메뉴 건너뛰기




Volumn 17, Issue 27, 2010, Pages 3030-3044

Identifying the cellular targets of bioactive small molecules with activity-based probes

Author keywords

Activity based probe; Biotin; Fluorophore; Mass spectrum; Phenotypic assay; Radioisotope; Structure activity relationship; Target identification

Indexed keywords

1 OXA SPIRO[2, 5]OCTANE; ARYL AZIDE; BENZOPHENONE; BIOTIN; CARBENE; COUMARIN DYE; DEC DHBPA; DIAZIRINE; DMC DHBPA; EXCITED CARBONYL; FEN B; FENOFIBRATE; FLURBI BPB; FR182877; FR901464; FUMAGILLIN; FUMAGILLOL BIOTIN; FUMAGILLOL CHLOROACETYLCARBAMATE; IODINE 125; LUMANICIN D; MJE 51; NITRENE; PHORBOXAZOLE A; PHORBOXAZOLE B; RHODAMINE; SMALL MOLECULE PROBE; TARENFLURBIL; TRIPTOLIDE; TRITIUM; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77955629600     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986710791959747     Document Type: Article
Times cited : (11)

References (101)
  • 1
    • 13844276627 scopus 로고    scopus 로고
    • Target-based drug discovery: Is something wrong?
    • Sams-Dodd, F. Target-based drug discovery: is something wrong? Drug Discov. Today, 2005, 10, 139-147.
    • (2005) Drug Discov. Today , vol.10 , pp. 139-147
    • Sams-Dodd, F.1
  • 2
    • 25644454404 scopus 로고    scopus 로고
    • A new grammar for drug discovery
    • Fishman, M.C.; Porter, J.A. A new grammar for drug discovery. Nature, 2005, 437, 491-493.
    • (2005) Nature , vol.437 , pp. 491-493
    • Fishman, M.C.1    Porter, J.A.2
  • 3
    • 20844432908 scopus 로고    scopus 로고
    • Can cell systems biology rescue drug discovery?
    • Butcher, E.C. Can cell systems biology rescue drug discovery? Nat.Rev. Drug Discov., 2005, 4, 461-467.
    • (2005) Nat.Rev. Drug Discov , vol.4 , pp. 461-467
    • Butcher, E.C.1
  • 4
    • 2942616604 scopus 로고    scopus 로고
    • Complex phenotypic assays in high-throughput screening
    • Clemons, P.A. Complex phenotypic assays in high-throughput screening. Curr. Opin. Chem. Biol., 2004, 8, 334-338.
    • (2004) Curr. Opin. Chem. Biol , vol.8 , pp. 334-338
    • Clemons, P.A.1
  • 5
    • 0034678033 scopus 로고    scopus 로고
    • Target-oriented and diversity-oriented organic synthesis in drug discovery
    • Schreiber, S.L. Target-oriented and diversity-oriented organic synthesis in drug discovery. Science, 2000, 287, 1964-1969.
    • (2000) Science , vol.287 , pp. 1964-1969
    • Schreiber, S.L.1
  • 7
    • 17044373269 scopus 로고    scopus 로고
    • Finding the target after screening the phenotype
    • Hart, C.P. Finding the target after screening the phenotype. Drug Discov. Today, 2005, 10, 513-519.
    • (2005) Drug Discov. Today , vol.10 , pp. 513-519
    • Hart, C.P.1
  • 8
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix, U.; Superti-Furga, G. Target profiling of small molecules by chemical proteomics. Nat. Chem. Biol., 2009, 5, 616-624.
    • (2009) Nat. Chem. Biol , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 11
    • 33847016153 scopus 로고    scopus 로고
    • Identification of intracellular targets of small molecular weight chemical compounds using affinity chromatogra- phy
    • Guiffant, D.; Tribouillard, D.; Gug, F.; Galons, H.; Meijer, L.; Blondel, M.; Bach, S. Identification of intracellular targets of small molecular weight chemical compounds using affinity chromatogra- phy. Biotechnol. J., 2007, 2, 68-75.
    • (2007) Biotechnol. J , vol.2 , pp. 68-75
    • Guiffant, D.1    Tribouillard, D.2    Gug, F.3    Galons, H.4    Meijer, L.5    Blondel, M.6    Bach, S.7
  • 12
    • 45749158648 scopus 로고    scopus 로고
    • Identification of the cellular targets of bioactive small organic molecules using affinity reagents
    • Leslie, B.J.; Hergenrother, P.J. Identification of the cellular targets of bioactive small organic molecules using affinity reagents. Chem. Soc. Rev., 2008, 37, 1347-1360.
    • (2008) Chem. Soc. Rev , vol.37 , pp. 1347-1360
    • Leslie, B.J.1    Hergenrother, P.J.2
  • 13
    • 0033215240 scopus 로고    scopus 로고
    • Display cloning: Functional identification of natural product receptors using cDNA-phage display
    • Sche, P.P.; McKenzie, K.M.; White, J.D.; Austin, D.J. Display cloning: functional identification of natural product receptors using cDNA-phage display. Chem. Biol., 1999, 6, 707-716.
    • (1999) Chem. Biol , vol.6 , pp. 707-716
    • Sche, P.P.1    McKenzie, K.M.2    White, J.D.3    Austin, D.J.4
  • 15
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath, G.; Schreiber, S. Printing proteins as microarrays for high-throughput function determination. Science, 2000, 289, 1760-1763.
    • (2000) Science , vol.289 , pp. 1760-1763
    • Macbeath, G.1    Schreiber, S.2
  • 16
    • 0024472603 scopus 로고
    • A receptor for the immuno-suppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding, M.W.; Galat, A.; Uehling, D.E.; Schreiber, S.L. A receptor for the immuno-suppressant FK506 is a cis-trans peptidyl-prolyl isomerase. Nature, 1989, 341, 758-760.
    • (1989) Nature , vol.341 , pp. 758-760
    • Harding, M.W.1    Galat, A.2    Uehling, D.E.3    Schreiber, S.L.4
  • 17
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J.; Hassig, C.A.; Schreiber, S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science, 1996, 272, 408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 19
    • 0036514084 scopus 로고    scopus 로고
    • Photoaffinity labeling in drug discovery and developments: Chemical gateway for entering proteomic frontier
    • Hatanaka, Y.; Sadakane, Y. Photoaffinity labeling in drug discovery and developments: chemical gateway for entering proteomic frontier. Curr. Top. Med. Chem., 2002, 2, 271-288.
    • (2002) Curr. Top. Med. Chem , vol.2 , pp. 271-288
    • Hatanaka, Y.1    Sadakane, Y.2
  • 20
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery, D.A.; Bogyo, M. Chemical proteomics and its application to drug discovery. Curr. Opin. Biotech., 2003, 14, 87-95.
    • (2003) Curr. Opin. Biotech , vol.14 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 21
    • 25144482909 scopus 로고    scopus 로고
    • A chemical inhibitor reveals the role of raf kinase inhibitor protein in cell migration
    • Zhu, S.; Mc Henry, K.T.; Lane, W.S.; Fenteany, G. A chemical inhibitor reveals the role of raf kinase inhibitor protein in cell migration. Chem. Biol., 2005, 12, 981-991.
    • (2005) Chem. Biol , vol.12 , pp. 981-991
    • Zhu, S.1    McHenry, K.T.2    Lane, W.S.3    Fenteany, G.4
  • 22
    • 28844476583 scopus 로고    scopus 로고
    • Studies on calcium dependence reveal multiple modes of action for triptolide
    • Leuenroth, S.J.; Crews, C.M. Studies on calcium dependence reveal multiple modes of action for triptolide. Chem. Biol., 2005, 12, 1259-1268.
    • (2005) Chem. Biol , vol.12 , pp. 1259-1268
    • Leuenroth, S.J.1    Crews, C.M.2
  • 24
    • 0028137859 scopus 로고
    • Selective protein adducts to membrane proteins in cultured rat hepatocytes exposed to diclofenac: Radiochemical and immunochemical analysis
    • Kretz-Rommel, A.; Boelsterli, U.A. Selective protein adducts to membrane proteins in cultured rat hepatocytes exposed to diclofenac: radiochemical and immunochemical analysis. Mol. Pharmacol., 1994, 45, 237-244.
    • (1994) Mol. Pharmacol , vol.45 , pp. 237-244
    • Kretz-Rommel, A.1    Boelsterli, U.A.2
  • 29
    • 33847788820 scopus 로고    scopus 로고
    • Diazonamide toxins reveal an unexpected function for ornithine 8-amino transferase in mitotic cell division
    • Wang, G.; Shang, L.; Burgett, A.W.G.; Harran, P.G.; Wang, X. Diazonamide toxins reveal an unexpected function for ornithine 8-amino transferase in mitotic cell division. Proc. Natl. Acad. Sci. USA, 2007, 104, 2068-2073.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2068-2073
    • Wang, G.1    Shang, L.2    Burgett, A.W.G.3    Harran, P.G.4    Wang, X.5
  • 31
    • 33846681655 scopus 로고    scopus 로고
    • Polyproline-rod approach to isolating protein targets of bioactive small molecules: Isolation of a new target of indomethacin
    • Sato, S.; Kwon, Y; Kamisuki, S.; Srivastava, N.; Mao, Q.; Kawa-zoe, Y; Uesugi, M. Polyproline-rod approach to isolating protein targets of bioactive small molecules: isolation of a new target of indomethacin. J. Am. Chem. Soc, 2007, 129, 873-880.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 873-880
    • Sato, S.1    Kwon, Y.2    Kamisuki, S.3    Srivastava, N.4    Mao, Q.5    Kawa-Zoe, Y.6    Uesugi, M.7
  • 34
    • 50249129580 scopus 로고    scopus 로고
    • Chemical synthesis and biochemical characterization of a biotinylated derivative of 17(3-estradiol with a long side chain covalently attached to its C-7a position
    • Jiang, X.R.; Wang, P.; Fu, X.; Zhu, B.T Chemical synthesis and biochemical characterization of a biotinylated derivative of 17(3-estradiol with a long side chain covalently attached to its C-7a position. Steroids, 2008, 73, 1252-1261.
    • (2008) Steroids , vol.73 , pp. 1252-1261
    • Jiang, X.R.1    Wang, P.2    Fu, X.3    Zhu, B.T.4
  • 37
    • 0030924753 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
    • Sin, N.; Meng, L.; Wang, M.Q.W.; Wen, J.J.; Bornmann, W.G.; Crews, CM. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl. Acad. Sci. USA, 1997, 94, 6099-6103.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6099-6103
    • Sin, N.1    Meng, L.2    Wang, M.Q.W.3    Wen, J.J.4    Bornmann, W.G.5    Crews, C.M.6
  • 38
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L.; Mohan, R.; Kwok, B.H.B.; Elofsson, M.; Sin, N.; Crews, CM. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA, 1999, 96, 10403-10408.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.B.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 39
    • 0034879173 scopus 로고    scopus 로고
    • The anti-inflammatory natural product parthenolide from the medicinal herb Feverfew directly binds to and inhibits IkB kinase
    • Kwok, B.H.B.; Koh, B.; Ndubuisi, M.I.; Elofsson, M.; Crews, CM. The anti-inflammatory natural product parthenolide from the medicinal herb Feverfew directly binds to and inhibits IkB kinase. Chem. Biol, 2001, 8, 759-766.
    • (2001) Chem. Biol , vol.8 , pp. 759-766
    • Kwok, B.H.B.1    Koh, B.2    Ndubuisi, M.I.3    Elofsson, M.4    Crews, C.M.5
  • 40
    • 36448960196 scopus 로고    scopus 로고
    • The natural product avrain-villamide binds to the oncoprotein nucleophosmin
    • Wulff, J.E.; Siegrist, R.; Myers, A.G. The natural product avrain-villamide binds to the oncoprotein nucleophosmin. J. Am. Chem. Soc, 2007, 129, 14444-14451.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 14444-14451
    • Wulff, J.E.1    Siegrist, R.2    Myers, A.G.3
  • 41
    • 0028176358 scopus 로고
    • Fumagillin Derivative Angiogenesis Inhibitor, AGM-1470, Inhibits activation of cyclin-dependent kinases and phosphorylation of retinoblastoma gene product but not protein tyrosyl phosphorylation or protooncogene expression in vascular endothelial cells
    • Abe, J.; Zhou, W.; Takuwa, N.; Taguchi, J.; Kurokawa, K.; Ku-mada, M.; Takuwa, Y. A Fumagillin Derivative Angiogenesis Inhibitor, AGM-1470, Inhibits activation of cyclin-dependent kinases and phosphorylation of retinoblastoma gene product but not protein tyrosyl phosphorylation or protooncogene expression in vascular endothelial cells. Cancer Res., 1994, 54, 3407-3412.
    • (1994) Cancer Res , vol.54 , pp. 3407-3412
    • Abe, J.1    Zhou, W.2    Takuwa, N.3    Taguchi, J.4    Kurokawa, K.5    Ku-Mada, M.6    Takuwa, Y.A.7
  • 42
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu, S.; Widom, J.; Kemp, C.W.; Crews, CM.; Clardy, J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science, 1998, 282, 1324-1327.
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 43
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • Speers, A.E.; Cravatt, B.F. A tandem orthogonal proteolysis strategy for high-content chemical proteomics. J. Am. Chem. Soc, 2005, 127, 10018-10019.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 44
    • 34250746414 scopus 로고    scopus 로고
    • Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)-a general method for mapping sites of probe modification in proteomes
    • Weerapana, E.; Speers, A.E.; Cravatt, B.F. Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)-a general method for mapping sites of probe modification in proteomes. Nat. Protoc, 2007, 2, 1414-1425.
    • (2007) Nat. Protoc , vol.2 , pp. 1414-1425
    • Weerapana, E.1    Speers, A.E.2    Cravatt, B.F.3
  • 45
    • 0003610959 scopus 로고
    • Chemically cleavable biotiny-lated nucleotide: Usefulness in the recovery of protein-DNA complexes from avidin affinity columns
    • Shimkus, M.; Levy, J.; Herman, T. A chemically cleavable biotiny-lated nucleotide: Usefulness in the recovery of protein-DNA complexes from avidin affinity columns. Proc. Natl. Acad. Sci. USA, 1985, 82, 2593-2597.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2593-2597
    • Shimkus, M.1    Levy, J.2    Herman, T.A.3
  • 46
    • 33747618271 scopus 로고    scopus 로고
    • Isotope-Coded and Affinity-Tagged Cross-Linking (ICATXL): An Efficient Strategy to Probe Protein Interaction Surfaces
    • Chu, F.; Mahrus, S.; Craik, C.S.; Burlingame, A.L. Isotope-Coded and Affinity-Tagged Cross-Linking (ICATXL): An Efficient Strategy to Probe Protein Interaction Surfaces. J. Am. Chem. Soc, 2006, 128, 10362-10363.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10362-10363
    • Chu, F.1    Mahrus, S.2    Craik, C.S.3    Burlingame, A.L.4
  • 48
    • 0029926683 scopus 로고    scopus 로고
    • Design and synthesis of a bifunctional label for selection of p-lactamase displayed on filamentous bacteriophage by catalytic activity
    • Marchand-Brynaert, J.; Bouchet, M.; Touillaux, R.; Beauve, C; Fastrez, J. Design and synthesis of a bifunctional label for selection of p-lactamase displayed on filamentous bacteriophage by catalytic activity. Tetrahedron, 1996, 52, 5591-5606.
    • (1996) Tetrahedron , vol.52 , pp. 5591-5606
    • Marchand-Brynaert, J.1    Bouchet, M.2    Touillaux, R.3    Beauve, C.4    Fastrez, J.5
  • 49
    • 59649112891 scopus 로고    scopus 로고
    • Fluorescent labeling of biomolecules with organic probes
    • Gonçalves, M.S.T. Fluorescent labeling of biomolecules with organic probes. Chem. Rev., 2009, 109, 190-212.
    • (2009) Chem. Rev , vol.109 , pp. 190-212
    • Gonçalves, M.S.T.1
  • 51
    • 44949244902 scopus 로고    scopus 로고
    • B) receptors on living cells: Design, synthesis, and biological evaluation
    • Li, X.; Cao, J.H.; Li, Y; Rondard, P.; Zhang, Y; Yi, P.; Liu, J.F.; Nan, F.J. Activity-based probe for specific photoaffinity labeling y-aminobutyric acid B (GABAB) receptors on living cells: design, synthesis, and biological evaluation. J. Med. Chem., 2008, 51, 3057-3060.
    • (2008) J. Med. Chem , vol.51 , pp. 3057-3060
    • Li, X.1    Cao, J.H.2    Li, Y.3    Rondard, P.4    Zhang, Y.5    Yi, P.6    Liu, J.F.7    Nan, F.J.8
  • 53
    • 0037345703 scopus 로고    scopus 로고
    • N-Ac-DEVD-N'-(Polyfluorobenzoyl)-R110: Novel cell-permeable fluorogenic caspase substrates for the detection of caspase activity and apoptosis
    • Zhang, H.Z.; Kasibhatla, S.; Guastella, J.; Tseng, B.; Drewe, J.; Cai, S.X. N-Ac-DEVD-N'-(Polyfluorobenzoyl)-R110: Novel cell-permeable fluorogenic caspase substrates for the detection of caspase activity and apoptosis. Bioconjugate Chem., 2003, 14, 458-463.
    • (2003) Bioconjugate Chem , vol.14 , pp. 458-463
    • Zhang, H.Z.1    Kasibhatla, S.2    Guastella, J.3    Tseng, B.4    Drewe, J.5    Cai, S.X.6
  • 55
    • 33645456729 scopus 로고    scopus 로고
    • Phorboxazole analogues induce association of cdk4 with extranuclear cytokeratin intermediate filaments
    • Forsyth, C.J.; Ying, L.; Chen, J.; Clair, J.J.L. Phorboxazole analogues induce association of cdk4 with extranuclear cytokeratin intermediate filaments. J. Am. Chem. Soc, 2006, 128, 3858-3859.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 3858-3859
    • Forsyth, C.J.1    Ying, L.2    Chen, J.3    Clair, J.J.L.4
  • 57
    • 0035806326 scopus 로고    scopus 로고
    • Direct observation of the target cell for leaf-movement factor using novel fluorescence-labeled probe compounds: Fluorescence studies of nyctinasty in legumes. Part 1
    • Ueda, M.; Wada, Y; Yamamura, S. Direct observation of the target cell for leaf-movement factor using novel fluorescence-labeled probe compounds: fluorescence studies of nyctinasty in legumes. Part 1. Tetrahedron Lett., 2001, 42, 3869-3872.
    • (2001) Tetrahedron Lett , vol.42 , pp. 3869-3872
    • Ueda, M.1    Wada, Y.2    Yamamura, S.3
  • 59
    • 33646462162 scopus 로고    scopus 로고
    • Proteomic profiling of metalloprotease activities with cocktails of active-site probes
    • Sieber, S.A.; Niessen, S.; Hoover, H.S.; Cravatt, B.F. Proteomic profiling of metalloprotease activities with cocktails of active-site probes. Nat. Chem. Biol, 2006, 2, 274-281.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 61
    • 33846807650 scopus 로고    scopus 로고
    • Tagging and detection strategies for activity-based proteomics
    • Sadaghiani, A.M.; Verhelst, S.H.L.; Bogyo, M. Tagging and detection strategies for activity-based proteomics. Curr. Opin. Chem. Biol, 2007, 11, 20-28.
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 20-28
    • Sadaghiani, A.M.1    Verhelst, S.H.L.2    Bogyo, M.3
  • 62
    • 0001047320 scopus 로고    scopus 로고
    • Trifunctional Chemical Probes for the Consolidated Detection and Identification of Enzyme Activities from Complex Proteomes
    • Adam, G.C.; Sorensen, E.J.; Cravatt, B.F. Trifunctional Chemical Probes for the Consolidated Detection and Identification of Enzyme Activities from Complex Proteomes. Mol. Cell. Proteom., 2002, 1, 828-835.
    • (2002) Mol. Cell. Proteom , vol.1 , pp. 828-835
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 63
    • 0344413531 scopus 로고    scopus 로고
    • (-)-FR182877 is a potent and selective inhibitor of carboxylesterase-1
    • Adam, G.C.; Vanderwal, CD.; Sorensen, E.J.; Cravatt, B.F. (-)-FR182877 is a potent and selective inhibitor of carboxylesterase-1. Angew. Chem. Int. Ed., 2003, 42, 5480-5484.
    • (2003) Angew. Chem. Int. Ed , vol.42 , pp. 5480-5484
    • Adam, G.C.1    Vanderwal, C.D.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 64
    • 0034009228 scopus 로고    scopus 로고
    • New antimitotic substance, FR182877. I. taxonomy, fermentation, isolation, physico-chemical properties and biological activities
    • (Tokyo)
    • Sato, B.; Muramatsu, H.; Miyauchi, M.; Hori, Y; Takase, S.; Hino, M.; Hashimoto, S.; Terano, H. A new antimitotic substance, FR182877. I. taxonomy, fermentation, isolation, physico-chemical properties and biological activities. J. Antibiot. (Tokyo), 2000, 53, 123-130.
    • (2000) J. Antibiot , vol.53 , pp. 123-130
    • Sato, B.1    Muramatsu, H.2    Miyauchi, M.3    Hori, Y.4    Takase, S.5    Hino, M.6    Hashimoto, S.7    Terano, H.A.8
  • 65
    • 0037846481 scopus 로고    scopus 로고
    • An enantioselective synthesis of FR182877 provides a chemical rationalization of its structure and affords multigram quantities of its direct precursor
    • Vanderwal, CD.; Vosburg, D.A.; Weiler, S.; Sorensen, E.J. An enantioselective synthesis of FR182877 provides a chemical rationalization of its structure and affords multigram quantities of its direct precursor. J. Am. Chem. Soc, 2003, 125, 5393-5407.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 5393-5407
    • Vanderwal, C.D.1    Vosburg, D.A.2    Weiler, S.3    Sorensen, E.J.4
  • 68
    • 0033792318 scopus 로고    scopus 로고
    • Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles
    • Thiele, C; Hannah, M.J.; Fahrenholz, F.; Huttner, W.B. Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles. Nat. Cell Biol, 2000, 2, 42-49.
    • (2000) Nat. Cell Biol , vol.2 , pp. 42-49
    • Thiele, C.1    Hannah, M.J.2    Fahrenholz, F.3    Huttner, W.B.4
  • 70
    • 33744949267 scopus 로고    scopus 로고
    • C-terminal Fragment of Presenilin Is the Molecular Target of a Dipeptidic y-Secretase-specific Inhibitor DAPT (N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycine t-Butyl Ester)
    • Morohashi, Y; Kan, T; Tominari, Y; Fuwa, H.; Okamura, Y; Watanabe, N.; Sato, C; Natsugari, H.; Fukuyama, T; Iwatsubo, T; Tomita, T. C-terminal Fragment of Presenilin Is the Molecular Target of a Dipeptidic y-Secretase-specific Inhibitor DAPT (N-[N-(3,5-Difluorophenacetyl)-L-alanyl]-S-phenylglycine t-Butyl Ester). J. Biol. Chem., 2006, 281, 14670-14676.
    • (2006) J. Biol. Chem , vol.281 , pp. 14670-14676
    • Morohashi, Y.1    Kan, T.2    Tominari, Y.3    Fuwa, H.4    Okamura, Y.5    Watanabe, N.6    Sato, C.7    Natsugari, H.8    Fukuyama, T.9    Iwatsubo, T.10    Tomita, T.11
  • 71
    • 0037076541 scopus 로고    scopus 로고
    • Identification of a contact region between the tridecapeptide -factor mating pheromone of Saccharomyces cerevisiae and its G protein-coupled receptor by photoaffinity labeling
    • Henry, L.K.; Khare, S.; Son, C; Babu, V.V.S.; Naider, F.; Becker, J.M. Identification of a contact region between the tridecapeptide -factor mating pheromone of Saccharomyces cerevisiae and its G protein-coupled receptor by photoaffinity labeling. Biochemistry 2002, 41, 6128-6139.
    • (2002) Biochemistry , vol.41 , pp. 6128-6139
    • Henry, L.K.1    Khare, S.2    Son, C.3    Babu, V.V.S.4    Naider, F.5    Becker, J.M.6
  • 73
    • 5444264224 scopus 로고    scopus 로고
    • Identification of ligand binding regions of the Saccharomyces cerevisiae -factor pheromone receptor by photoaffinity cross-linking
    • Son, CD.; Sargsyan, H.; Naider, F.; Becker, J.M. Identification of ligand binding regions of the Saccharomyces cerevisiae -factor pheromone receptor by photoaffinity cross-linking. Biochemistry, 2004, 43, 13193-13203.
    • (2004) Biochemistry , vol.43 , pp. 13193-13203
    • Son, C.D.1    Sargsyan, H.2    Naider, F.3    Becker, J.M.4
  • 74
    • 67049100554 scopus 로고    scopus 로고
    • Elucidation of the molecular basis of cholecystokinin peptide docking to its receptor using site-specific intrinsic photoaffinity labeling and molecular modeling
    • Dong, M.; Lam, P.C.H.; Pinon, D.I.; Abagyan, R.; Miller, L.J. Elucidation of the molecular basis of cholecystokinin peptide docking to its receptor using site-specific intrinsic photoaffinity labeling and molecular modeling. Biochemistry, 2009, 48, 5303-5312.
    • (2009) Biochemistry , vol.48 , pp. 5303-5312
    • Dong, M.1    Lam, P.C.H.2    Pinon, D.I.3    Abagyan, R.4    Miller, L.J.5
  • 76
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum, D.; Medzihradszky, K.F.; Burlingame, A.; Bogyo, M. Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol, 2000, 7, 569-581.
    • (2000) Chem. Biol , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 77
    • 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. Biotech., 2005, 23, 1303-1307.
    • (2005) Nat. Biotech , vol.23 , pp. 1303-1307
    • Evans, M.J.1    Saghatelian, A.2    Sorensen, E.J.3    Cravatt, B.F.4
  • 79
    • 73849163777 scopus 로고
    • The Photolysis of Diazoacetylchymotrypsin
    • PC3006-3008
    • Singh, A.; Thornton, E.R.; Westheimer, F.H. The Photolysis of Diazoacetylchymotrypsin. J. Biol. Chem., 1962, 237, PC3006-3008.
    • (1962) J. Biol. Chem , vol.237
    • Singh, A.1    Thornton, E.R.2    Westheimer, F.H.3
  • 80
    • 0033951038 scopus 로고    scopus 로고
    • Using photolabile ligands in drug discovery and development
    • Dormán, G.; Prestwich, G.D. Using photolabile ligands in drug discovery and development. Trends Biotech., 2000, 18, 64-77.
    • (2000) Trends Biotech , vol.18 , pp. 64-77
    • Dormán, G.1    Prestwich, G.D.2
  • 82
    • 32544459067 scopus 로고    scopus 로고
    • Photochemical fishing approaches for identifying target proteins and elucidating the structure of a ligand-binding region using carbene-generating photoreactive probes
    • Sadakane, Y.; Hatanaka, Y Photochemical fishing approaches for identifying target proteins and elucidating the structure of a ligand-binding region using carbene-generating photoreactive probes. Anal. Sci., 2006, 22, 209-218.
    • (2006) Anal. Sci , vol.22 , pp. 209-218
    • Sadakane, Y.1    Hatanaka, Y.2
  • 84
    • 0037462106 scopus 로고    scopus 로고
    • Activity-Based Protein Profiling in vivo Using a Copper(I)-Catalyzed Azide-Alkyne[3 + 2] Cycloaddition
    • Speers, A.E.; Adam, G.C.; Cravatt, B.F. Activity-Based Protein Profiling in vivo Using a Copper(I)-Catalyzed Azide-Alkyne[3 + 2] Cycloaddition. J. Am. Chem. Soc, 2003, 125, 4686-4687.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 85
    • 58849155922 scopus 로고    scopus 로고
    • Seeing small molecules in action with bioorthogonal chemistry
    • Raghavan, A.S.; Hang, H.C. Seeing small molecules in action with bioorthogonal chemistry. Drug Discov. Today, 2009, 14, 178-184.
    • (2009) Drug Discov. Today , vol.14 , pp. 178-184
    • Raghavan, A.S.1    Hang, H.C.2
  • 86
    • 0026516860 scopus 로고
    • Recent advances in the Staud-inger reaction
    • Gololobov, Y.G.; Kasukhin, L.F. Recent advances in the Staud-inger reaction. Tetrahedron, 1992, 48, 1353-1406.
    • (1992) Tetrahedron , vol.48 , pp. 1353-1406
    • Gololobov, Y.G.1    Kasukhin, L.F.2
  • 87
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H.C; Finn, M.G.; Sharpless, K.B. Click chemistry: Diverse chemical function from a few good reactions. Angew. Chem. Int. Ed., 2001, 40, 2004-2021.
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 88
    • 0034677879 scopus 로고    scopus 로고
    • Cell Surface Engineering by a Modified Staudinger Reaction
    • Saxon, E.; Bertozzi, C.R. Cell Surface Engineering by a Modified Staudinger Reaction. Science, 2000, 287, 2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 90
    • 36749047362 scopus 로고    scopus 로고
    • Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation
    • MacKinnon, A.L.; Garrison, J.L.; Hegde, R.S.; Taunton, J. Photo-leucine incorporation reveals the target of a cyclodepsipeptide inhibitor of cotranslational translocation. J. Am. Chem. Soc., 2007, 129, 14560-14561.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 14560-14561
    • Mackinnon, A.L.1    Garrison, J.L.2    Hegde, R.S.3    Taunton, J.4
  • 91
    • 1942522084 scopus 로고    scopus 로고
    • Profiling Enzyme Activities In vivo Using Click Chemistry Methods
    • Speers, A.E.; Cravatt, B.F. Profiling Enzyme Activities In vivo Using Click Chemistry Methods. Chem. Biol., 2004, 11, 535-546.
    • (2004) Chem. Biol , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 93
    • 34548118304 scopus 로고    scopus 로고
    • Activity-Based Protein Profiling for Type I Methionine Aminopeptidase by Using Photo-Affinity Trimodular Probes
    • Qiu, W.W.; Xu J.; Li J.Y.; Li, J.; Nan, F.J. Activity-Based Protein Profiling for Type I Methionine Aminopeptidase by Using Photo-Affinity Trimodular Probes. ChemBioChem, 2007, 8, 1351-1358.
    • (2007) ChemBioChem , vol.8 , pp. 1351-1358
    • Qiu, W.W.1    Xu, J.2    Li, J.Y.3    Li, J.4    Nan, F.J.5
  • 94
    • 50649112213 scopus 로고    scopus 로고
    • Activity-based protein profiling: From enzyme chemistry to proteomic chemistry
    • Cravatt, B.F.; Wright, A.T.; Kozarich, J.W. Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu. Rev. Biochem., 2008, 77, 383-414.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 383-414
    • Cravatt, B.F.1    Wright, A.T.2    Kozarich, J.W.3
  • 95
    • 77955594851 scopus 로고    scopus 로고
    • Identification and characterization of molecular targets of natural products by mass spectrometry
    • Cheng, K.W.; Wong, C.C.; Wang, M.; He, Q.Y.; Chen, F. Identification and characterization of molecular targets of natural products by mass spectrometry. Mass Spectrom Rev., 2009, 28, 1-30.
    • (2009) Mass Spectrom Rev , vol.28 , pp. 1-30
    • Cheng, K.W.1    Wong, C.C.2    Wang, M.3    He, Q.Y.4    Chen, F.5
  • 96
    • 37249014081 scopus 로고    scopus 로고
    • The biological impact of mass-spectrometry-based proteomics
    • Cravatt, B.F.; Simon, G.M.; Yates III, J.R. The biological impact of mass-spectrometry-based proteomics. Nature, 2007, 450, 991-1000.
    • (2007) Nature , vol.450 , pp. 991-1000
    • Cravatt, B.F.1    Simon, G.M.2    Yates III, J.R.3
  • 97
    • 67349250376 scopus 로고    scopus 로고
    • Application of LC/MS to proteomics studies: Current status and future prospects
    • Chen, G.; Pramanik, B.N. Application of LC/MS to proteomics studies: current status and future prospects. Drug Discov. Today, 2009, 14, 465-471.
    • (2009) Drug Discov. Today , vol.14 , pp. 465-471
    • Chen, G.1    Pramanik, B.N.2
  • 98
    • 1842865013 scopus 로고    scopus 로고
    • Pladienolides, new substances from culture of Streptomyces platensis Mer-111077. III. In vitro and in vivo antitumoe activities
    • (Tokyo)
    • Mizui, Y.; Sakai, T.; Iwata, M.; Uenaka, T.; Okamoto, K.; Shimizu, H.; Yamori, T.; Yoshimatsu, K.; Asada, M. Pladienolides, new substances from culture of Streptomyces platensis Mer-111077. III. In vitro and in vivo antitumoe activities. J. Antibiot. (Tokyo), 2004, 57, 188-196.
    • (2004) J. Antibiot , vol.57 , pp. 188-196
    • Mizui, Y.1    Sakai, T.2    Iwata, M.3    Uenaka, T.4    Okamoto, K.5    Shimizu, H.6    Yamori, T.7    Yoshimatsu, K.8    Asada, M.9
  • 100
    • 70350307216 scopus 로고    scopus 로고
    • A Click chemistry mediated in vivo activity probe for dimethylarginine dimethylaminohydrolase
    • Wang, Y.; Hu, S.; Fast, W. A Click chemistry mediated in vivo activity probe for dimethylarginine dimethylaminohydrolase. J. Am. Chem. Soc., 2009, 131, 15096-15097.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 15096-15097
    • Wang, Y.1    Hu, S.2    Fast, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.