메뉴 건너뛰기




Volumn 34, Issue 2, 2006, Pages 205-212

Structural genomics: The ultimate approach for rational drug design

Author keywords

Crystallization; Expression; G protein coupled receptors; Purification; Structural genomics

Indexed keywords

CRYSTALLIZATION; DRUG PRODUCTS; MOLECULAR STRUCTURE; PROTEINS; PURIFICATION;

EID: 33845959766     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:34:2:205     Document Type: Conference Paper
Times cited : (13)

References (31)
  • 1
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • Blundell, T. L. (1996) Structure-based drug design. Nature 384S, 23-26.
    • (1996) Nature , vol.384 S , pp. 23-26
    • Blundell, T.L.1
  • 2
    • 0033787344 scopus 로고    scopus 로고
    • Science, art and drug discovery: A personal perspective
    • Campbell, S. F. (2000) Science, art and drug discovery: a personal perspective. Clin. Sci. 99, 255-260.
    • (2000) Clin. Sci , vol.99 , pp. 255-260
    • Campbell, S.F.1
  • 3
    • 0348227698 scopus 로고    scopus 로고
    • The impact of structure-guided drug design on clinical agents
    • Hardy, L. W. and Malikayil, A. (2003) The impact of structure-guided drug design on clinical agents. Curr. Drug. Discov. 3, 15-20.
    • (2003) Curr. Drug. Discov , vol.3 , pp. 15-20
    • Hardy, L.W.1    Malikayil, A.2
  • 4
    • 0036280264 scopus 로고    scopus 로고
    • X-ray crystallographic structure of ABT-378 (lopinavir) bound to HIV-1 protease
    • Stoll, V., Qin, W., Stewart, K. D., et al. (2002) X-ray crystallographic structure of ABT-378 (lopinavir) bound to HIV-1 protease. Bioorg. Med. Chem. 10, 2803-2806.
    • (2002) Bioorg. Med. Chem , vol.10 , pp. 2803-2806
    • Stoll, V.1    Qin, W.2    Stewart, K.D.3
  • 5
    • 0032996584 scopus 로고    scopus 로고
    • Development of neuroaminidase inhibitors as anti-influenza virus drugs
    • Varghese, J. N. (1999) Development of neuroaminidase inhibitors as anti-influenza virus drugs. Drug Dev. Res. 46, 176-196.
    • (1999) Drug Dev. Res , vol.46 , pp. 176-196
    • Varghese, J.N.1
  • 6
    • 1642377401 scopus 로고    scopus 로고
    • Max Planck Institute of Biophysics, Frankfurt, Germany
    • Michel, H. (2005) Membrane proteins of known structure. Max Planck Institute of Biophysics, Frankfurt, Germany. http://www.mpibp-frankfurt.mpg.de/ michel/public/memprotstruct.html.
    • (2005) Membrane proteins of known structure
    • Michel, H.1
  • 8
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B., and MacKinnon, R. (2005) Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 9
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • Unwin, N. (2003) Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy. FEBS Lett. 555, 91-95.
    • (2003) FEBS Lett , vol.555 , pp. 91-95
    • Unwin, N.1
  • 10
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K., Kumasaka, T., Hori, T., et al. (2000) Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745.
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1    Kumasaka, T.2    Hori, T.3
  • 11
    • 0035213854 scopus 로고    scopus 로고
    • Patent status of the therapeutically important G protein-coupled receptors. Exp. Opin. Ther. Patents 11, 1861-1887
    • Vanti, W. B., Swaminathan, S., Blevins, R., et al. (2001) Patent status of the therapeutically important G protein-coupled receptors. Exp. Opin. Ther. Patents 11, 1861-1887.
    • (2001)
    • Vanti, W.B.1    Swaminathan, S.2    Blevins, R.3
  • 12
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker, J. and Grisshammer, R. (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317, 891-899.
    • (1996) Biochem. J , vol.317 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 13
    • 0032521005 scopus 로고    scopus 로고
    • Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris
    • Weiss, H. M., Haase, W., Michel, H., and Reilander, H. (1998) Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris. Biochem. J. 330, 1137-1147.
    • (1998) Biochem. J , vol.330 , pp. 1137-1147
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 14
    • 0037450572 scopus 로고    scopus 로고
    • G protein-coupled receptor overexpression with the baculovirus-insect cell system: A tool for structural and functional studies
    • Massotte, D. (2003) G protein-coupled receptor overexpression with the baculovirus-insect cell system: a tool for structural and functional studies. Biochim. Biophys Acta 1610, 77-89.
    • (2003) Biochim. Biophys Acta , vol.1610 , pp. 77-89
    • Massotte, D.1
  • 15
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucos-aminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P. J., Callewaert, N., Contreras, R., and Khorana, H. G. (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucos-aminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acd. Sci. USA 99, 13,419-13,424.
    • (2002) Proc. Natl. Acd. Sci. USA , vol.99
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 16
    • 0037450521 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins
    • Lundstrom, K. (2003) Semliki Forest virus vectors for rapid and high-level expression of integral membrane proteins. Biochim. Biophys. Acta 1610, 90-96.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 90-96
    • Lundstrom, K.1
  • 17
    • 10744228030 scopus 로고    scopus 로고
    • Structural genomics of Mycobacterium tuberculosis: A preliminary report of progress at UCLA
    • Goulding, C. W., Perry, L. J., Anderson, D., et al. (2003) Structural genomics of Mycobacterium tuberculosis: a preliminary report of progress at UCLA. Biophys. Chem. 105, 361-370.
    • (2003) Biophys. Chem , vol.105 , pp. 361-370
    • Goulding, C.W.1    Perry, L.J.2    Anderson, D.3
  • 18
    • 0036408584 scopus 로고    scopus 로고
    • Structural genomics of "non-standard" proteins: A chance for membrane proteins?
    • Essen, L. O. (2002) Structural genomics of "non-standard" proteins: a chance for membrane proteins? Gene Funct. Dis. 3, 39-48.
    • (2002) Gene Funct. Dis , vol.3 , pp. 39-48
    • Essen, L.O.1
  • 19
    • 8544275816 scopus 로고    scopus 로고
    • Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: Maximum clustering strategy for structural genomics
    • Canaves, J. M., Page, R., Wilson, I. A., and Stevens, R. C. (2004) Protein biophysical properties that correlate with crystallization success in Thermotoga maritima: maximum clustering strategy for structural genomics. J. Mol. Biol. 344, 977-991.
    • (2004) J. Mol. Biol , vol.344 , pp. 977-991
    • Canaves, J.M.1    Page, R.2    Wilson, I.A.3    Stevens, R.C.4
  • 20
    • 0033762813 scopus 로고    scopus 로고
    • Structural genomics projects in Japan
    • Yokoyama, S., Hirota, H., Kigawa, T., et al. (2000) Structural genomics projects in Japan. Nat. Struct. Biol. 7, 943-945.
    • (2000) Nat. Struct. Biol , vol.7 , pp. 943-945
    • Yokoyama, S.1    Hirota, H.2    Kigawa, T.3
  • 21
    • 8844246397 scopus 로고    scopus 로고
    • The Paris-Sud yeast structural genomics pilot-project: From structure to function
    • Quevillon-Cheruel, S., Liger, D., Leulliot, N., et al. (2004) The Paris-Sud yeast structural genomics pilot-project: from structure to function. Biochimie 86, 617-623.
    • (2004) Biochimie , vol.86 , pp. 617-623
    • Quevillon-Cheruel, S.1    Liger, D.2    Leulliot, N.3
  • 22
    • 26444606331 scopus 로고    scopus 로고
    • Protein production and crystallization at SECSG: An overview
    • Wang, B. C., Adams, M. W., Dailey, H., et al. (2005) Protein production and crystallization at SECSG: an overview. J. Struct. Funct. Genomics 6, 233-243.
    • (2005) J. Struct. Funct. Genomics , vol.6 , pp. 233-243
    • Wang, B.C.1    Adams, M.W.2    Dailey, H.3
  • 23
    • 26244451778 scopus 로고    scopus 로고
    • Progress of structural genomics initiatives: An analysis of solved target structures
    • Todd, A. E., Marsden, R. L., Thornton, J. M., and Orengo, C. A. (2005) Progress of structural genomics initiatives: an analysis of solved target structures. J. Mol. Biol. 353, 760.
    • (2005) J. Mol. Biol , vol.353 , pp. 760
    • Todd, A.E.1    Marsden, R.L.2    Thornton, J.M.3    Orengo, C.A.4
  • 25
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji, E. R. S., Slotboom, D. -J., and Poolman, B. (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim. Biophys. Acta 1610, 97-108.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.S.1    Slotboom, D.-J.2    Poolman, B.3
  • 26
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: Purification, reconstitution, and ligand binding
    • Kiefer, H., Krieger, J., Olszewski, J. D., Von Heijne, G., Prestwich, G. D., and Breer, H. (1996) Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 35, 16,077-16,084.
    • (1996) Biochemistry , vol.35
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 27
    • 0037450517 scopus 로고    scopus 로고
    • In vitro folding of alpha-helical membrane proteins
    • Kiefer, H. (2003) In vitro folding of alpha-helical membrane proteins. Biochim. Biophys. Acta 1610, 57-62.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 57-62
    • Kiefer, H.1
  • 28
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: Conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres, J. L., Martin, A., Hullot, P., Girard, J. P., Rossi, J. C., and Parello, J. (2003) Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329, 801-814.
    • (2003) J. Mol. Biol , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 29
    • 0037518197 scopus 로고    scopus 로고
    • The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1
    • Lopez de Maturana, R., Willshaw, A., Kuntzsch, A., Rudolph, R., and Donnelly, D. (2003) The isolated N-terminal domain of the glucagon-like peptide-1 (GLP-1) receptor binds exendin peptides with much higher affinity than GLP-1. J. Biol. Chem. 278, 10,195-10,200.
    • (2003) J. Biol. Chem , vol.278
    • Lopez de Maturana, R.1    Willshaw, A.2    Kuntzsch, A.3    Rudolph, R.4    Donnelly, D.5
  • 30
    • 31044446490 scopus 로고    scopus 로고
    • Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells
    • Hassaine, G., Wagner, R., Kempf, J., et al. (2006) Semliki Forest virus vectors for overexpression of 101 G protein-coupled receptors in mammalian host cells. Protein Expr. Purif. 45, 343-351.
    • (2006) Protein Expr. Purif , vol.45 , pp. 343-351
    • Hassaine, G.1    Wagner, R.2    Kempf, J.3
  • 31
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B., Campbell, E. B., and MacKinnon, R. (2005) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903.
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.