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Volumn 8, Issue 4, 2004, Pages 399-406

Making drugs on proteins: Site-directed ligand discovery for fragment-based lead assembly

Author keywords

ADC; aspartate decarboxylase; electrospray ionization mass spectrometry; ESI MS; high throughput screening; HTS; IL 2; interleukin 2; MALDI TOF; matrix assisted laser desorption ionization time of flight; methanethiosulfonate; MTS; PTP 1B

Indexed keywords

ALRESTATIN; LIGAND; PEPTIDE; RO 26 4550; UNCLASSIFIED DRUG;

EID: 3342998507     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.06.010     Document Type: Review
Times cited : (68)

References (47)
  • 1
    • 0030039619 scopus 로고    scopus 로고
    • The art and practice of structure-based drug design: A molecular modeling perspective
    • Bohacek R.S., McMartin C., Guida W.C. The art and practice of structure-based drug design: a molecular modeling perspective. Med Res Rev. 16:1996;3-50
    • (1996) Med Res Rev , vol.16 , pp. 3-50
    • Bohacek, R.S.1    McMartin, C.2    Guida, W.C.3
  • 2
    • 3042689621 scopus 로고    scopus 로고
    • Fragment-based drug discovery
    • A chemo-centric Perspective on this emerging field.
    • Erlanson D.A., McDowell R.S., O'Brien T. Fragment-based drug discovery. J Med Chem. 47:2004;3463-3482 A chemo-centric Perspective on this emerging field.
    • (2004) J Med Chem , vol.47 , pp. 3463-3482
    • Erlanson, D.A.1    McDowell, R.S.2    O'Brien, T.3
  • 3
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • A watershed paper that provides mechanistic explanations for non-specific inhibition of proteins by high concentrations of small molecules.
    • McGovern S.L., Caselli E., Grigorieff N., Shoichet B.K. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J Med Chem. 45:2002;1712-1722 A watershed paper that provides mechanistic explanations for non-specific inhibition of proteins by high concentrations of small molecules.
    • (2002) J Med Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 4
    • 0037439447 scopus 로고    scopus 로고
    • Nonleadlikeness and leadlikeness in biochemical screening
    • Rishton G.M. Nonleadlikeness and leadlikeness in biochemical screening. Drug Discov Today. 8:2003;86-96
    • (2003) Drug Discov Today , vol.8 , pp. 86-96
    • Rishton, G.M.1
  • 5
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins: SAR by NMR. Science. 274:1996;1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 6
    • 0037256273 scopus 로고    scopus 로고
    • Application of NMR screening in drug discovery
    • Fejzo J., Lepre C., Xie X. Application of NMR screening in drug discovery. Curr Top Med Chem. 3:2003;81-97
    • (2003) Curr Top Med Chem , vol.3 , pp. 81-97
    • Fejzo, J.1    Lepre, C.2    Xie, X.3
  • 7
    • 0347761359 scopus 로고    scopus 로고
    • NMR spectroscopy tools for structure-aided drug design
    • Homans S.W. NMR spectroscopy tools for structure-aided drug design. Angew Chem Int Ed Engl. 43:2004;290-300
    • (2004) Angew Chem Int Ed Engl , vol.43 , pp. 290-300
    • Homans, S.W.1
  • 8
    • 0038198865 scopus 로고    scopus 로고
    • High-throughput crystallography to enhance drug discovery
    • Sharff A., Jhoti H. High-throughput crystallography to enhance drug discovery. Curr Opin Chem Biol. 7:2003;340-345
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 340-345
    • Sharff, A.1    Jhoti, H.2
  • 9
    • 3342988956 scopus 로고    scopus 로고
    • Tethering is a service mark of Sunesis Pharmaceuticals, Inc. for its fragment-based drug discovery.
    • Tethering is a service mark of Sunesis Pharmaceuticals, Inc. for its fragment-based drug discovery.
  • 11
    • 2542542373 scopus 로고    scopus 로고
    • Tethering: Fragment-based drug discovery
    • A thorough review of the theory and practice of Tethering.
    • Erlanson D.A., Wells J.A., Braisted A.C. Tethering: fragment-based drug discovery. Annu Rev Biophys Biomol Struct. 33:2004;199-223 A thorough review of the theory and practice of Tethering.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 199-223
    • Erlanson, D.A.1    Wells, J.A.2    Braisted, A.C.3
  • 12
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • Toogood P.L. Inhibition of protein-protein association by small molecules: approaches and progress. J Med Chem. 45:2002;1543-1558
    • (2002) J Med Chem , vol.45 , pp. 1543-1558
    • Toogood, P.L.1
  • 13
    • 0037860938 scopus 로고    scopus 로고
    • Modulation of protein-protein interactions with small organic molecules
    • Berg T. Modulation of protein-protein interactions with small organic molecules. Angew Chem Int Ed Engl. 42:2003;2462-2481
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 2462-2481
    • Berg, T.1
  • 14
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • An exhaustive recent review discussing the state of the art in this field.
    • Arkin M.R., Wells J.A. Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov. 3:2004;301-317 An exhaustive recent review discussing the state of the art in this field.
    • (2004) Nat Rev Drug Discov , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 15
    • 0033491981 scopus 로고    scopus 로고
    • Biology of the interleukin-2 receptor
    • Nelson B.H., Willerford D.M. Biology of the interleukin-2 receptor. Adv Immunol. 70:1998;1-81
    • (1998) Adv Immunol , vol.70 , pp. 1-81
    • Nelson, B.H.1    Willerford, D.M.2
  • 18
    • 0038010557 scopus 로고    scopus 로고
    • Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2
    • Hyde J., Braisted A.C., Randal M., Arkin M.R. Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2. Biochemistry. 42:2003;6475-6483
    • (2003) Biochemistry , vol.42 , pp. 6475-6483
    • Hyde, J.1    Braisted, A.C.2    Randal, M.3    Arkin, M.R.4
  • 19
    • 0037414274 scopus 로고    scopus 로고
    • Discovery of a potent small molecule IL-2 inhibitor through fragment assembly
    • The first report of a nanomolar inhibitor of a protein-protein interaction discovered using Tethering.
    • Braisted A.C., Oslob J.D., Delano W.L., Hyde J., McDowell R.S., Waal N., Yu C., Arkin M.R., Raimundo B.C. Discovery of a potent small molecule IL-2 inhibitor through fragment assembly. J Am Chem Soc. 125:2003;3714-3715 The first report of a nanomolar inhibitor of a protein-protein interaction discovered using Tethering.
    • (2003) J Am Chem Soc , vol.125 , pp. 3714-3715
    • Braisted, A.C.1    Oslob, J.D.2    Delano, W.L.3    Hyde, J.4    McDowell, R.S.5    Waal, N.6    Yu, C.7    Arkin, M.R.8    Raimundo, B.C.9
  • 20
    • 0346850033 scopus 로고    scopus 로고
    • Potent small-molecule binding to a dynamic hot spot on IL-2
    • Thanos C.D., Randal M., Wells J.A. Potent small-molecule binding to a dynamic hot spot on IL-2. J Am Chem Soc. 125:2003;15280-15281
    • (2003) J Am Chem Soc , vol.125 , pp. 15280-15281
    • Thanos, C.D.1    Randal, M.2    Wells, J.A.3
  • 23
    • 0037038325 scopus 로고    scopus 로고
    • Identification of potent and selective small-molecule inhibitors of caspase-3 through the use of extended tethering and structure-based drug design
    • Choong I.C., Lew W., Lee D., Pham P., Burdett M.T., Lam J.W., Wiesmann C., Luong T.N., Fahr B., DeLano W.L., et al. Identification of potent and selective small-molecule inhibitors of caspase-3 through the use of extended tethering and structure-based drug design. J Med Chem. 45:2002;5005-5022
    • (2002) J Med Chem , vol.45 , pp. 5005-5022
    • Choong, I.C.1    Lew, W.2    Lee, D.3    Pham, P.4    Burdett, M.T.5    Lam, J.W.6    Wiesmann, C.7    Luong, T.N.8    Fahr, B.9    Delano, W.L.10
  • 26
    • 0037466277 scopus 로고    scopus 로고
    • Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences
    • Obita T., Muto T., Endo T., Kohda D. Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences. J Mol Biol. 328:2003;495-504
    • (2003) J Mol Biol , vol.328 , pp. 495-504
    • Obita, T.1    Muto, T.2    Endo, T.3    Kohda, D.4
  • 27
    • 0030898702 scopus 로고    scopus 로고
    • Virtual combinatorial libraries: Dynamic generation of molecular and supramolecular diversity by self-assembly
    • Huc I., Lehn J-M. Virtual combinatorial libraries: dynamic generation of molecular and supramolecular diversity by self-assembly. Proc Natl Acad Sci USA. 94:1997;2106-2110
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2106-2110
    • Huc, I.1    Lehn, J.-M.2
  • 28
    • 0037133560 scopus 로고    scopus 로고
    • Target-induced formation of neuraminidase inhibitors from in vitro virtual combinatorial libraries
    • A proof-of-concept study of dynamic combinatorial chemistry to generate potent inhibitors of an enzyme.
    • Hochgurtel M., Kroth H., Piecha D., Hofmann M.W., Nicolau C., Krause S., Schaaf O., Sonnenmoser G., Eliseev A.V. Target-induced formation of neuraminidase inhibitors from in vitro virtual combinatorial libraries. Proc Natl Acad Sci USA. 99:2002;3382-3387 A proof-of-concept study of dynamic combinatorial chemistry to generate potent inhibitors of an enzyme.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 3382-3387
    • Hochgurtel, M.1    Kroth, H.2    Piecha, D.3    Hofmann, M.W.4    Nicolau, C.5    Krause, S.6    Schaaf, O.7    Sonnenmoser, G.8    Eliseev, A.V.9
  • 29
    • 0037472768 scopus 로고    scopus 로고
    • Ketones as building blocks for dynamic combinatorial libraries: Highly active neuraminidase inhibitors generated via selection pressure of the biological target
    • Hochgurtel M., Biesinger R., Kroth H., Piecha D., Hofmann M.W., Krause S., Schaaf O., Nicolau C., Eliseev A.V. Ketones as building blocks for dynamic combinatorial libraries: highly active neuraminidase inhibitors generated via selection pressure of the biological target. J Med Chem. 46:2003;356-358
    • (2003) J Med Chem , vol.46 , pp. 356-358
    • Hochgurtel, M.1    Biesinger, R.2    Kroth, H.3    Piecha, D.4    Hofmann, M.W.5    Krause, S.6    Schaaf, O.7    Nicolau, C.8    Eliseev, A.V.9
  • 30
    • 0142074723 scopus 로고    scopus 로고
    • Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites
    • Webb ME, Stephens E, Smith AG, Abell C: Rapid screening by MALDI-TOF mass spectrometry to probe binding specificity at enzyme active sites. Chem Commun 2003:2416-2417.
    • (2003) Chem Commun , pp. 2416-2417
    • Webb, M.E.1    Stephens, E.2    Smith, A.G.3    Abell, C.4
  • 34
    • 0038143609 scopus 로고    scopus 로고
    • Selective inhibition of engineered receptors via proximity-accelerated alkylation
    • Levitsky K., Ciolli C.J., Belshaw P.J. Selective inhibition of engineered receptors via proximity-accelerated alkylation. Org Lett. 5:2003;693-696
    • (2003) Org Lett , vol.5 , pp. 693-696
    • Levitsky, K.1    Ciolli, C.J.2    Belshaw, P.J.3
  • 35
    • 0038344159 scopus 로고    scopus 로고
    • Reactivity of functional groups on the protein surface: Development of epoxide probes for protein labeling
    • Chen G., Heim A., Riether D., Yee D., Milgrom Y., Gawinowicz M.A., Sames D. Reactivity of functional groups on the protein surface: development of epoxide probes for protein labeling. J Am Chem Soc. 125:2003;8130-8133
    • (2003) J Am Chem Soc , vol.125 , pp. 8130-8133
    • Chen, G.1    Heim, A.2    Riether, D.3    Yee, D.4    Milgrom, Y.5    Gawinowicz, M.A.6    Sames, D.7
  • 37
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • Lewis W.G., Green L.G., Grynszpan F., Radic Z., Carlier P.R., Taylor P., Finn M.G., Sharpless K.B. Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks. Angew Chem Int Ed Engl. 41:2002;1053-1057
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radic, Z.4    Carlier, P.R.5    Taylor, P.6    Finn, M.G.7    Sharpless, K.B.8
  • 38
    • 0348109450 scopus 로고    scopus 로고
    • The growing impact of click chemistry on drug discovery
    • Kolb H.C., Sharpless K.B. The growing impact of click chemistry on drug discovery. Drug Discov Today. 8:2003;1128-1137
    • (2003) Drug Discov Today , vol.8 , pp. 1128-1137
    • Kolb, H.C.1    Sharpless, K.B.2
  • 39
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • A comprehensive review of a widely applicable technology, although not explicitly used for site-directed ligand discovery.
    • Muir T. Semisynthesis of proteins by expressed protein ligation. Annu Rev Biochem. 72:2003;249-289 A comprehensive review of a widely applicable technology, although not explicitly used for site-directed ligand discovery.
    • (2003) Annu Rev Biochem , vol.72 , pp. 249-289
    • Muir, T.1
  • 40
    • 0036171482 scopus 로고    scopus 로고
    • Chemical approaches to the investigation of cellular systems
    • Cook B.N., Bertozzi C.R. Chemical approaches to the investigation of cellular systems. Bioorg Med Chem. 10:2002;829-840
    • (2002) Bioorg Med Chem , vol.10 , pp. 829-840
    • Cook, B.N.1    Bertozzi, C.R.2
  • 41
    • 0037397491 scopus 로고    scopus 로고
    • Functional profiling of the proteome with affinity labels
    • Campbell D.A., Szardenings A.K. Functional profiling of the proteome with affinity labels. Curr Opin Chem Biol. 7:2003;296-303
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 296-303
    • Campbell, D.A.1    Szardenings, A.K.2
  • 42
    • 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 Biotechnol. 14:2003;87-95
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 44
    • 0036977909 scopus 로고    scopus 로고
    • Affinity labeling of cysteine-mutants evidences contact residues in modeled receptor binding sites
    • Perret P., Laube B., Schemm R., Betz H., Goeldner M., Foucaud B. Affinity labeling of cysteine-mutants evidences contact residues in modeled receptor binding sites. J Recept Signal Transduct Res. 22:2002;345-356
    • (2002) J Recept Signal Transduct Res , vol.22 , pp. 345-356
    • Perret, P.1    Laube, B.2    Schemm, R.3    Betz, H.4    Goeldner, M.5    Foucaud, B.6
  • 45
    • 0036047069 scopus 로고    scopus 로고
    • Drug discovery by dynamic combinatorial libraries
    • Ramstrom O., Lehn J.M. Drug discovery by dynamic combinatorial libraries. Nat Rev Drug Discov. 1:2002;26-32
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 26-32
    • Ramstrom, O.1    Lehn, J.M.2
  • 47
    • 2542643984 scopus 로고    scopus 로고
    • Integrating fragment assembly and biophysical methods in the chemical advancement of small-molecule antagonists of IL-2: An approach for inhibiting protein-protein interactions
    • Raimundo B.C., Oslob J.D., Braisted A.C., Hyde J., McDowell R.S., Randal M., Waal N.D., Wilkinson J., Yu C.H., Arkin M.R. Integrating fragment assembly and biophysical methods in the chemical advancement of small-molecule antagonists of IL-2: an approach for inhibiting protein-protein interactions. J Med Chem. 47:2004;3111-3130
    • (2004) J Med Chem , vol.47 , pp. 3111-3130
    • Raimundo, B.C.1    Oslob, J.D.2    Braisted, A.C.3    Hyde, J.4    McDowell, R.S.5    Randal, M.6    Waal, N.D.7    Wilkinson, J.8    Yu, C.H.9    Arkin, M.R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.