메뉴 건너뛰기




Volumn 51, Issue 15, 2008, Pages 4571-4580

Chemical proteomics-based drug design: Target and antitarget fishing with a catechol-rhodanine privileged scaffold for NAD(P)(H) binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

CATECHOL; DIHYDRODIPICOLINATE REDUCTASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RHODANINE; SCAFFOLD PROTEIN;

EID: 49449109858     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm8002284     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 27644555675 scopus 로고    scopus 로고
    • Opinion: Anticipating change in drug development: the emerging era of translational medicine and therapeutics
    • Fitzgerald, G. A. Opinion: anticipating change in drug development: the emerging era of translational medicine and therapeutics. Nat. Rev. Drug Discovery 2005, 4, 815-818.
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 815-818
    • Fitzgerald, G.A.1
  • 3
    • 0037432765 scopus 로고    scopus 로고
    • From knowing to controlling: A path from genomics to drugs using small molecule probes
    • Strausberg, R. L.; Schreiber, S. L. From knowing to controlling: a path from genomics to drugs using small molecule probes. Science 2003, 300, 294-295.
    • (2003) Science , vol.300 , pp. 294-295
    • Strausberg, R.L.1    Schreiber, S.L.2
  • 4
    • 36049026281 scopus 로고    scopus 로고
    • Chemical genomic and proteomic methods for determining kinase inhibitor selectivity
    • Krishnamurty, R.; Maly, D. J. Chemical genomic and proteomic methods for determining kinase inhibitor selectivity. Comb. Chem. High Throughput Screening 2007, 10, 652-666.
    • (2007) Comb. Chem. High Throughput Screening , vol.10 , pp. 652-666
    • Krishnamurty, R.1    Maly, D.J.2
  • 5
  • 6
    • 35948972522 scopus 로고    scopus 로고
    • Peters, E. C.; Gray, N. S. Chemical proteomics identifies unanticipated targets of clinical kinase inhibitors. ACS Chem. Biol. 2007, 2, 661-664.
    • Peters, E. C.; Gray, N. S. Chemical proteomics identifies unanticipated targets of clinical kinase inhibitors. ACS Chem. Biol. 2007, 2, 661-664.
  • 7
    • 33751583815 scopus 로고    scopus 로고
    • Argyrou, A.; Jin, L.; Siconilfi.Baez, L.; Angeletti, R. H.; Blanchard, J. S. Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis. Biochemistry 2006, 45, 13947-13953.
    • Argyrou, A.; Jin, L.; Siconilfi.Baez, L.; Angeletti, R. H.; Blanchard, J. S. Proteome-wide profiling of isoniazid targets in Mycobacterium tuberculosis. Biochemistry 2006, 45, 13947-13953.
  • 8
    • 49449112550 scopus 로고    scopus 로고
    • A simple and fuzzy method to align and compare draggable ligand-binding sites
    • in press
    • Schalon, C.; Surgand, J. S.; Kellenberger, E.; Rognan, D. A simple and fuzzy method to align and compare draggable ligand-binding sites. Proteins, in press.
    • Proteins
    • Schalon, C.1    Surgand, J.S.2    Kellenberger, E.3    Rognan, D.4
  • 11
    • 36749018204 scopus 로고    scopus 로고
    • Privileged structures: A useful concept for the rational design of new lead drug candidates
    • Duarte, C. D.; Barreiro, E. J.; Fraga, C. A. Privileged structures: a useful concept for the rational design of new lead drug candidates. Mini-Rev. Med. Chem. 2007, 7, 1108-1119.
    • (2007) Mini-Rev. Med. Chem , vol.7 , pp. 1108-1119
    • Duarte, C.D.1    Barreiro, E.J.2    Fraga, C.A.3
  • 12
    • 33644872086 scopus 로고    scopus 로고
    • Privileged structures as leads in medicinal chemistry
    • Costantino, L.; Barlocco, D. Privileged structures as leads in medicinal chemistry. Curr. Med. Chem. 2006, 13, 65-85.
    • (2006) Curr. Med. Chem , vol.13 , pp. 65-85
    • Costantino, L.1    Barlocco, D.2
  • 13
    • 0042121318 scopus 로고    scopus 로고
    • Medicinal chemistry of target family-directed masterkeys
    • Muller, G. Medicinal chemistry of target family-directed masterkeys. Drug Discovery Today 2003, 8, 681-691.
    • (2003) Drug Discovery Today , vol.8 , pp. 681-691
    • Muller, G.1
  • 14
    • 0029894013 scopus 로고    scopus 로고
    • The properties of known drugs. 1. Molecular frameworks
    • Bemis, G. W.; Murcko, M. A. The properties of known drugs. 1. Molecular frameworks. J. Med. Chem. 1996, 39, 2887-2893.
    • (1996) J. Med. Chem , vol.39 , pp. 2887-2893
    • Bemis, G.W.1    Murcko, M.A.2
  • 16
    • 33750238670 scopus 로고    scopus 로고
    • Probing cell-division phenotype space and Polo-like kinase function using small molecules
    • Peters, U.; Cherian, J.; Kim, J. H.; Kwok, B. H.; Kapoor, T. M. Probing cell-division phenotype space and Polo-like kinase function using small molecules. Nat. Chem. Biol. 2006, 2, 618-626.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 618-626
    • Peters, U.1    Cherian, J.2    Kim, J.H.3    Kwok, B.H.4    Kapoor, T.M.5
  • 17
    • 0033011780 scopus 로고    scopus 로고
    • Molecular modeling, synthesis, and structures of N-methylated 3,5-linked pyrrolin-4-ones toward the creation of a privileged nonpeptide scaffold
    • Smith, A. B., 3rd; Favor, D. A.; Sprengeler, P. A.; Guzman, M. C.; Carroll, P. J.; Furst, G. T.; Hirschmann, R. Molecular modeling, synthesis, and structures of N-methylated 3,5-linked pyrrolin-4-ones toward the creation of a privileged nonpeptide scaffold. Bioorg. Med. Chem. 1999, 7, 9-22.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 9-22
    • Smith 3rd, A.B.1    Favor, D.A.2    Sprengeler, P.A.3    Guzman, M.C.4    Carroll, P.J.5    Furst, G.T.6    Hirschmann, R.7
  • 18
    • 34250169806 scopus 로고    scopus 로고
    • A novel bis- tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI), GRL-98065, is potent against multiple-Pl-resistant human immunodeficiency virus in vitro
    • Amano, M.; Koh, Y.; Das, D.; Li, J.; Leschenko, S.; Wang, Y. F.; Boross, P. I.; Weber, I. T.; Ghosh, A. K.; Mitsuya, H. A novel bis- tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI), GRL-98065, is potent against multiple-Pl-resistant human immunodeficiency virus in vitro. Antimicrob. Agents Chemother. 2007, 51, 2143-2155.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 2143-2155
    • Amano, M.1    Koh, Y.2    Das, D.3    Li, J.4    Leschenko, S.5    Wang, Y.F.6    Boross, P.I.7    Weber, I.T.8    Ghosh, A.K.9    Mitsuya, H.10
  • 19
    • 4243133144 scopus 로고    scopus 로고
    • Privileged structure-based combinatorial libraries targeting G protein-coupled receptors
    • Guo, T.; Hobbs, D. W. Privileged structure-based combinatorial libraries targeting G protein-coupled receptors. Assay Drug Dev. Technol. 2003, 1, 579-592.
    • (2003) Assay Drug Dev. Technol , vol.1 , pp. 579-592
    • Guo, T.1    Hobbs, D.W.2
  • 20
    • 35148898301 scopus 로고    scopus 로고
    • Hybrid approach for the design of highly affine and selective dopamine D(3) receptor ligands using privileged scaffolds of biogenic amine GPCR ligands
    • Sasse, B. C.; Mach, U. R.; Leppaenen, J.; Calmels, T.; Stark, H. Hybrid approach for the design of highly affine and selective dopamine D(3) receptor ligands using privileged scaffolds of biogenic amine GPCR ligands. Bioorg. Med. Chem. 2007, 15, 7258-7273.
    • (2007) Bioorg. Med. Chem , vol.15 , pp. 7258-7273
    • Sasse, B.C.1    Mach, U.R.2    Leppaenen, J.3    Calmels, T.4    Stark, H.5
  • 22
    • 0346881746 scopus 로고    scopus 로고
    • Genome-wide profile of oxidoreductases in viruses, prokaryotes, and eukaryotes
    • Kho, R.; Newman, J. V.; Jack, R. M.; Villar, H. O.; Hansen, M. R. Genome-wide profile of oxidoreductases in viruses, prokaryotes, and eukaryotes. J. Proteome Res. 2003, 2, 626-632.
    • (2003) J. Proteome Res , vol.2 , pp. 626-632
    • Kho, R.1    Newman, J.V.2    Jack, R.M.3    Villar, H.O.4    Hansen, M.R.5
  • 26
    • 15444374352 scopus 로고    scopus 로고
    • Poupaert, J.; Carato, P.; Colacino, E.; Yous, S. 2(3H)- Benzoxazolone and bioisosters as privileged scaffold in the design of pharmacological probes. Curr. Med. Chem. 2005, 12, 877-885.
    • Poupaert, J.; Carato, P.; Colacino, E.; Yous, S. 2(3H)- Benzoxazolone and bioisosters as "privileged scaffold" in the design of pharmacological probes. Curr. Med. Chem. 2005, 12, 877-885.
  • 29
    • 0030693983 scopus 로고    scopus 로고
    • Bolton, J. L.; Pisha, E.; Shen, L.; Krol, E. S.; Iverson, S. L.; Huang, Z.; van.Breemen, R. B.; Pezzuto, J. M. The reactivity of o-quinones which do not isomerize to quinone methides correlates with alkylcatechol-induced toxicity in human melanoma cells. Chem. Biol. Interact. 1997, 106, 133-148.
    • Bolton, J. L.; Pisha, E.; Shen, L.; Krol, E. S.; Iverson, S. L.; Huang, Z.; van.Breemen, R. B.; Pezzuto, J. M. The reactivity of o-quinones which do not isomerize to quinone methides correlates with alkylcatechol-induced toxicity in human melanoma cells. Chem. Biol. Interact. 1997, 106, 133-148.
  • 31
    • 0015755909 scopus 로고
    • Affinity chromatography of nicotinamide - adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide
    • Barry, S.; O'Carra, P. Affinity chromatography of nicotinamide - adenine dinucleotide-linked dehydrogenases on immobilized derivatives of the dinucleotide. Biochem. J. 1973, 135, 595-607.
    • (1973) Biochem. J , vol.135 , pp. 595-607
    • Barry, S.1    O'Carra, P.2
  • 32
    • 0016308522 scopus 로고
    • Simple chemical synthesis of a specific effector for the affinity chromatography of nicotinamide adenine dinucleotide phosphate-dependent dehydrogenases
    • Morelli, A.; Benatti, U. Simple chemical synthesis of a specific effector for the affinity chromatography of nicotinamide adenine dinucleotide phosphate-dependent dehydrogenases. Ital. J. Biochem. 1974, 23, 279-291.
    • (1974) Ital. J. Biochem , vol.23 , pp. 279-291
    • Morelli, A.1    Benatti, U.2
  • 33
    • 0016158151 scopus 로고
    • Affinity chromatography of nicotinamide nucleotide-dependent dehydrogenases on immobilized nucleotide derivatives
    • Trayer, I. P.; Trayer, H. R. Affinity chromatography of nicotinamide nucleotide-dependent dehydrogenases on immobilized nucleotide derivatives. Biochem. J. 1974, 141, 775-787.
    • (1974) Biochem. J , vol.141 , pp. 775-787
    • Trayer, I.P.1    Trayer, H.R.2
  • 34
    • 28544435359 scopus 로고    scopus 로고
    • Ng, E.; Schriemer, D. C. Emerging challenges in ligand discovery: new opportunities for chromatographic assay. Expert Rev. Proteomics 2005, 2, 891-900.
    • Ng, E.; Schriemer, D. C. Emerging challenges in ligand discovery: new opportunities for chromatographic assay. Expert Rev. Proteomics 2005, 2, 891-900.
  • 35
    • 0034727641 scopus 로고    scopus 로고
    • Fluorescence characterization of structural transitions at the strong actin binding motif in skeletal myosin affinity labeled at cysteine 540 with novel spectroscopic cysteaminyl mixed disulfides
    • Bertrand, R.; Derancourt, J.; Kassab, R. Fluorescence characterization of structural transitions at the strong actin binding motif in skeletal myosin affinity labeled at cysteine 540 with novel spectroscopic cysteaminyl mixed disulfides. Biochemistry 2000, 39, 14626-14637.
    • (2000) Biochemistry , vol.39 , pp. 14626-14637
    • Bertrand, R.1    Derancourt, J.2    Kassab, R.3
  • 36
    • 0030725699 scopus 로고    scopus 로고
    • Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate
    • Scapin, G.; Reddy, S. G.; Zheng, R.; Blanchard, J. S. Three-dimensional structure of Escherichia coli dihydrodipicolinate reductase in complex with NADH and the inhibitor 2,6-pyridinedicarboxylate. Biochemistry 1997, 36, 15081-15088.
    • (1997) Biochemistry , vol.36 , pp. 15081-15088
    • Scapin, G.1    Reddy, S.G.2    Zheng, R.3    Blanchard, J.S.4
  • 37
    • 34748920713 scopus 로고    scopus 로고
    • Affinity-based chemical proteomic probe for dehydrogenases: Fluorescence and visible binding assays in gels
    • Ge, X.; Sem, D. S. Affinity-based chemical proteomic probe for dehydrogenases: fluorescence and visible binding assays in gels. Anal. Biochem. 2007, 370, 171-179.
    • (2007) Anal. Biochem , vol.370 , pp. 171-179
    • Ge, X.1    Sem, D.S.2
  • 38
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow, K. T.; Cravatt, B. F. Activity-based protein profiling for the functional annotation of enzymes. Nat. Methods 2007, 4, 822-827.
    • (2007) Nat. Methods , vol.4 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 39
    • 27144510184 scopus 로고    scopus 로고
    • Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling
    • Evans, M. J.; Saghatelian, A.; Sorensen, E. J.; Cravatt, B. F. Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling. Nat. Biotechnol. 2005, 23, 1303-1307.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1303-1307
    • Evans, M.J.1    Saghatelian, A.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 40
    • 0033581124 scopus 로고    scopus 로고
    • Consensus statement. Global burden of tuberculosis: Estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project
    • Dye, C.; Scheele, S.; Dolin, P.; Pathania, V.; Raviglione, M. C. Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project. JAMA, J. Am. Med. Assoc. 1999, 282, 677-686.
    • (1999) JAMA, J. Am. Med. Assoc , vol.282 , pp. 677-686
    • Dye, C.1    Scheele, S.2    Dolin, P.3    Pathania, V.4    Raviglione, M.C.5
  • 41
    • 38449109109 scopus 로고    scopus 로고
    • Recent progress in mycobacteriology
    • Okada, M.; Kobayashi, K. Recent progress in mycobacteriology. Kekkaku 2007, 82, 783-799.
    • (2007) Kekkaku , vol.82 , pp. 783-799
    • Okada, M.1    Kobayashi, K.2
  • 42
    • 33750682661 scopus 로고    scopus 로고
    • Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy
    • Hori, T.; Ishijima, J.; Yokomizo, T.; Ago, H.; Shimizu, T.; Miyano, M. Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy. J. Biochem. 2006, 140, 457-466.
    • (2006) J. Biochem , vol.140 , pp. 457-466
    • Hori, T.1    Ishijima, J.2    Yokomizo, T.3    Ago, H.4    Shimizu, T.5    Miyano, M.6
  • 43
    • 0035834581 scopus 로고    scopus 로고
    • Identification of dual cyclooxygenase-eicosanoid oxidoreductase inhibitors: NSAIDs that inhibit PG-LX reductase/LTB(4) dehydrogenase
    • Clish, C. B.; Sun, Y. P.; Serhan, C. N. Identification of dual cyclooxygenase-eicosanoid oxidoreductase inhibitors: NSAIDs that inhibit PG-LX reductase/LTB(4) dehydrogenase. Biochem. Biophys. Res. Commun. 2001, 288, 868-874.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 868-874
    • Clish, C.B.1    Sun, Y.P.2    Serhan, C.N.3
  • 45
    • 34547662436 scopus 로고    scopus 로고
    • Pyridoxine-dependent seizures in Dutch patients: Diagnosis by elevated urinary alpha-aminoadipic semialdehyde levels
    • Bok, L. A.; Strays, E.; Willemsen, M. A.; Been, J. V.; Jakobs, C. Pyridoxine-dependent seizures in Dutch patients: diagnosis by elevated urinary alpha-aminoadipic semialdehyde levels. Arch Dis. Child. 2007, 92, 687-689.
    • (2007) Arch Dis. Child , vol.92 , pp. 687-689
    • Bok, L.A.1    Strays, E.2    Willemsen, M.A.3    Been, J.V.4    Jakobs, C.5
  • 47
    • 0018655454 scopus 로고
    • Distribution of coenzyme F420 and properties of its hvdrolytic fragments
    • Eirich, L. D.; Vogels, G. D.; Wolfe, R. S. Distribution of coenzyme F420 and properties of its hvdrolytic fragments. J. Bacteriol. 1979, 140, 20-27.
    • (1979) J. Bacteriol , vol.140 , pp. 20-27
    • Eirich, L.D.1    Vogels, G.D.2    Wolfe, R.S.3
  • 48
    • 0018114941 scopus 로고
    • Proposed structure for coenzyme F420 from Methanobacterium
    • Eirich, L. D.; Vogels, G. D.; Wolfe, R. S. Proposed structure for coenzyme F420 from Methanobacterium. Biochemistry 1978, 17, 4583-4593.
    • (1978) Biochemistry , vol.17 , pp. 4583-4593
    • Eirich, L.D.1    Vogels, G.D.2    Wolfe, R.S.3
  • 49
    • 0031923498 scopus 로고    scopus 로고
    • Molecular analysis of the gene encoding F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis
    • Purwantini, E.; Daniels, L. Molecular analysis of the gene encoding F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis. J. Bacteriol. 1998, 180, 2212-2219.
    • (1998) J. Bacteriol , vol.180 , pp. 2212-2219
    • Purwantini, E.1    Daniels, L.2
  • 50
    • 0344736963 scopus 로고    scopus 로고
    • Rapid determination of vitamin B2 secretion by bacteria growing on solid media
    • Salvetti, S.; Celandroni, F.; Ghelardi, E.; Baggiani, A.; Senesi, S. Rapid determination of vitamin B2 secretion by bacteria growing on solid media. J. Appl. Microbiol. 2003, 95, 1255-1260.
    • (2003) J. Appl. Microbiol , vol.95 , pp. 1255-1260
    • Salvetti, S.1    Celandroni, F.2    Ghelardi, E.3    Baggiani, A.4    Senesi, S.5
  • 53
    • 0036175346 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr gene within macrophages, in standing versus shaking cultures, and under low oxygen conditions
    • Purkayastha, A.; McCue, L. A.; McDonough, K. A. Identification of a Mycobacterium tuberculosis putative classical nitroreductase gene whose expression is coregulated with that of the acr gene within macrophages, in standing versus shaking cultures, and under low oxygen conditions. Infect. Immun. 2002, 70, 1518-1529.
    • (2002) Infect. Immun , vol.70 , pp. 1518-1529
    • Purkayastha, A.1    McCue, L.A.2    McDonough, K.A.3
  • 54
    • 33947369443 scopus 로고    scopus 로고
    • Macrophage-specific Mycobacterium tuberculosis genes: Identification by green fluorescent protein and kanamycin resistance selection
    • Srivastava, V.; Rouanet, C.; Srivastava, R.; Ramalingam, B.; Locht, C.; Srivastava, B. S. Macrophage-specific Mycobacterium tuberculosis genes: identification by green fluorescent protein and kanamycin resistance selection. Microbiology 2007, 153, 659-666.
    • (2007) Microbiology , vol.153 , pp. 659-666
    • Srivastava, V.1    Rouanet, C.2    Srivastava, R.3    Ramalingam, B.4    Locht, C.5    Srivastava, B.S.6
  • 55
    • 0019887630 scopus 로고
    • Synthesis and application of cleavable photoactivable heterobifunctional reagents
    • Vanin, E. F.; Ji, T. H. Synthesis and application of cleavable photoactivable heterobifunctional reagents. Biochemistry 1981, 20, 6754-6760.
    • (1981) Biochemistry , vol.20 , pp. 6754-6760
    • Vanin, E.F.1    Ji, T.H.2
  • 56
    • 0018635842 scopus 로고
    • Affinity-directed cross-linking of membrane-bound acetylcholine receptor polypeptides with photolabile alpha-bungarotoxin derivatives
    • Witzemann, V.; Muchmore, D.; Raftery, M. A. Affinity-directed cross-linking of membrane-bound acetylcholine receptor polypeptides with photolabile alpha-bungarotoxin derivatives. Biochemistry 1979, 18, 5511-5518.
    • (1979) Biochemistry , vol.18 , pp. 5511-5518
    • Witzemann, V.1    Muchmore, D.2    Raftery, M.A.3
  • 57
    • 0024599294 scopus 로고
    • Isolation of a proteolytically derived domain of the insulin receptor containing the major site of cross-linking/binding
    • Waugh, S. M.; DiBella, E. E.; Pilch, P. F. Isolation of a proteolytically derived domain of the insulin receptor containing the major site of cross-linking/binding. Biochemistry 1989, 28, 3448-3455.
    • (1989) Biochemistry , vol.28 , pp. 3448-3455
    • Waugh, S.M.1    DiBella, E.E.2    Pilch, P.F.3
  • 58
    • 0028905536 scopus 로고
    • Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase
    • Reddy, S. G.; Sacchettini, J. C.; Blanchard, J. S. Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase. Biochemistry 1995, 34, 3492-3501.
    • (1995) Biochemistry , vol.34 , pp. 3492-3501
    • Reddy, S.G.1    Sacchettini, J.C.2    Blanchard, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.