pyrophosphatase/ phosphodiesterase-1 by EDTA: A full account of the reported inhibition by commercial preparations of acidic fibroblast growth factor (FGF-1)
    • Gomez JL, Costas MJ, Ribeiro JM, Fernandez A, Romero A, Avalos M, Cameselle JC. Glycine-enhanced inhibition of rat liver nucleotide pyrophosphatase/phosphodiesterase-1 by EDTA: A full account of the reported inhibition by commercial preparations of acidic fibroblast growth factor (FGF-1). FEBS Lett 1998; 421: 77-9
    • (1998) FEBS Lett , vol.421 , pp. 77-79
    • Gomez, J.L.1    Costas, M.J.2    Ribeiro, J.M.3    Fernandez, A.4    Romero, A.5    Avalos, M.6    Cameselle, J.C.7
  • 14
    • 11944249405 scopus 로고    scopus 로고
    • Enzyme assay of thymidine phosphorylase. 1979. US Patent 4,178.212; 1979 (Burroughs, Wellcome Co., Research Triangle Park, NC)
    • Krenitsky TA, Bushby SRM. Enzyme assay of thymidine phosphorylase. 1979. US Patent 4,178.212; 1979 (Burroughs, Wellcome Co., Research Triangle Park, NC)
    • Krenitsky, T.A.1    Bushby, S.R.M.2
  • 15
    • 0028888275 scopus 로고
    • Hydroxybenzoic acids from Boreava orientalis
    • Sakushima A, Coskun M, Maoka T. Hydroxybenzoic acids from Boreava orientalis. Phytochemistry 1995; 40: 257-61
    • (1995) Phytochemistry , vol.40 , pp. 257-261
    • Sakushima, A.1    Coskun, M.2    Maoka, T.3
  • 19
    • 0024459370 scopus 로고
    • Competitive inhibition of Klebsiella aerogenes urease
    • Todd MJ, Hausinger RP. Competitive inhibition of Klebsiella aerogenes urease. J Biol Chem 1989; 264: 15835-42
    • (1989) J Biol Chem , vol.264 , pp. 15835-15842
    • Todd, M.J.1    Hausinger, R.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.