메뉴 건너뛰기




Volumn 2, Issue 4, 2005, Pages 511-519

Structural proteomics in drug discovery

Author keywords

Automated crystallization; Drug design; High throughput methods; Protein crystallography; Protein expression; Structural genomics

Indexed keywords

CLONING; DRUG DESIGN; GENOMICS; HIGH THROUGHPUT SCREENING; PHARMACOPHORE; PROTEIN EXPRESSION; PROTEIN STRUCTURE; PROTEOMICS; REVIEW; X RAY CRYSTALLOGRAPHY;

EID: 23744472649     PISSN: 14789450     EISSN: None     Source Type: Journal    
DOI: 10.1586/14789450.2.4.511     Document Type: Review
Times cited : (3)

References (59)
  • 1
    • 0028846226 scopus 로고
    • Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme
    • Kim EE, Baker CT, Dwyer MD et al. Crystal structure of HIV-1 protease in complex with VX-478, a potent and orally bioavailable inhibitor of the enzyme. J. Am. Chem. Soc. 117, 1181-1182 (1995).
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1181-1182
    • Kim, E.E.1    Baker, C.T.2    Dwyer, M.D.3
  • 2
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein M, Wu WY, Kok GB et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363(6428), 418-423 (1993).
    • (1993) Nature , vol.363 , Issue.6428 , pp. 418-423
    • Von Itzstein, M.1    Wu, W.Y.2    Kok, G.B.3
  • 3
    • 0031048319 scopus 로고    scopus 로고
    • Influenzae neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active sight: Design, synthesis and structural analysis of carbocyclic sialic acid analogues with potent anti-influenzae activity
    • Kim CU, Lew W, Williams MA et al. Influenzae neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active sight: design, synthesis and structural analysis of carbocyclic sialic acid analogues with potent anti-influenzae activity. J. Am. Chem. Soc. 119, 681-690 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3
  • 4
    • 14244271957 scopus 로고    scopus 로고
    • Parallel cloning, expression, purification and crystallization of human proteins for structural genomics
    • Ding HT, Ren H, Chen Q et al. Parallel cloning, expression, purification and crystallization of human proteins for structural genomics. Acta Crystallogr. D Biol. Crystallogr. 58(Pt 12), 2102-2108 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , Issue.PART 12 , pp. 2102-2108
    • Ding, H.T.1    Ren, H.2    Chen, Q.3
  • 5
    • 0033768325 scopus 로고    scopus 로고
    • Protein production: Feeding the crystallographers and NMR spectroscopists
    • Edwards AM, Arrowsmith CH, Christendat D et al. Protein production: feeding the crystallographers and NMR spectroscopists. Nature Struct. Biol. 7(Suppl.), 970-972 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 970-972
    • Edwards, A.M.1    Arrowsmith, C.H.2    Christendat, D.3
  • 7
    • 0035665932 scopus 로고    scopus 로고
    • FLEXGene repository: From sequenced genomes to gene repositories for high-throughput functional biology and proteomics
    • Brizuela L, Braun P, LaBaer J. FLEXGene repository: from sequenced genomes to gene repositories for high-throughput functional biology and proteomics. Mol. Biochem. Parasitol. 118(2), 155-165 (2001).
    • (2001) Mol. Biochem. Parasitol. , vol.118 , Issue.2 , pp. 155-165
    • Brizuela, L.1    Braun, P.2    LaBaer, J.3
  • 8
    • 0036415243 scopus 로고    scopus 로고
    • A micro-scale process for high-throughput expression of cDNAs in the yeast Saccharomyces cerevisiae
    • Holz C, Hesse O, Bolotina N, Stahl U, Lang C. A micro-scale process for high-throughput expression of cDNAs in the yeast Saccharomyces cerevisiae. Protein Expr. Purif. 25(3), 372-378 (2002).
    • (2002) Protein Expr. Purif. , vol.25 , Issue.3 , pp. 372-378
    • Holz, C.1    Hesse, O.2    Bolotina, N.3    Stahl, U.4    Lang, C.5
  • 9
    • 0034957669 scopus 로고    scopus 로고
    • High-throughput proteomics: Protein expression and purification in the postgenomic world
    • Lesley SA. High-throughput proteomics: protein expression and purification in the postgenomic world. Protein Expr. Purif. 22(2), 159-164 (2001).
    • (2001) Protein Expr. Purif. , vol.22 , Issue.2 , pp. 159-164
    • Lesley, S.A.1
  • 10
    • 0024330605 scopus 로고
    • Multiwavelength anomalous diffraction as a direct phasing vehicle in macromolecular crystallography
    • Hendrickson WA, Horton JR, Murthy HM, Pahler A, Smith JL. Multiwavelength anomalous diffraction as a direct phasing vehicle in macromolecular crystallography. Basic Life Sci. 51, 317-324 (1989).
    • (1989) Basic Life Sci. , vol.51 , pp. 317-324
    • Hendrickson, W.A.1    Horton, J.R.2    Murthy, H.M.3    Pahler, A.4    Smith, J.L.5
  • 11
    • 0025262173 scopus 로고
    • Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): A vehicle for direct determination of three-dimensional structure
    • Hendrickson WA, Horton JR, LeMaster DM. Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure. EMBO J. 9(5), 1665-1672 (1990)
    • (1990) EMBO J. , vol.9 , Issue.5 , pp. 1665-1672
    • Hendrickson, W.A.1    Horton, J.R.2    LeMaster, D.M.3
  • 12
    • 0033213464 scopus 로고    scopus 로고
    • Cool data: Quantity and quality
    • Garman E. Cool data: quantity AND quality. Acta Crystallogr. D Biol. Crystallogr. 55(Pt 10), 1641-1653 (1999).
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , Issue.PART 10 , pp. 1641-1653
    • Garman, E.1
  • 13
    • 0036795668 scopus 로고    scopus 로고
    • The TB structural genomics consortium crystallization facility: Towards automation from protein to electron density
    • Rupp B, Segelke BW, Krupka HI et al. The TB structural genomics consortium crystallization facility: towards automation from protein to electron density. Acta Crystallogr. D Biol. Crystallogr. 58(Pt 10 Pt 1), 1514-1518 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , Issue.PART 10 AND PART 1 , pp. 1514-1518
    • Rupp, B.1    Segelke, B.W.2    Krupka, H.I.3
  • 14
    • 0036793459 scopus 로고    scopus 로고
    • Automated mounting, centering and screening of crystals for high-throughput protein crystallography
    • Karain WI, Bourenkov GP, Blume H, Bartunik HD. Automated mounting, centering and screening of crystals for high-throughput protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 58(Pt 10 Pt 1), 1519-1522 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , Issue.PART 10 AND PART 1 , pp. 1519-1522
    • Karain, W.I.1    Bourenkov, G.P.2    Blume, H.3    Bartunik, H.D.4
  • 15
    • 0034476897 scopus 로고    scopus 로고
    • Automated crystal mounting and data collection for protein crystallography
    • Muchmore SW, Olson J, Jones R et al. Automated crystal mounting and data collection for protein crystallography. Structure Fold Des. 8(12), R243-R246 (2000).
    • (2000) Structure Fold Des. , vol.8 , Issue.12
    • Muchmore, S.W.1    Olson, J.2    Jones, R.3
  • 16
    • 0033762983 scopus 로고    scopus 로고
    • Current state of automated crystallographic data analysis
    • Lamzin VS, Perrakis A. Current state of automated crystallographic data analysis. Nature Struct. Biol. 7(Suppl.), 978-981 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , Issue.SUPPL. , pp. 978-981
    • Lamzin, V.S.1    Perrakis, A.2
  • 17
    • 0032806795 scopus 로고    scopus 로고
    • A database method for automated map interpretation in protein crystallography
    • Diller DJ, Redinbo MR, Pohl E, Hol WG. A database method for automated map interpretation in protein crystallography. Proteins 36(4), 526-541 (1999).
    • (1999) Proteins , vol.36 , Issue.4 , pp. 526-541
    • Diller, D.J.1    Redinbo, M.R.2    Pohl, E.3    Hol, W.G.4
  • 19
    • 0036593788 scopus 로고    scopus 로고
    • High-throughput protein crystallography
    • Yasutake Y, Yao M, Tanaka I. High-throughput protein crystallography. Tanpakushitsu Kakusan Koso 47(8 Suppl.), 1033-1037 (2002).
    • (2002) Tanpakushitsu Kakusan Koso , vol.47 , Issue.8 SUPPL. , pp. 1033-1037
    • Yasutake, Y.1    Yao, M.2    Tanaka, I.3
  • 20
    • 0036594206 scopus 로고    scopus 로고
    • Development of high-throughput automatic protein crystallization and observation system
    • Sugahara M, Miyano M. Development of high-throughput automatic protein crystallization and observation system. Tanpakushitsu Kakusan Koso 47(8 Suppl.), 1026-1032 (2002).
    • (2002) Tanpakushitsu Kakusan Koso , vol.47 , Issue.8 SUPPL. , pp. 1026-1032
    • Sugahara, M.1    Miyano, M.2
  • 21
    • 0036462475 scopus 로고    scopus 로고
    • High-throughput crystallization and structure determination in drug discovery
    • Stewart L, Clark R, Behnke C. High-throughput crystallization and structure determination in drug discovery. Drug Discov. Today 7(3), 187-196 (2002).
    • (2002) Drug Discov. Today , vol.7 , Issue.3 , pp. 187-196
    • Stewart, L.1    Clark, R.2    Behnke, C.3
  • 22
    • 0035919686 scopus 로고    scopus 로고
    • Tech.Sight. Industrializing structural biology
    • Stevens RC, Wilson IA. Tech.Sight. Industrializing structural biology. Science 293(5529), 519-520 (2001).
    • (2001) Science , vol.293 , Issue.5529 , pp. 519-520
    • Stevens, R.C.1    Wilson, I.A.2
  • 23
    • 0033794367 scopus 로고    scopus 로고
    • High-throughput protein crystallization
    • Stevens RC. High-throughput protein crystallization. Curr. Opin. Struct. Biol. 10(5), 558-563 (2000).
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , Issue.5 , pp. 558-563
    • Stevens, R.C.1
  • 24
    • 0036791908 scopus 로고    scopus 로고
    • Structural proteomics: The potential of high-throughput structure determination
    • Schmid MB. Structural proteomics: the potential of high-throughput structure determination. Trends Microbiol. 10(10 Suppl.), S27-S31 (2002).
    • (2002) Trends Microbiol. , vol.10 , Issue.10 SUPPL.
    • Schmid, M.B.1
  • 25
    • 0036804362 scopus 로고    scopus 로고
    • The genesis of high-throughput structure-based drug discovery using protein crystallography
    • Kuhn P, Wilson K, Patch MG, Stevens RC. The genesis of high-throughput structure-based drug discovery using protein crystallography. Curr. Opin. Chem. Biol. 6(5), 704-710 (2002).
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.5 , pp. 704-710
    • Kuhn, P.1    Wilson, K.2    Patch, M.G.3    Stevens, R.C.4
  • 26
    • 0036793499 scopus 로고    scopus 로고
    • The high-speed Hydra-Plus-One system for automated high-throughput protein crystallography
    • Krupka HI, Rupp B, Segelke BW et al. The high-speed Hydra-Plus-One system for automated high-throughput protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 58(Pt 10 Pt 1), 1523-1526 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , Issue.PART 10 AND PART 1 , pp. 1523-1526
    • Krupka, H.I.1    Rupp, B.2    Segelke, B.W.3
  • 27
    • 0036589881 scopus 로고    scopus 로고
    • Structural genomics: Bridging functional genomics and structure-based drug design
    • Buchanan SG. Structural genomics: bridging functional genomics and structure-based drug design. Curr. Opin. Drug Discov. Devel. 5(3), 367-381 (2002).
    • (2002) Curr. Opin. Drug Discov. Devel. , vol.5 , Issue.3 , pp. 367-381
    • Buchanan, S.G.1
  • 29
    • 0036051992 scopus 로고    scopus 로고
    • High-throughput crystallography for lead discovery in drug design
    • Blundell TL, Jhoti H, Abell C. High-throughput crystallography for lead discovery in drug design. Nature Rev. Drug Discov. 1(1), 45-54 (2002).
    • (2002) Nature Rev. Drug Discov. , vol.1 , Issue.1 , pp. 45-54
    • Blundell, T.L.1    Jhoti, H.2    Abell, C.3
  • 30
    • 11844260128 scopus 로고    scopus 로고
    • Life in the fast lane for protein crystallization and x-ray crystallography
    • Pusey ML, Liu ZJ, Tempel W et al. Life in the fast lane for protein crystallization and x-ray crystallography. Prog. Biophys. Mol. Biol. 88(3), 359-386 (2005).
    • (2005) Prog. Biophys. Mol. Biol. , vol.88 , Issue.3 , pp. 359-386
    • Pusey, M.L.1    Liu, Z.J.2    Tempel, W.3
  • 31
    • 0033732564 scopus 로고    scopus 로고
    • GATEWAY recombinational cloning: Application to the cloning of large numbers of open reading frames or ORFeomes
    • Walhout AJ, Temple GF, Brasch MA et al. GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes. Methods Enzymol. 328, 575-592 (2000).
    • (2000) Methods Enzymol. , vol.328 , pp. 575-592
    • Walhout, A.J.1    Temple, G.F.2    Brasch, M.A.3
  • 32
    • 0032923248 scopus 로고    scopus 로고
    • Genome-scale cloning and expression of individual open reading frames using topoisomerase 1-mediated ligation
    • Heyman JA, Cornthwaite J, Foncerada L et al. Genome-scale cloning and expression of individual open reading frames using topoisomerase 1-mediated ligation. Genome Res. 9(4), 383-392 (1999).
    • (1999) Genome Res. , vol.9 , Issue.4 , pp. 383-392
    • Heyman, J.A.1    Cornthwaite, J.2    Foncerada, L.3
  • 33
    • 0347753417 scopus 로고    scopus 로고
    • Evidence for high specificity and efficiency of multiple recombination signals in mixed DNA cloning by the Multisite Gateway system
    • Sasaki Y, Sone T, Yoshida S et al. Evidence for high specificity and efficiency of multiple recombination signals in mixed DNA cloning by the Multisite Gateway system. J. Biotechnol. 107(3), 233-243 (2004).
    • (2004) J. Biotechnol. , vol.107 , Issue.3 , pp. 233-243
    • Sasaki, Y.1    Sone, T.2    Yoshida, S.3
  • 34
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher KP, Lee AT, Rees DC. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296(5570), 1091-1098 (2002). Demonstrates the value of exploiting diversity of genomic information for tackling challenging targets for protein crystallography. The authors cloned 28 distinct and diverse ATP transporters from different species that led to solving the structure of the BtuCD transport complex.
    • (2002) Science , vol.296 , Issue.5570 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 35
    • 0038384417 scopus 로고    scopus 로고
    • Shotgun crystallization strategy for structural genomics: An optimized two-tiered crystallization screen against the Thermotoga maritima proteome
    • Page R, Grzechnik SK, Canaves JM et al. Shotgun crystallization strategy for structural genomics: an optimized two-tiered crystallization screen against the Thermotoga maritima proteome. Acta Crystallogr. D Biol. Crystallogr. 59(Pt 6), 1028-1037 (2003).
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , Issue.PART 6 , pp. 1028-1037
    • Page, R.1    Grzechnik, S.K.2    Canaves, J.M.3
  • 36
    • 3543109683 scopus 로고    scopus 로고
    • Establishing a versatile fermentation and purification procedure for human proteins expressed in the yeasts Saccharomyces cerevisiae and Pichia pastoris for structural genomics
    • Prinz B, Schultchen J, Rydzewski R et al. Establishing a versatile fermentation and purification procedure for human proteins expressed in the yeasts Saccharomyces cerevisiae and Pichia pastoris for structural genomics. J. Struct. Funct. Genomics 5(1-2), 29-44 (2004).
    • (2004) J. Struct. Funct. Genomics , vol.5 , Issue.1-2 , pp. 29-44
    • Prinz, B.1    Schultchen, J.2    Rydzewski, R.3
  • 37
    • 0030700315 scopus 로고    scopus 로고
    • Baculoviruses as expression vectors
    • Possee RD. Baculoviruses as expression vectors. Curr. Opin. Biotechnol. 8(5), 569-572 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , Issue.5 , pp. 569-572
    • Possee, R.D.1
  • 38
    • 3543074650 scopus 로고    scopus 로고
    • Towards higher-throughput membrane protein production for structural genomics initiatives
    • Laible PD, Scott HN, Henry L, Hanson DK. Towards higher-throughput membrane protein production for structural genomics initiatives. J. Struct. Funct. Genomics 5(1-2), 167-172 (2004). Describes an attempt to overcome limitations in production of integral membrane proteins by using a bacterial species that naturally has relatively large quantities of (internal) membranes. Although the approaches for protein production and purification are clearly not high throughput, the reported yields are impressive.
    • (2004) J. Struct. Funct. Genomics , vol.5 , Issue.1-2 , pp. 167-172
    • Laible, P.D.1    Scott, H.N.2    Henry, L.3    Hanson, D.K.4
  • 39
    • 33645206405 scopus 로고    scopus 로고
    • Genome wide analysis of the response to expression of a foreign outer membrane protein
    • In Press
    • Kolodka D, Hoang TT, Surette M, Schryvers AB. Genome wide analysis of the response to expression of a foreign outer membrane protein. Mol. Microbiol. (2005) (In Press).
    • (2005) Mol. Microbiol.
    • Kolodka, D.1    Hoang, T.T.2    Surette, M.3    Schryvers, A.B.4
  • 40
    • 0001434101 scopus 로고
    • Crystallizing proteins - A rational approach?
    • D 'Arty A. Crystallizing proteins - a rational approach? Acta Crystallogr. D Biol. Crystallogr. 50(Pt 4), 469-471 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , Issue.PART 4 , pp. 469-471
    • D'Arty, A.1
  • 41
    • 0037305599 scopus 로고    scopus 로고
    • Protein expression systems for structural genomics and proteomics
    • Yokoyama S. Protein expression systems for structural genomics and proteomics. Curr. Opin. Chem. Biol. 7(1), 39-43 (2003).
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , Issue.1 , pp. 39-43
    • Yokoyama, S.1
  • 42
    • 0036713170 scopus 로고    scopus 로고
    • Engineering soluble proteins for structural genomics
    • Pedelacq JD, Piltch E, Liong EC et al. Engineering soluble proteins for structural genomics. Nature Biotechnol. 20(9), 927-932 (2002).
    • (2002) Nature Biotechnol. , vol.20 , Issue.9 , pp. 927-932
    • Pedelacq, J.D.1    Piltch, E.2    Liong, E.C.3
  • 43
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous S, Terwilliger TC, Waldo GS. Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nature Biotechnol. 23(1), 102-107 (2005). Description of a system for detection of solubility of expressed foreign proteins. The system involves fusing a small 15-mer peptide fragment of green fluorescent protein (GFP) to the C-terminus of the protein. The GFP subfragment forms a functional GFP molecule, with the remainder of the protein expressed separately. This system has the advantage that the tag does not influence the solubility of the foreign protein.
    • (2005) Nature Biotechnol. , vol.23 , Issue.1 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 44
    • 1842621078 scopus 로고    scopus 로고
    • The cost and value of three-dimensional protein structure
    • Stevens RC. The cost and value of three-dimensional protein structure. Drug Disc. World 4, 35-48 (2003).
    • (2003) Drug Disc. World , vol.4 , pp. 35-48
    • Stevens, R.C.1
  • 45
    • 18344375268 scopus 로고    scopus 로고
    • An approach to rapid protein crystallization using nanodroplets
    • Santarsiero BD, Yegian DT, Lee CC et al. An approach to rapid protein crystallization using nanodroplets. J. Applied Crystallog. 35, 278-281 (2002).
    • (2002) J. Applied Crystallog. , vol.35 , pp. 278-281
    • Santarsiero, B.D.1    Yegian, D.T.2    Lee, C.C.3
  • 46
    • 0037394499 scopus 로고    scopus 로고
    • A fully integrated protein crystallization platform for small-molecule drug discovery
    • Hosfield D, Palan J, Hilgers M et al. A fully integrated protein crystallization platform for small-molecule drug discovery. J. Struct. Biol. 142(1), 207-217 (2003).
    • (2003) J. Struct. Biol. , vol.142 , Issue.1 , pp. 207-217
    • Hosfield, D.1    Palan, J.2    Hilgers, M.3
  • 47
    • 0001011919 scopus 로고    scopus 로고
    • High-throughput Xrya crystallography for structure-based drug design
    • Goodwill KE, Tennant MG, Stevens RC. High-throughput Xrya crystallography for structure-based drug design. Drug Discov. Today 6, S113-S118 (2001).
    • (2001) Drug Discov. Today , vol.6
    • Goodwill, K.E.1    Tennant, M.G.2    Stevens, R.C.3
  • 48
    • 13844308684 scopus 로고    scopus 로고
    • Reduction in diffuso-convective disturbances in nanovolume crystallization experiments
    • Carter DC, Rhodes P, McRee DE et al. Reduction in diffuso-convective disturbances in nanovolume crystallization experiments. J. Applied Crystallog. 38, 87-90 (2005).
    • (2005) J. Applied Crystallog. , vol.38 , pp. 87-90
    • Carter, D.C.1    Rhodes, P.2    McRee, D.E.3
  • 49
    • 0037168508 scopus 로고    scopus 로고
    • A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion
    • Hansen CL, Skordalakes E, Berger JM, Quake SR. A robust and scalable microfluidic metering method that allows protein crystal growth by free interface diffusion. Proc. Natl Acad. Sci. USA 99(26), 16531-16536 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.26 , pp. 16531-16536
    • Hansen, C.L.1    Skordalakes, E.2    Berger, J.M.3    Quake, S.R.4
  • 50
    • 0037131390 scopus 로고    scopus 로고
    • Microfluidic large-scale integration
    • Thorsen T, Maerkl SJ, Quake SR. Microfluidic large-scale integration. Science 298(5593), 580-584 (2002).
    • (2002) Science , vol.298 , Issue.5593 , pp. 580-584
    • Thorsen, T.1    Maerkl, S.J.2    Quake, S.R.3
  • 53
    • 11144357937 scopus 로고    scopus 로고
    • Automated sample mounting and alignment system for biological crystallography at a synchrotron source
    • Snell G, Cork C, Nordmeyer R et al. Automated sample mounting and alignment system for biological crystallography at a synchrotron source. Structure (Camb.) 12(4), 537-545 (2004).
    • (2004) Structure (Camb.) , vol.12 , Issue.4 , pp. 537-545
    • Snell, G.1    Cork, C.2    Nordmeyer, R.3
  • 54
    • 0038581953 scopus 로고
    • A probability representation for phase information from multiwavelength anomalous dispersion
    • Pahler A, Smith JL, Hendrickson WA. A probability representation for phase information from multiwavelength anomalous dispersion. Acta Crystallogr. A. 46(Pt 7), 537-540 (1990).
    • (1990) Acta Crystallogr. A , vol.46 , Issue.PART 7 , pp. 537-540
    • Pahler, A.1    Smith, J.L.2    Hendrickson, W.A.3
  • 55
    • 0035157217 scopus 로고    scopus 로고
    • Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II
    • Bushnell DA, Cramer P, Kornberg RD. Selenomethionine incorporation in Saccharomyces cerevisiae RNA polymerase II. Structure (Camb.) 9(1), R11-R14 (2001).
    • (2001) Structure (Camb.) , vol.9 , Issue.1
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 57
    • 0033787344 scopus 로고    scopus 로고
    • Science, art and drug discovery: A personal perspective
    • Campbell SF. Science, art and drug discovery: a personal perspective. Clin. Sci. (Lond.) 99(4), 255-260 (2000).
    • (2000) Clin. Sci. (Lond.) , vol.99 , Issue.4 , pp. 255-260
    • Campbell, S.F.1
  • 58
    • 20844437061 scopus 로고    scopus 로고
    • A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design
    • Card GL, Blasdel L, England BP et al. A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nature Biotechnol. 23(2), 201-207 (2005). Excellent example of the application of fragment-based screening to generate nanomolar lead compounds against phosphodiesterase type IV from a starting pool of 316 fragments and subsequent synthesis of 21 additional compounds.
    • (2005) Nature Biotechnol. , vol.23 , Issue.2 , pp. 201-207
    • Card, G.L.1    Blasdel, L.2    England, B.P.3
  • 59
    • 0033773899 scopus 로고    scopus 로고
    • Discovering novel ligands for macromolecules using x-ray crystallographic screening
    • Nienaber VL, Richardson PL, Klighofer V et al. Discovering novel ligands for macromolecules using x-ray crystallographic screening. Nature Biotechnol. 18(10), 1105-1108 (2000).
    • (2000) Nature Biotechnol. , vol.18 , Issue.10 , pp. 1105-1108
    • Nienaber, V.L.1    Richardson, P.L.2    Klighofer, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.