메뉴 건너뛰기




Volumn 6, Issue 1, 2011, Pages 34-46

Identification of direct protein targets of small molecules

Author keywords

[No Author keywords available]

Indexed keywords

CELECOXIB; CURCUMIN; DIDEMNIN A; PROTEOME; RAPAMYCIN; RESVERATROL; TACROLIMUS;

EID: 79251511501     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb100294v     Document Type: Review
Times cited : (259)

References (127)
  • 1
    • 84942071302 scopus 로고
    • Bedeutung der Stereochemie fuür die Physiologie
    • Fischer, E. (1898) Bedeutung der Stereochemie fuür die Physiologie Z. Physiol Chem. 26, 60-87
    • (1898) Z. Physiol Chem. , vol.26 , pp. 60-87
    • Fischer, E.1
  • 3
    • 3042799070 scopus 로고    scopus 로고
    • A planning strategy for diversity-oriented synthesis
    • Burke, M. D. and Schreiber, S. L. (2004) A planning strategy for diversity-oriented synthesis Angew. Chem., Int. Ed. 43, 46-58
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 46-58
    • Burke, M.D.1    Schreiber, S.L.2
  • 4
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D. E., Walsh, C. T., and Khosla, C. (1998) Harnessing the biosynthetic code: combinations, permutations, and mutations Science 282, 63-68
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 5
    • 4544357020 scopus 로고    scopus 로고
    • DNA-templated organic synthesis: Natures strategy for controlling chemical reactivity applied to synthetic molecules
    • Li, X. and Liu, D. R. (2004) DNA-templated organic synthesis: natures strategy for controlling chemical reactivity applied to synthetic molecules Angew. Chem., Int. Ed. 43, 4848-4870
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 4848-4870
    • Li, X.1    Liu, D.R.2
  • 6
    • 34548603604 scopus 로고    scopus 로고
    • Chemical evolution as a tool for molecular discovery
    • Wrenn, S. J. and Harbury, P. B. (2007) Chemical evolution as a tool for molecular discovery Annu. Rev. Biochem. 76, 331-349
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 331-349
    • Wrenn, S.J.1    Harbury, P.B.2
  • 7
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., and Fesik, S. W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR Science 274, 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
  • 9
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer, D. M., Wandless, T. J., Schreiber, S. L., and Crabtree, G. R. (1993) Controlling signal transduction with synthetic ligands Science 262, 1019-1024
    • (1993) Science , vol.262 , pp. 1019-1024
    • Spencer, D.M.1    Wandless, T.J.2    Schreiber, S.L.3    Crabtree, G.R.4
  • 12
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang, J., Yang, P. L., and Gray, N. S. (2009) Targeting cancer with small molecule kinase inhibitors Nat. Rev. Cancer 9, 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 14
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire, A., Xu, S., Montgomery, M. K., Kostas, S. A., Driver, S. E., and Mello, C. C. (1998) Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans Nature 391, 806-811
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1    Xu, S.2    Montgomery, M.K.3    Kostas, S.A.4    Driver, S.E.5    Mello, C.C.6
  • 15
    • 0034830898 scopus 로고    scopus 로고
    • Molecular recognition of DNA by small molecules
    • Dervan, P. B. (2001) Molecular recognition of DNA by small molecules Bioorg. Med. Chem. 9, 2215-2235
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2215-2235
    • Dervan, P.B.1
  • 16
    • 11144311139 scopus 로고    scopus 로고
    • Lessons from natural molecules
    • Clardy, J. and Walsh, C. (2004) Lessons from natural molecules Nature 432, 829-837
    • (2004) Nature , vol.432 , pp. 829-837
    • Clardy, J.1    Walsh, C.2
  • 17
    • 34247109045 scopus 로고    scopus 로고
    • Natural products as sources of new drugs over the last 25 years
    • Newman, D. J. and Cragg, G. M. (2007) Natural products as sources of new drugs over the last 25 years J. Nat. Prod. 70, 461-477
    • (2007) J. Nat. Prod. , vol.70 , pp. 461-477
    • Newman, D.J.1    Cragg, G.M.2
  • 18
    • 52049109838 scopus 로고    scopus 로고
    • Natural products in drug discovery
    • Harvey, A. L. (2008) Natural products in drug discovery Drug Discovery Today 13, 894-901
    • (2008) Drug Discovery Today , vol.13 , pp. 894-901
    • Harvey, A.L.1
  • 19
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene networks
    • Yamamoto, K. R. (1985) Steroid receptor regulated transcription of specific genes and gene networks Annu. Rev. Genet. 19, 209-252
    • (1985) Annu. Rev. Genet. , vol.19 , pp. 209-252
    • Yamamoto, K.R.1
  • 21
    • 0030221053 scopus 로고    scopus 로고
    • Understanding and controlling the cell cycle with natural products
    • Hung, D. T., Jamison, T. F., and Schreiber, S. L. (1996) Understanding and controlling the cell cycle with natural products Chem. Biol. 3, 623-639
    • (1996) Chem. Biol. , vol.3 , pp. 623-639
    • Hung, D.T.1    Jamison, T.F.2    Schreiber, S.L.3
  • 22
    • 0034177962 scopus 로고    scopus 로고
    • Dissecting cellular processes using small molecules: Identification of colchicine-like, taxol-like and other small molecules that perturb mitosis
    • Haggarty, S. J., Mayer, T. U., Miyamoto, D. T., Fathi, R., King, R. W., Mitchison, T. J., and Schreiber, S. L. (2000) Dissecting cellular processes using small molecules: identification of colchicine-like, taxol-like and other small molecules that perturb mitosis Chem. Biol. 7, 275-286
    • (2000) Chem. Biol. , vol.7 , pp. 275-286
    • Haggarty, S.J.1    Mayer, T.U.2    Miyamoto, D.T.3    Fathi, R.4    King, R.W.5    Mitchison, T.J.6    Schreiber, S.L.7
  • 23
    • 0037562075 scopus 로고    scopus 로고
    • Chemical genetic modifier screens: Small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation
    • Koeller, K. M., Haggarty, S. J., Perkins, B. D., Leykin, I., Wong, J. C., Kao, M. C., and Schreiber, S. L. (2003) Chemical genetic modifier screens: small molecule trichostatin suppressors as probes of intracellular histone and tubulin acetylation Chem. Biol. 10, 397-410
    • (2003) Chem. Biol. , vol.10 , pp. 397-410
    • Koeller, K.M.1    Haggarty, S.J.2    Perkins, B.D.3    Leykin, I.4    Wong, J.C.5    Kao, M.C.6    Schreiber, S.L.7
  • 24
    • 9344247454 scopus 로고    scopus 로고
    • Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips
    • Huang, J., Zhu, H., Haggarty, S. J., Spring, D. R., Hwang, H., Jin, F., Snyder, M., and Schreiber, S. L. (2004) Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips Proc. Natl. Acad. Sci. U.S.A. 101, 16594-16599
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16594-16599
    • Huang, J.1    Zhu, H.2    Haggarty, S.J.3    Spring, D.R.4    Hwang, H.5    Jin, F.6    Snyder, M.7    Schreiber, S.L.8
  • 26
    • 0142167588 scopus 로고    scopus 로고
    • Zebrafish-based small molecule discovery
    • MacRae, C. A. and Peterson, R. T. (2003) Zebrafish-based small molecule discovery Chem. Biol. 10, 901-908
    • (2003) Chem. Biol. , vol.10 , pp. 901-908
    • MacRae, C.A.1    Peterson, R.T.2
  • 27
    • 3042744026 scopus 로고    scopus 로고
    • A role for chemistry in stem cell biology
    • Ding, S. and Schultz, P. G. (2004) A role for chemistry in stem cell biology Nat. Biotechnol. 22, 833-840
    • (2004) Nat. Biotechnol. , vol.22 , pp. 833-840
    • Ding, S.1    Schultz, P.G.2
  • 29
    • 36549006956 scopus 로고    scopus 로고
    • An antidepressant that extends lifespan in adult Caenorhabditis elegans
    • Petrascheck, M., Ye, X., and Buck, L. B. (2007) An antidepressant that extends lifespan in adult Caenorhabditis elegans Nature 450, 553-556
    • (2007) Nature , vol.450 , pp. 553-556
    • Petrascheck, M.1    Ye, X.2    Buck, L.B.3
  • 31
    • 0002925350 scopus 로고
    • A biochemically specific method for enzyme isolation
    • Lerman, L. S. (1953) A biochemically specific method for enzyme isolation Proc. Natl. Acad. Sci. U.S.A. 39, 232-236
    • (1953) Proc. Natl. Acad. Sci. U.S.A. , vol.39 , pp. 232-236
    • Lerman, L.S.1
  • 32
    • 0000606011 scopus 로고
    • Purification of liver flavokinase by column chromatography on flavin-cellulose compounds
    • Arsenis, C. and McCormick, D. B. (1964) Purification of liver flavokinase by column chromatography on flavin-cellulose compounds J. Biol. Chem. 239, 3093-3097
    • (1964) J. Biol. Chem. , vol.239 , pp. 3093-3097
    • Arsenis, C.1    McCormick, D.B.2
  • 34
    • 0014117442 scopus 로고
    • The mechanism of action of colchicine. Binding of colchincine-3H to cellular protein
    • Borisy, G. G. and Taylor, E. W. (1967) The mechanism of action of colchicine. Binding of colchincine-3H to cellular protein J. Cell Biol. 34, 525-533
    • (1967) J. Cell Biol. , vol.34 , pp. 525-533
    • Borisy, G.G.1    Taylor, E.W.2
  • 35
    • 0014118455 scopus 로고
    • The mechanism of action of colchicine. Colchicine binding to sea urchin eggs and the mitotic apparatus
    • Borisy, G. G. and Taylor, E. W. (1967) The mechanism of action of colchicine. Colchicine binding to sea urchin eggs and the mitotic apparatus J. Cell Biol. 34, 535-548
    • (1967) J. Cell Biol. , vol.34 , pp. 535-548
    • Borisy, G.G.1    Taylor, E.W.2
  • 36
    • 0014119107 scopus 로고
    • Isolation of a protein subunit from microtubules
    • Shelanski, M. L. and Taylor, E. W. (1967) Isolation of a protein subunit from microtubules J. Cell Biol. 34, 549-554
    • (1967) J. Cell Biol. , vol.34 , pp. 549-554
    • Shelanski, M.L.1    Taylor, E.W.2
  • 37
    • 0014321783 scopus 로고
    • Properties of the protein subunit of central-pair and outer-doublet microtubules of sea urchin flagella
    • Shelanski, M. L. and Taylor, E. W. (1968) Properties of the protein subunit of central-pair and outer-doublet microtubules of sea urchin flagella J. Cell Biol. 38, 304-315
    • (1968) J. Cell Biol. , vol.38 , pp. 304-315
    • Shelanski, M.L.1    Taylor, E.W.2
  • 38
    • 0014382446 scopus 로고
    • The colchicine-binding protein of mammalian brain and its relation to microtubules
    • Weisenberg, R. C., Borisy, G. G., and Taylor, E. W. (1968) The colchicine-binding protein of mammalian brain and its relation to microtubules Biochemistry 7, 4466-4479
    • (1968) Biochemistry , vol.7 , pp. 4466-4479
    • Weisenberg, R.C.1    Borisy, G.G.2    Taylor, E.W.3
  • 41
    • 0015918260 scopus 로고
    • Opiate receptor: Demonstration in nervous tissue
    • Pert, C. B. and Snyder, S. H. (1973) Opiate receptor: demonstration in nervous tissue Science 179, 1011-1014
    • (1973) Science , vol.179 , pp. 1011-1014
    • Pert, C.B.1    Snyder, S.H.2
  • 42
    • 0016150992 scopus 로고
    • Purification and properties of the cholinergic receptor protein from Electrophorus electricus electric tissue
    • Meunier, J. C., Sealock, R., Olsen, R., and Changeux, J. P. (1974) Purification and properties of the cholinergic receptor protein from Electrophorus electricus electric tissue Eur. J. Biochem. 45, 371-394
    • (1974) Eur. J. Biochem. , vol.45 , pp. 371-394
    • Meunier, J.C.1    Sealock, R.2    Olsen, R.3    Changeux, J.P.4
  • 43
    • 33751119897 scopus 로고    scopus 로고
    • Identification of a GABAA receptor anesthetic binding site at subunit interfaces by photolabeling with an etomidate analog
    • Li, G. D., Chiara, D. C., Sawyer, G. W., Husain, S. S., Olsen, R. W., and Cohen, J. B. (2006) Identification of a GABAA receptor anesthetic binding site at subunit interfaces by photolabeling with an etomidate analog J. Neurosci. 26, 11599-11605
    • (2006) J. Neurosci. , vol.26 , pp. 11599-11605
    • Li, G.D.1    Chiara, D.C.2    Sawyer, G.W.3    Husain, S.S.4    Olsen, R.W.5    Cohen, J.B.6
  • 45
    • 0024472603 scopus 로고
    • A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase
    • Harding, M. W., Galat, A., Uehling, D. E., and Schreiber, S. L. (1989) A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase Nature 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
  • 46
    • 0024442393 scopus 로고
    • A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
    • Siekierka, J. J., Hung, S. H., Poe, M., Lin, C. S., and Sigal, N. H. (1989) A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin Nature 341, 755-757
    • (1989) Nature , vol.341 , pp. 755-757
    • Siekierka, J.J.1    Hung, S.H.2    Poe, M.3    Lin, C.S.4    Sigal, N.H.5
  • 47
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu, J., Farmer, J. D., Jr., Lane, W. S., Friedman, J., Weissman, I., and Schreiber, S. L. (1991) Calcineurin is a common target of cyclophilin- cyclosporin A and FKBP-FK506 complexes Cell 66, 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer Jr., J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 49
    • 0028239893 scopus 로고
    • RAFT1: A mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs
    • Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P., and Snyder, S. H. (1994) RAFT1: a mammalian protein that binds to FKBP12 in a rapamycin-dependent fashion and is homologous to yeast TORs Cell 78, 35-43
    • (1994) Cell , vol.78 , pp. 35-43
    • Sabatini, D.M.1    Erdjument-Bromage, H.2    Lui, M.3    Tempst, P.4    Snyder, S.H.5
  • 51
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R. F., Lane, W. S., Choi, S., Corey, E. J., and Schreiber, S. L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin Science 268, 726-731
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 52
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J., Hassig, C. A., and Schreiber, S. L. (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p Science 272, 408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 53
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix, U. and Superti-Furga, G. (2009) Target profiling of small molecules by chemical proteomics Nat. Chem. Biol. 5, 616-624
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 54
    • 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. and Hatanaka, Y. (2006) Photochemical fishing approaches for identifying target proteins and elucidating the structure of a ligand-binding region using carbene-generating photoreactive probes Anal. Sci. 22, 209-218
    • (2006) Anal. Sci. , vol.22 , pp. 209-218
    • Sadakane, Y.1    Hatanaka, Y.2
  • 55
    • 40849130043 scopus 로고    scopus 로고
    • Proteomic methods for drug target discovery
    • Sleno, L. and Emili, A. (2008) Proteomic methods for drug target discovery Curr. Opin. Chem. Biol. 12, 46-54
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 46-54
    • Sleno, L.1    Emili, A.2
  • 56
    • 77953708147 scopus 로고    scopus 로고
    • Biochemical target isolation for novices: Affinity-based strategies
    • Sato, S., Murata, A., Shirakawa, T., and Uesugi, M. (2010) Biochemical target isolation for novices: affinity-based strategies Chem. Biol. 17, 616-623
    • (2010) Chem. Biol. , vol.17 , pp. 616-623
    • Sato, S.1    Murata, A.2    Shirakawa, T.3    Uesugi, M.4
  • 61
    • 67650070045 scopus 로고    scopus 로고
    • Multi-parameter phenotypic profiling: Using cellular effects to characterize small-molecule compounds
    • Feng, Y., Mitchison, T. J., Bender, A., Young, D. W., and Tallarico, J. A. (2009) Multi-parameter phenotypic profiling: using cellular effects to characterize small-molecule compounds Nat. Rev. Drug Discovery 8, 567-578
    • (2009) Nat. Rev. Drug Discovery , vol.8 , pp. 567-578
    • Feng, Y.1    Mitchison, T.J.2    Bender, A.3    Young, D.W.4    Tallarico, J.A.5
  • 64
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B. and Johnson, K. S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase Gene 67, 31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 65
    • 1542704738 scopus 로고    scopus 로고
    • Identification of Protein-Protein Interactions with Glutathione S-Transferase Fusion Proteins
    • in, pp, Cold Spring Harbor Laboratory Press, Woodbury, NY
    • Einarson, M. B. and Orlinick, J. R. (2002) Identification of Protein-Protein Interactions with Glutathione S-Transferase Fusion Proteins, in Protein-Protein Interactions: A Molecular Cloning Manual, pp 37-57, Cold Spring Harbor Laboratory Press, Woodbury, NY.
    • (2002) Protein-Protein Interactions: A Molecular Cloning Manual , pp. 37-57
    • Einarson, M.B.1    Orlinick, J.R.2
  • 66
    • 34547383713 scopus 로고
    • Preparation of iodine-131 labelled human growth hormone of high specific activity
    • Hunter, W. M. and Greenwood, F. C. (1962) Preparation of iodine-131 labelled human growth hormone of high specific activity Nature 194, 495-496
    • (1962) Nature , vol.194 , pp. 495-496
    • Hunter, W.M.1    Greenwood, F.C.2
  • 67
    • 77956127888 scopus 로고
    • The preparation of I-131-labelled human growth hormone of high specific radioactivity
    • Greenwood, F. C., Hunter, W. M., and Glover, J. S. (1963) The preparation of I-131-labelled human growth hormone of high specific radioactivity Biochem. J. 89, 114-123
    • (1963) Biochem. J. , vol.89 , pp. 114-123
    • Greenwood, F.C.1    Hunter, W.M.2    Glover, J.S.3
  • 68
    • 0019321060 scopus 로고
    • Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation
    • Pace, C. N. and McGrath, T. (1980) Substrate stabilization of lysozyme to thermal and guanidine hydrochloride denaturation J. Biol. Chem. 255, 3862-3865
    • (1980) J. Biol. Chem. , vol.255 , pp. 3862-3865
    • Pace, C.N.1    McGrath, T.2
  • 69
    • 0015785662 scopus 로고
    • Hydrogen exchange studies of respiratory proteins. 3. Structural and free energy changes in hemoglobin by use of a difference method
    • Englander, S. W. and Rolfe, A. (1973) Hydrogen exchange studies of respiratory proteins. 3. Structural and free energy changes in hemoglobin by use of a difference method J. Biol. Chem. 248, 4852-4861
    • (1973) J. Biol. Chem. , vol.248 , pp. 4852-4861
    • Englander, S.W.1    Rolfe, A.2
  • 71
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K. and Kern, D. (2007) Dynamic personalities of proteins Nature 450, 964-972
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 72
    • 61349196789 scopus 로고    scopus 로고
    • Differential responses of the backbone and side-chain conformational dynamics in FKBP12 upon binding the transition-state analog FK506: Implications for transition-state stabilization and target protein recognition
    • Brath, U. and Akke, M. (2009) Differential responses of the backbone and side-chain conformational dynamics in FKBP12 upon binding the transition-state analog FK506: implications for transition-state stabilization and target protein recognition J. Mol. Biol. 387, 233-244
    • (2009) J. Mol. Biol. , vol.387 , pp. 233-244
    • Brath, U.1    Akke, M.2
  • 74
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • Senisterra, G. A., Markin, E., Yamazaki, K., Hui, R., Vedadi, M., and Awrey, D. E. (2006) Screening for ligands using a generic and high-throughput light-scattering-based assay J. Biomol. Screening 11, 940-948
    • (2006) J. Biomol. Screening , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5    Awrey, D.E.6
  • 75
    • 44849085505 scopus 로고    scopus 로고
    • Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands
    • Senisterra, G. A., Soo Hong, B., Park, H. W., and Vedadi, M. (2008) Application of high-throughput isothermal denaturation to assess protein stability and screen for ligands J. Biomol. Screening 13, 337-342
    • (2008) J. Biomol. Screening , vol.13 , pp. 337-342
    • Senisterra, G.A.1    Soo Hong, B.2    Park, H.W.3    Vedadi, M.4
  • 76
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt, S. and Freire, E. (2001) Direct measurement of protein binding energetics by isothermal titration calorimetry Curr. Opin. Struct. Biol. 11, 560-566
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 77
    • 18744391410 scopus 로고    scopus 로고
    • Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
    • Park, C. and Marqusee, S. (2005) Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding Nat. Methods 2, 207-212
    • (2005) Nat. Methods , vol.2 , pp. 207-212
    • Park, C.1    Marqusee, S.2
  • 80
    • 0013789498 scopus 로고
    • Protein substrate conformation and proteolysis
    • Markus, G. (1965) Protein substrate conformation and proteolysis Proc. Natl. Acad. Sci. U.S.A. 54, 253-258
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 253-258
    • Markus, G.1
  • 81
    • 0014199105 scopus 로고
    • Ligand-stabilized conformations in serum albumin
    • Markus, G., McClintock, D. K., and Castellani, B. A. (1967) Ligand-stabilized conformations in serum albumin J. Biol. Chem. 242, 4402-4408
    • (1967) J. Biol. Chem. , vol.242 , pp. 4402-4408
    • Markus, G.1    McClintock, D.K.2    Castellani, B.A.3
  • 82
    • 0014670540 scopus 로고
    • Ligand-induced resistance of staphylococcal nuclease and nuclease-T to proteolysis by subtilisin, alpha-chymotrypsin, and thermolysin
    • Taniuchi, H., Moravek, L., and Anfinsen, C. B. (1969) Ligand-induced resistance of staphylococcal nuclease and nuclease-T to proteolysis by subtilisin, alpha-chymotrypsin, and thermolysin J. Biol. Chem. 244, 4600-4606
    • (1969) J. Biol. Chem. , vol.244 , pp. 4600-4606
    • Taniuchi, H.1    Moravek, L.2    Anfinsen, C.B.3
  • 83
    • 0025823443 scopus 로고
    • Modulation of firefly luciferase stability and impact on studies of gene regulation
    • Thompson, J. F., Hayes, L. S., and Lloyd, D. B. (1991) Modulation of firefly luciferase stability and impact on studies of gene regulation Gene 103, 171-177
    • (1991) Gene , vol.103 , pp. 171-177
    • Thompson, J.F.1    Hayes, L.S.2    Lloyd, D.B.3
  • 84
    • 0028300782 scopus 로고
    • GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha
    • Crews, C. M., Collins, J. L., Lane, W. S., Snapper, M. L., and Schreiber, S. L. (1994) GTP-dependent binding of the antiproliferative agent didemnin to elongation factor 1 alpha J. Biol. Chem. 269, 15411-15414
    • (1994) J. Biol. Chem. , vol.269 , pp. 15411-15414
    • Crews, C.M.1    Collins, J.L.2    Lane, W.S.3    Snapper, M.L.4    Schreiber, S.L.5
  • 85
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J. Mol. Biol. 229, 105-124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 87
    • 0025647885 scopus 로고
    • Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin
    • Bierer, B. E., Mattila, P. S., Standaert, R. F., Herzenberg, L. A., Burakoff, S. J., Crabtree, G., and Schreiber, S. L. (1990) Two distinct signal transmission pathways in T lymphocytes are inhibited by complexes formed between an immunophilin and either FK506 or rapamycin Proc. Natl. Acad. Sci. U.S.A. 87, 9231-9235
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9231-9235
    • Bierer, B.E.1    Mattila, P.S.2    Standaert, R.F.3    Herzenberg, L.A.4    Burakoff, S.J.5    Crabtree, G.6    Schreiber, S.L.7
  • 88
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman, J., Movva, N. R., and Hall, M. N. (1991) Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast Science 253, 905-909
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 89
    • 0028598672 scopus 로고
    • RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex
    • Chiu, M. I., Katz, H., and Berlin, V. (1994) RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex Proc. Natl. Acad. Sci. U.S.A. 91, 12574-12578
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12574-12578
    • Chiu, M.I.1    Katz, H.2    Berlin, V.3
  • 90
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi, J., Chen, J., Schreiber, S. L., and Clardy, J. (1996) Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP Science 273, 239-242
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 91
    • 59149091041 scopus 로고    scopus 로고
    • Curcumin disrupts the mammalian target of rapamycin-raptor complex
    • Beevers, C. S., Chen, L., Liu, L., Luo, Y., Webster, N. J., and Huang, S. (2009) Curcumin disrupts the mammalian target of rapamycin-raptor complex Cancer Res. 69, 1000-1008
    • (2009) Cancer Res. , vol.69 , pp. 1000-1008
    • Beevers, C.S.1    Chen, L.2    Liu, L.3    Luo, Y.4    Webster, N.J.5    Huang, S.6
  • 95
    • 35148824614 scopus 로고    scopus 로고
    • Network pharmacology
    • Hopkins, A. L. (2007) Network pharmacology Nat. Biotechnol. 25, 1110-1111
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1110-1111
    • Hopkins, A.L.1
  • 97
    • 5644255981 scopus 로고    scopus 로고
    • Photo-affinity labeling strategies in identifying the protein ligands of bioactive small molecules: Examples of targeted synthesis of drug analog photoprobes
    • Colca, J. R. and Harrigan, G. G. (2004) Photo-affinity labeling strategies in identifying the protein ligands of bioactive small molecules: examples of targeted synthesis of drug analog photoprobes Comb. Chem. High Throughput Screening 7, 699-704
    • (2004) Comb. Chem. High Throughput Screening , vol.7 , pp. 699-704
    • Colca, J.R.1    Harrigan, G.G.2
  • 98
    • 1042287126 scopus 로고    scopus 로고
    • Tagged library approach to chemical genomics and proteomics
    • Mitsopoulos, G., Walsh, D. P., and Chang, Y. T. (2004) Tagged library approach to chemical genomics and proteomics Curr. Opin. Chem. Biol. 8, 26-32
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 26-32
    • Mitsopoulos, G.1    Walsh, D.P.2    Chang, Y.T.3
  • 99
    • 78349276459 scopus 로고    scopus 로고
    • Detection of the specific binding on protein microarrays by oblique-incidence reflectivity difference method
    • published online September 6, 2010, DOI: 10.1088/2040-8978/12/9/095301
    • Lu, H., Wen, J. A., Wang, X., Yuan, K., Li, W., Lu, H. B., Zhou, Y. L., Jin, K. J., Ruan, K. C., and Yang, G. Z. (2010) Detection of the specific binding on protein microarrays by oblique-incidence reflectivity difference method, J. Opt. 12, published online September 6, 2010, DOI: 10.1088/2040-8978/12/9/095301.
    • (2010) J. Opt. , vol.12
    • Lu, H.1    Wen, J.A.2    Wang, X.3    Yuan, K.4    Li, W.5    Lu, H.B.6    Zhou, Y.L.7    Jin, K.J.8    Ruan, K.C.9    Yang, G.Z.10
  • 102
    • 22244445882 scopus 로고    scopus 로고
    • A tandem orthogonal proteolysis strategy for high-content chemical proteomics
    • Speers, A. E. and Cravatt, B. F. (2005) A tandem orthogonal proteolysis strategy for high-content chemical proteomics J. Am. Chem. Soc. 127, 10018-10019
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10018-10019
    • Speers, A.E.1    Cravatt, B.F.2
  • 103
    • 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., and Cravatt, B. F. (2005) Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling Nat. Biotechnol. 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
  • 104
    • 77950493758 scopus 로고    scopus 로고
    • Natural products and their biological targets: Proteomic and metabolomic labeling strategies
    • Bottcher, T., Pitscheider, M., and Sieber, S. A. (2010) Natural products and their biological targets: proteomic and metabolomic labeling strategies Angew. Chem., Int. Ed. 49, 2680-2698
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 2680-2698
    • Bottcher, T.1    Pitscheider, M.2    Sieber, S.A.3
  • 105
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo, M., Verhelst, S., Bellingard-Dubouchaud, V., Toba, S., and Greenbaum, D. (2000) Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs Chem. Biol. 7, 27-38
    • (2000) Chem. Biol. , vol.7 , pp. 27-38
    • Bogyo, M.1    Verhelst, S.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 106
    • 76649096660 scopus 로고    scopus 로고
    • Synthesis of S -adenosyl- l -homocysteine capture compounds for selective photoinduced isolation of methyltransferases
    • Dalhoff, C., Huben, M., Lenz, T., Poot, P., Nordhoff, E., Koster, H., and Weinhold, E. (2010) Synthesis of S -adenosyl- l -homocysteine capture compounds for selective photoinduced isolation of methyltransferases ChemBioChem 11, 256-265
    • (2010) ChemBioChem , vol.11 , pp. 256-265
    • Dalhoff, C.1    Huben, M.2    Lenz, T.3    Poot, P.4    Nordhoff, E.5    Koster, H.6    Weinhold, E.7
  • 107
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • Evans, M. J. and Cravatt, B. F. (2006) Mechanism-based profiling of enzyme families Chem. Rev. 106, 3279-3301
    • (2006) Chem. Rev. , vol.106 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 109
    • 77952722630 scopus 로고    scopus 로고
    • Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements
    • West, G. M., Tucker, C. L., Xu, T., Park, S. K., Han, X., Yates, J. R., 3rd, and Fitzgerald, M. C. (2010) Quantitative proteomics approach for identifying protein-drug interactions in complex mixtures using protein stability measurements Proc. Natl. Acad. Sci. U.S.A. 107, 9078-9082
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9078-9082
    • West, G.M.1    Tucker, C.L.2    Xu, T.3    Park, S.K.4    Han, X.5    Yates III, J.R.6    Fitzgerald, M.C.7
  • 110
    • 0029161284 scopus 로고
    • Mass-spectrometric characterization of a protein ligand interaction
    • Anderegg, R. J. and Wagner, D. S. (1995) Mass-spectrometric characterization of a protein ligand interaction J. Am. Chem. Soc. 117, 1374-1377
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1374-1377
    • Anderegg, R.J.1    Wagner, D.S.2
  • 111
    • 0030992108 scopus 로고    scopus 로고
    • Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase
    • Wang, F., Blanchard, J. S., and Tang, X. J. (1997) Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase Biochemistry 36, 3755-3759
    • (1997) Biochemistry , vol.36 , pp. 3755-3759
    • Wang, F.1    Blanchard, J.S.2    Tang, X.J.3
  • 112
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G., and Yates, J. R., 3rd. (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics Anal. Chem. 76, 4193-4201
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 113
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius, D. and Bondarenko, P. V. (2002) Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry J. Proteome Res. 1, 317-323
    • (2002) J. Proteome Res. , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 114
    • 41149127192 scopus 로고    scopus 로고
    • A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen
    • Asara, J. M., Christofk, H. R., Freimark, L. M., and Cantley, L. C. (2008) A label-free quantification method by MS/MS TIC compared to SILAC and spectral counting in a proteomics screen Proteomics 8, 994-999
    • (2008) Proteomics , vol.8 , pp. 994-999
    • Asara, J.M.1    Christofk, H.R.2    Freimark, L.M.3    Cantley, L.C.4
  • 115
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • OFarrell, P. H. (1975) High resolution two-dimensional electrophoresis of proteins J. Biol. Chem. 250, 4007-4021
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • Ofarrell, P.H.1
  • 116
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu, M., Morgan, M. E., and Minden, J. S. (1997) Difference gel electrophoresis: a single gel method for detecting changes in protein extracts Electrophoresis 18, 2071-2077
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 117
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., and Yates, J. R., 3rd. (2001) Large-scale analysis of the yeast proteome by multidimensional protein identification technology Nat. Biotechnol. 19, 242-247
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 118
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 119
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 17, 994-999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 120
    • 17444383113 scopus 로고    scopus 로고
    • Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry
    • DeSouza, L., Diehl, G., Rodrigues, M. J., Guo, J., Romaschin, A. D., Colgan, T. J., and Siu, K. W. (2005) Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry J. Proteome Res. 4, 377-386
    • (2005) J. Proteome Res. , vol.4 , pp. 377-386
    • Desouza, L.1    Diehl, G.2    Rodrigues, M.J.3    Guo, J.4    Romaschin, A.D.5    Colgan, T.J.6    Siu, K.W.7
  • 122
    • 70549111633 scopus 로고    scopus 로고
    • Methods for the proteomic identification of protease substrates
    • Agard, N. J. and Wells, J. A. (2009) Methods for the proteomic identification of protease substrates Curr. Opin. Chem. Biol. 13, 503-509
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 503-509
    • Agard, N.J.1    Wells, J.A.2
  • 123
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet, A., Butler, G. S., Rodriguez, D., Prudova, A., and Overall, C. M. (2008) Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome Mol. Cell. Proteomics 7, 1925-1951
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodriguez, D.3    Prudova, A.4    Overall, C.M.5
  • 125
    • 60649093306 scopus 로고    scopus 로고
    • High throughput methods of assessing protein stability and aggregation
    • Senisterra, G. A. and Finerty, P. J., Jr. (2009) High throughput methods of assessing protein stability and aggregation Mol. Biosyst. 5, 217-223
    • (2009) Mol. Biosyst. , vol.5 , pp. 217-223
    • Senisterra, G.A.1    Finerty Jr., P.J.2
  • 126
    • 0033621118 scopus 로고    scopus 로고
    • The propagation of binding interactions to remote sites in proteins: Analysis of the binding of the monoclonal antibody D1.3 to lysozyme
    • Freire, E. (1999) The propagation of binding interactions to remote sites in proteins: analysis of the binding of the monoclonal antibody D1.3 to lysozyme Proc. Natl. Acad. Sci. U.S.A. 96, 10118-10122
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10118-10122
    • Freire, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.