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Volumn 270, Issue 19, 2003, Pages 3939-3945

Protein farnesyltransferase inhibitors interfere with farnesyl diphosphate binding by rubber transferase

Author keywords

Chaetomellic acid A; Hevea brasiliensis; Hydroxyfarnesylphosphonic acid; Parthenium argentatum

Indexed keywords

ALPHA HYDROXYFARNESYLPHOSPHONIC ACID; DIMETHYLALLYLTRANSFERASE; FARNESYL DIPHOSPHATE; ISOPENTENYL DIPHOSPHATE; PROTEIN FARNESYLTRANSFERASE INHIBITOR;

EID: 0141704105     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03775.x     Document Type: Article
Times cited : (16)

References (21)
  • 1
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • Cornish, K. (2001) Similarities and differences in rubber biochemistry among plant species. Phytochemistry 57, 1123-1134.
    • (2001) Phytochemistry , vol.57 , pp. 1123-1134
    • Cornish, K.1
  • 2
    • 0141639466 scopus 로고
    • Enzymatic synthesis of rubber from mevalonic acid
    • Park, R.B. & Bonner, J. (1958) Enzymatic synthesis of rubber from mevalonic acid. J. Biol. Chem. 233, 340-343.
    • (1958) J. Biol. Chem. , vol.233 , pp. 340-343
    • Park, R.B.1    Bonner, J.2
  • 3
    • 0004241729 scopus 로고
    • US Government Research Report AD-601729
    • Berndt, J. (1963) The Biosynthesis of Rubber. pp 1-22. US Government Research Report AD-601729.
    • (1963) The Biosynthesis of Rubber , pp. 1-22
    • Berndt, J.1
  • 4
    • 0001514540 scopus 로고
    • Biochemical problems of rubber synthesis
    • Lynen, F. (1969) Biochemical problems of rubber synthesis. J. Rubber Res. Inst Malaya 21, 389-406.
    • (1969) J. Rubber Res. Inst Malaya , vol.21 , pp. 389-406
    • Lynen, F.1
  • 5
    • 84984233737 scopus 로고
    • New aspects of rubber biosynthesis
    • Archer, B.L. & Audley, B.G. (1987) New aspects of rubber biosynthesis. Bot. J. Linnean Soc. 94, 181-196.
    • (1987) Bot. J. Linnean Soc. , vol.94 , pp. 181-196
    • Archer, B.L.1    Audley, B.G.2
  • 8
    • 0029833497 scopus 로고    scopus 로고
    • Synthesis of protein farnesyltransferase and protein geranylgeranyltransferase inhibitors: Rapid access to chaetomellic acid A and its analogs
    • Ratemi, E.S., Dolence, J.M., Poulter, C.D. & Vederas, J.C. (1996) Synthesis of protein farnesyltransferase and protein geranylgeranyltransferase inhibitors: Rapid access to chaetomellic acid A and its analogs. J. Org. Chem. 61, 6296-6301.
    • (1996) J. Org. Chem. , vol.61 , pp. 6296-6301
    • Ratemi, E.S.1    Dolence, J.M.2    Poulter, C.D.3    Vederas, J.C.4
  • 10
    • 0001346415 scopus 로고
    • Rubber transferase activity in rubber particles of guayule
    • Cornish, K. & Backhaus, R.A. (1990) Rubber transferase activity in rubber particles of guayule. Phytochemistry 29, 3809-3813.
    • (1990) Phytochemistry , vol.29 , pp. 3809-3813
    • Cornish, K.1    Backhaus, R.A.2
  • 11
    • 0001035422 scopus 로고
    • A protein from Ficus elastica rubber particles is related to proteins from Hevea brasiliensis and Parthenium argentatum
    • Siler, D.J. & Cornish, K. (1993) A protein from Ficus elastica rubber particles is related to proteins from Hevea brasiliensis and Parthenium argentatum. Phytochemistry 32, 1097-1102.
    • (1993) Phytochemistry , vol.32 , pp. 1097-1102
    • Siler, D.J.1    Cornish, K.2
  • 12
    • 0030913491 scopus 로고    scopus 로고
    • Stabilisation of particle integrity and particle bound cis-prenyltransferase activity in stored, purified rubber particles
    • Cornish, K. & Bartlett, D.L. (1997) Stabilisation of particle integrity and particle bound cis-prenyltransferase activity in stored, purified rubber particles. Phytochem. Anal. 8, 130-134.
    • (1997) Phytochem. Anal. , vol.8 , pp. 130-134
    • Cornish, K.1    Bartlett, D.L.2
  • 13
    • 0034502667 scopus 로고    scopus 로고
    • Multiwell filtration system results in rapid, high-throughput rubber transferase microassay
    • Mau, C.J.D., Scott, D.J. & Cornish, K. (2000) Multiwell filtration system results in rapid, high-throughput rubber transferase microassay. Phytochem. Anal. 11, 356-361.
    • (2000) Phytochem. Anal. , vol.11 , pp. 356-361
    • Mau, C.J.D.1    Scott, D.J.2    Cornish, K.3
  • 14
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York, NY
    • Segel, I. (1975). Enzyme Kinetics. John Wiley and Sons, New York, NY.
    • (1975) Enzyme Kinetics
    • Segel, I.1
  • 15
    • 0035051051 scopus 로고    scopus 로고
    • Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species
    • Cornish, K. (2001) Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species. Nat. Prod. Report 18, 182-189.
    • (2001) Nat. Prod. Report , vol.18 , pp. 182-189
    • Cornish, K.1
  • 16
    • 0032903712 scopus 로고    scopus 로고
    • Regulation of initiation and polymer molecular weight of cis-1,4-polyisoprene synthesized in vitro by particles isolated from Parthenium argentatum (Gray)
    • Castillón, J. & Cornish, K. (1999) Regulation of initiation and polymer molecular weight of cis-1,4-polyisoprene synthesized in vitro by particles isolated from Parthenium argentatum (Gray). Phytochemistry 51, 43-51.
    • (1999) Phytochemistry , vol.51 , pp. 43-51
    • Castillón, J.1    Cornish, K.2
  • 17
    • 0034578097 scopus 로고    scopus 로고
    • Rubber molecular weight regulation in vitro, in plant species that produce high and low molecular weights in vivo
    • Cornish, K., Castillón, J. & Scott, D.J. (2000) Rubber molecular weight regulation in vitro, in plant species that produce high and low molecular weights in vivo. Biomacromolecules 1, 632-641.
    • (2000) Biomacromolecules , vol.1 , pp. 632-641
    • Cornish, K.1    Castillón, J.2    Scott, D.J.3
  • 18
    • 0033406808 scopus 로고    scopus 로고
    • Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane
    • Cornish, K., Wood, D.F. & Windle, J.J. (1999) Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane. Planta 210, 85-96.
    • (1999) Planta , vol.210 , pp. 85-96
    • Cornish, K.1    Wood, D.F.2    Windle, J.J.3
  • 19
    • 0035836712 scopus 로고    scopus 로고
    • Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
    • Fujihashi, M., Zhang, Y.-W., Higuchi, Y., Li, X.-Y., Koyama, T. & Miki, K. (2001) Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl Acad Sci. USA 98, 4337-4342.
    • (2001) Proc. Natl Acad Sci. USA , vol.98 , pp. 4337-4342
    • Fujihashi, M.1    Zhang, Y.-W.2    Higuchi, Y.3    Li, X.-Y.4    Koyama, T.5    Miki, K.6
  • 20
    • 0035861579 scopus 로고    scopus 로고
    • Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis
    • Ko, T.-P., Chen, Y.-K., Robinson, H., Tsai, P.-C., Gao, Y.-G., Chen, A.P.-C., Wang, A.H.-J. & Liang, P.-H. (2001) Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis. J. Biol. Chem. 276, 47474-47482.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47474-47482
    • Ko, T.-P.1    Chen, Y.-K.2    Robinson, H.3    Tsai, P.-C.4    Gao, Y.-G.5    Chen, A.P.-C.6    Wang, A.H.-J.7    Liang, P.-H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.