메뉴 건너뛰기




Volumn 30, Issue 1, 2005, Pages 26-34

Manipulating proteins with chemistry: A cross-section of chemical biology

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; PROTEIN DERIVATIVE; TRANSCRIPTION FACTOR;

EID: 11844291287     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2004.10.010     Document Type: Review
Times cited : (79)

References (70)
  • 1
    • 0642346948 scopus 로고    scopus 로고
    • Ten commandments of enzymology, amended
    • A. Kornberg Ten commandments of enzymology, amended Trends Biochem. Sci. 28 2003 515 517
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 515-517
    • Kornberg, A.1
  • 2
    • 0035233367 scopus 로고    scopus 로고
    • Recent advances in chemical approaches to the study of biological systems
    • M.A. Shogren-Knaak Recent advances in chemical approaches to the study of biological systems Annu. Rev. Cell Dev. Biol. 17 2001 405 433
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 405-433
    • Shogren-Knaak, M.A.1
  • 3
    • 0037416141 scopus 로고    scopus 로고
    • The small-molecule approach to biology
    • S.L. Schreiber The small-molecule approach to biology Chem. Eng. News 81 2003 51 61
    • (2003) Chem. Eng. News , vol.81 , pp. 51-61
    • Schreiber, S.L.1
  • 4
    • 0037125492 scopus 로고    scopus 로고
    • Catalytic subunit of protein kinase a caged at the activating phosphothreonine
    • K. Zou Catalytic subunit of protein kinase A caged at the activating phosphothreonine J. Am. Chem. Soc. 124 2002 8220 8229
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8220-8229
    • Zou, K.1
  • 5
    • 0037139515 scopus 로고    scopus 로고
    • A new strategy for caging proteins regulated by kinases
    • M. Ghosh A new strategy for caging proteins regulated by kinases J. Am. Chem. Soc. 124 2002 2440 2441
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2440-2441
    • Ghosh, M.1
  • 6
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • M. Ghosh Cofilin promotes actin polymerization and defines the direction of cell motility Science 304 2004 743 746
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1
  • 7
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • P.E. Dawson, and S.B. Kent Synthesis of native proteins by chemical ligation Annu. Rev. Biochem. 69 2000 923 960
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 8
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • T.W. Muir Semisynthesis of proteins by expressed protein ligation Annu. Rev. Biochem. 72 2003 249 289
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 9
    • 0034758469 scopus 로고    scopus 로고
    • Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling
    • W. Lu Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling Mol. Cell 8 2001 759 769
    • (2001) Mol. Cell , vol.8 , pp. 759-769
    • Lu, W.1
  • 10
    • 0344628799 scopus 로고    scopus 로고
    • Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation
    • W. Zheng Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation Nat. Struct. Biol. 10 2003 1054 1057
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1054-1057
    • Zheng, W.1
  • 11
    • 2942534048 scopus 로고    scopus 로고
    • Simultaneous triggering of protein activity and fluorescence
    • J.P. Pellois Simultaneous triggering of protein activity and fluorescence J. Am. Chem. Soc. 126 2004 7170 7171
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7170-7171
    • Pellois, J.P.1
  • 12
    • 8844266024 scopus 로고    scopus 로고
    • Photo-control of Smad2, a multi-phosphorylated cell signaling protein, through caging of activating phospho-serines
    • (in press)
    • Hahn, M.E. and Muir, T.W. Photo-control of Smad2, a multi-phosphorylated cell signaling protein, through caging of activating phospho-serines. Angew Chem., Int. Ed. Engl. (in press)
    • Angew Chem., Int. Ed. Engl.
    • Hahn, M.E.1    Muir, T.W.2
  • 13
    • 0034828385 scopus 로고    scopus 로고
    • Peptide chemical ligation inside living cells: In vivo generation of a circular protein domain
    • J.A. Camarero Peptide chemical ligation inside living cells: in vivo generation of a circular protein domain Bioorg. Med. Chem. 9 2001 2479 2484
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2479-2484
    • Camarero, J.A.1
  • 14
    • 0344874141 scopus 로고    scopus 로고
    • Cell-permeable small molecule probes for site-specific labeling of proteins
    • D.S. Yeo Cell-permeable small molecule probes for site-specific labeling of proteins Chem. Commun. 23 2003 2870 2871
    • (2003) Chem. Commun. , vol.23 , pp. 2870-2871
    • Yeo, D.S.1
  • 15
    • 0942287129 scopus 로고    scopus 로고
    • Versatile protein biotinylation strategies for potential high-throughput proteomics
    • R.Y. Lue Versatile protein biotinylation strategies for potential high-throughput proteomics J. Am. Chem. Soc. 126 2004 1055 1062
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1055-1062
    • Lue, R.Y.1
  • 16
    • 0037774580 scopus 로고    scopus 로고
    • Protein semi-synthesis in living cells
    • I. Giriat, and T.W. Muir Protein semi-synthesis in living cells J. Am. Chem. Soc. 125 2003 7180 7181
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 17
    • 0036902813 scopus 로고    scopus 로고
    • Creating new fluorescent probes for cell biology
    • J. Zhang Creating new fluorescent probes for cell biology Nat. Rev. Mol. Cell Biol. 3 2002 906 918
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 906-918
    • Zhang, J.1
  • 18
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • B.A. Griffin Specific covalent labeling of recombinant protein molecules inside live cells Science 281 1998 269 272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1
  • 19
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • S.R. Adams New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications J. Am. Chem. Soc. 124 2002 6063 6076
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1
  • 20
    • 10744232737 scopus 로고    scopus 로고
    • Activity-dependent regulation of dendritic synthesis and trafficking of AMPA receptors
    • W. Ju Activity-dependent regulation of dendritic synthesis and trafficking of AMPA receptors Nat. Neurosci. 7 2004 244 253
    • (2004) Nat. Neurosci. , vol.7 , pp. 244-253
    • Ju, W.1
  • 21
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • A. Keppler A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat. Biotechnol. 21 2003 86 89
    • (2003) Nat. Biotechnol. , vol.21 , pp. 86-89
    • Keppler, A.1
  • 22
    • 3042798464 scopus 로고    scopus 로고
    • Labeling of fusion proteins with synthetic fluorophores in live cells
    • A. Keppler Labeling of fusion proteins with synthetic fluorophores in live cells Proc. Natl. Acad. Sci. U. S. A. 101 2004 9955 9959
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9955-9959
    • Keppler, A.1
  • 23
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • J. Yin Labeling proteins with small molecules by site-specific posttranslational modification J. Am. Chem. Soc. 126 2004 7754 7755
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7754-7755
    • Yin, J.1
  • 24
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • N. George Specific labeling of cell surface proteins with chemically diverse compounds J. Am. Chem. Soc. 126 2004 8896 8897
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8896-8897
    • George, N.1
  • 25
    • 0032879690 scopus 로고    scopus 로고
    • Chromophore-assisted laser inactivation (CALI) to elucidate cellular mechanisms of cancer
    • D.G. Jay, and T. Sakurai Chromophore-assisted laser inactivation (CALI) to elucidate cellular mechanisms of cancer Biochim. Biophys. Acta 1424 1999 M39 M48
    • (1999) Biochim. Biophys. Acta , vol.1424
    • Jay, D.G.1    Sakurai, T.2
  • 26
    • 0037028010 scopus 로고    scopus 로고
    • Transgenically encoded protein photoinactivation (FlAsH-FALI): Acute inactivation of synaptotagmin I
    • K.W. Marek, and G.W. Davis Transgenically encoded protein photoinactivation (FlAsH-FALI): acute inactivation of synaptotagmin I Neuron 36 2002 805 813
    • (2002) Neuron , vol.36 , pp. 805-813
    • Marek, K.W.1    Davis, G.W.2
  • 27
    • 0347568469 scopus 로고    scopus 로고
    • Genetically targeted chromophore-assisted light inactivation
    • O. Tour Genetically targeted chromophore-assisted light inactivation Nat. Biotechnol. 21 2003 1505 1508
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1505-1508
    • Tour, O.1
  • 28
    • 0037829824 scopus 로고    scopus 로고
    • Spatiotemporal laser inactivation of inositol 1,4,5-trisphosphate receptors using synthetic small-molecule probes
    • T. Inoue Spatiotemporal laser inactivation of inositol 1,4,5-trisphosphate receptors using synthetic small-molecule probes Chem. Biol. 10 2003 503 509
    • (2003) Chem. Biol. , vol.10 , pp. 503-509
    • Inoue, T.1
  • 29
    • 0037033377 scopus 로고    scopus 로고
    • Expanding the genetic code
    • L. Wang, and P.G. Schultz Expanding the genetic code Chem. Commun. 1 2002 1 11
    • (2002) Chem. Commun. , vol.1 , pp. 1-11
    • Wang, L.1    Schultz, P.G.2
  • 30
    • 0038383546 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis in mapping ion channel function
    • D.L. Beene Unnatural amino acid mutagenesis in mapping ion channel function Curr. Opin. Neurobiol. 13 2003 264 270
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 264-270
    • Beene, D.L.1
  • 31
    • 0035807914 scopus 로고    scopus 로고
    • Import of amber and ochre suppressor tRNAs into mammalian cells: A general approach to site-specific insertion of amino acid analogues into proteins
    • C. Kohrer Import of amber and ochre suppressor tRNAs into mammalian cells: a general approach to site-specific insertion of amino acid analogues into proteins Proc. Natl. Acad. Sci. U. S. A. 98 2001 14310 14315
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14310-14315
    • Kohrer, C.1
  • 32
    • 0036885131 scopus 로고    scopus 로고
    • Monitoring mis-acylated tRNA suppression efficiency in mammalian cells via EGFP fluorescence recovery
    • E. Ilegems Monitoring mis-acylated tRNA suppression efficiency in mammalian cells via EGFP fluorescence recovery Nucleic Acids Res. 30 2002 e128
    • (2002) Nucleic Acids Res. , vol.30
    • Ilegems, E.1
  • 33
    • 0038506126 scopus 로고    scopus 로고
    • Site-specific incorporation of unnatural amino acids into receptors expressed in mammalian cells
    • S.L. Monahan Site-specific incorporation of unnatural amino acids into receptors expressed in mammalian cells Chem. Biol. 10 2003 573 580
    • (2003) Chem. Biol. , vol.10 , pp. 573-580
    • Monahan, S.L.1
  • 34
    • 0037471631 scopus 로고    scopus 로고
    • Generation of a bacterium with a 21 amino acid genetic code
    • R.A. Mehl Generation of a bacterium with a 21 amino acid genetic code J. Am. Chem. Soc. 125 2003 935 939
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 935-939
    • Mehl, R.A.1
  • 35
    • 0141732270 scopus 로고    scopus 로고
    • Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae
    • A. Deiters Adding amino acids with novel reactivity to the genetic code of Saccharomyces cerevisiae J. Am. Chem. Soc. 125 2003 11782 11783
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11782-11783
    • Deiters, A.1
  • 36
    • 0037462121 scopus 로고    scopus 로고
    • A fluorogenic dye activated by the Staudinger ligation
    • G.A. Lemieux A fluorogenic dye activated by the Staudinger ligation J. Am. Chem. Soc. 125 2003 4708 4709
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4708-4709
    • Lemieux, G.A.1
  • 37
    • 0036171482 scopus 로고    scopus 로고
    • Chemical approaches to the investigation of cellular systems
    • B.N. Cook, and C.R. Bertozzi 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
  • 38
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • J.A. Prescher Chemical remodelling of cell surfaces in living animals Nature 430 2004 873 877
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1
  • 39
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • H.C. Kolb Click chemistry: diverse chemical function from a few good reactions Angew. Chem., Int. Ed. Engl. 40 2001 2004 2021
    • (2001) Angew. Chem., Int. Ed. Engl. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1
  • 40
    • 0036849244 scopus 로고    scopus 로고
    • Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells
    • K. Sakamoto Site-specific incorporation of an unnatural amino acid into proteins in mammalian cells Nucleic Acids Res. 30 2002 4692 4699
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4692-4699
    • Sakamoto, K.1
  • 41
    • 0038265881 scopus 로고    scopus 로고
    • Progress toward an expanded eukaryotic genetic code
    • J.W. Chin Progress toward an expanded eukaryotic genetic code Chem. Biol. 10 2003 511 519
    • (2003) Chem. Biol. , vol.10 , pp. 511-519
    • Chin, J.W.1
  • 42
    • 2642553258 scopus 로고    scopus 로고
    • Target identification in chemical genetics: The (often) missing link
    • L. Burdine, and T. Kodadek Target identification in chemical genetics: the (often) missing link Chem. Biol. 11 2004 593 597
    • (2004) Chem. Biol. , vol.11 , pp. 593-597
    • Burdine, L.1    Kodadek, T.2
  • 43
    • 0023665149 scopus 로고
    • A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein
    • Y.W. Hwang, and D.L. Miller A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein J. Biol. Chem. 262 1987 13081 13085
    • (1987) J. Biol. Chem. , vol.262 , pp. 13081-13085
    • Hwang, Y.W.1    Miller, D.L.2
  • 44
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • T. Powers, and P. Walter Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases Science 269 1995 1422 1424
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 45
    • 33748226936 scopus 로고
    • Rational design of orthogonal receptor-ligand combinations
    • P.J. Belshaw Rational design of orthogonal receptor-ligand combinations Angew. Chem., Int. Ed. Engl. 34 1995 2129 2132
    • (1995) Angew. Chem., Int. Ed. Engl. , vol.34 , pp. 2129-2132
    • Belshaw, P.J.1
  • 46
  • 47
    • 0037134801 scopus 로고    scopus 로고
    • Functionally orthogonal ligand-receptor pairs for the selective regulation of gene expression generated by manipulation of charged residues at the ligand-receptor interface of ERα and ERβ
    • Y. Shi, and J.T. Koh Functionally orthogonal ligand-receptor pairs for the selective regulation of gene expression generated by manipulation of charged residues at the ligand-receptor interface of ERα and ERβ J. Am. Chem. Soc. 124 2002 6921 6928
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6921-6928
    • Shi, Y.1    Koh, J.T.2
  • 48
    • 0037388214 scopus 로고    scopus 로고
    • Inducible protein knockout reveals temporal requirement of CaMKII reactivation for memory consolidation in the brain
    • H. Wang Inducible protein knockout reveals temporal requirement of CaMKII reactivation for memory consolidation in the brain Proc. Natl. Acad. Sci. U. S. A. 100 2003 4287 4292
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4287-4292
    • Wang, H.1
  • 49
    • 0242300176 scopus 로고    scopus 로고
    • Targets of the cyclin-dependent kinase Cdk1
    • J.A. Ubersax Targets of the cyclin-dependent kinase Cdk1 Nature 425 2003 859 864
    • (2003) Nature , vol.425 , pp. 859-864
    • Ubersax, J.A.1
  • 50
    • 0037036791 scopus 로고    scopus 로고
    • Protein splicing triggered by a small molecule
    • H.D. Mootz, and T.W. Muir Protein splicing triggered by a small molecule J. Am. Chem. Soc. 124 2002 9044 9045
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9044-9045
    • Mootz, H.D.1    Muir, T.W.2
  • 51
    • 0041854719 scopus 로고    scopus 로고
    • Conditional protein splicing: A new tool to control protein structure and function in vitro and in vivo
    • H.D. Mootz Conditional protein splicing: a new tool to control protein structure and function in vitro and in vivo J. Am. Chem. Soc. 125 2003 10561 10569
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10561-10569
    • Mootz, H.D.1
  • 52
    • 6044271721 scopus 로고    scopus 로고
    • Activation of an autoregulated protein kinase by conditional protein splicing
    • H.D. Mootz Activation of an autoregulated protein kinase by conditional protein splicing Angew Chem., Int. Ed. Engl. 43 2004 5189 5192
    • (2004) Angew Chem., Int. Ed. Engl. , vol.43 , pp. 5189-5192
    • Mootz, H.D.1
  • 53
    • 3242694003 scopus 로고    scopus 로고
    • Directed evolution of ligand dependence: Small-molecule-activated protein splicing
    • A.R. Buskirk Directed evolution of ligand dependence: small-molecule-activated protein splicing Proc. Natl. Acad. Sci. U. S. A. 101 2004 10505 10510
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10505-10510
    • Buskirk, A.R.1
  • 54
    • 0346156074 scopus 로고    scopus 로고
    • Conditional protein alleles using knockin mice and a chemical inducer of dimerization
    • K. Stankunas Conditional protein alleles using knockin mice and a chemical inducer of dimerization Mol. Cell 12 2003 1615 1624
    • (2003) Mol. Cell , vol.12 , pp. 1615-1624
    • Stankunas, K.1
  • 55
    • 0035902475 scopus 로고    scopus 로고
    • Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation
    • K.M. Sakamoto Protacs: chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation Proc. Natl. Acad. Sci. U. S. A. 98 2001 8554 8559
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8554-8559
    • Sakamoto, K.M.1
  • 56
    • 1642343326 scopus 로고    scopus 로고
    • Chemical genetic control of protein levels: Selective in vivo targeted degradation
    • J.S. Schneekloth Jr Chemical genetic control of protein levels: selective in vivo targeted degradation J. Am. Chem. Soc. 126 2004 3748 3754
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3748-3754
    • Schneekloth Jr., J.S.1
  • 58
    • 0033568193 scopus 로고    scopus 로고
    • A fluorescent indicator for tyrosine phosphorylation-based insulin signaling pathways
    • M. Sato A fluorescent indicator for tyrosine phosphorylation-based insulin signaling pathways Anal. Chem. 71 1999 3948 3954
    • (1999) Anal. Chem. , vol.71 , pp. 3948-3954
    • Sato, M.1
  • 59
    • 0034177596 scopus 로고    scopus 로고
    • Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation
    • G.J. Cotton, and T.W. Muir Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation Chem. Biol. 7 2000 253 261
    • (2000) Chem. Biol. , vol.7 , pp. 253-261
    • Cotton, G.J.1    Muir, T.W.2
  • 60
    • 0037192839 scopus 로고    scopus 로고
    • Real time visualization of protein kinase activity in living cells
    • R.H. Yeh Real time visualization of protein kinase activity in living cells J. Biol. Chem. 277 2002 11527 11532
    • (2002) J. Biol. Chem. , vol.277 , pp. 11527-11532
    • Yeh, R.H.1
  • 61
    • 0344443386 scopus 로고    scopus 로고
    • Versatile fluorescence probes of protein kinase activity
    • M.D. Shults, and B. Imperiali Versatile fluorescence probes of protein kinase activity J. Am. Chem. Soc. 125 2003 14248 14249
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14248-14249
    • Shults, M.D.1    Imperiali, B.2
  • 62
    • 1542366681 scopus 로고    scopus 로고
    • Molecular recognition and fluorescence sensing of monophosphorylated peptides in aqueous solution by bis(zinc(II)-dipicolylamine)-based artificial receptors
    • A. Ojida Molecular recognition and fluorescence sensing of monophosphorylated peptides in aqueous solution by bis(zinc(II)-dipicolylamine)- based artificial receptors J. Am. Chem. Soc. 126 2004 2454 2463
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2454-2463
    • Ojida, A.1
  • 63
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • D.A. Jeffery, and M. Bogyo 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
  • 64
    • 0037397491 scopus 로고    scopus 로고
    • Functional profiling of the proteome with affinity labels
    • D.A. Campbell, and A.K. Szardenings 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
  • 65
    • 0036391485 scopus 로고    scopus 로고
    • Design and synthesis of class-selective activity probes for protein tyrosine phosphatases
    • L.C. Lo Design and synthesis of class-selective activity probes for protein tyrosine phosphatases J. Proteome Res. 1 2002 35 40
    • (2002) J. Proteome Res. , vol.1 , pp. 35-40
    • Lo, L.C.1
  • 66
    • 2542529285 scopus 로고    scopus 로고
    • Activity-based probes for protein tyrosine phosphatases
    • S. Kumar Activity-based probes for protein tyrosine phosphatases Proc. Natl. Acad. Sci. U. S. A. 101 2004 7943 7948
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7943-7948
    • Kumar, S.1
  • 67
    • 3242759075 scopus 로고    scopus 로고
    • Design and synthesis of AX7574: A microcystin-derived, fluorescent probe for serine/threonine phosphatases
    • K.R. Shreder Design and synthesis of AX7574: a microcystin-derived, fluorescent probe for serine/threonine phosphatases Bioconjug. Chem. 15 2004 790 798
    • (2004) Bioconjug. Chem. , vol.15 , pp. 790-798
    • Shreder, K.R.1
  • 68
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3+2] cycloaddition
    • A.E. Speers Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3+2] cycloaddition J. Am. Chem. Soc. 125 2003 4686 4687
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4686-4687
    • Speers, A.E.1
  • 69
    • 10744221240 scopus 로고    scopus 로고
    • Chemistry in living cells: Detection of active proteasomes by a two-step labeling strategy
    • H. Ovaa Chemistry in living cells: detection of active proteasomes by a two-step labeling strategy Angew. Chem. Int. Ed. Engl. 42 2003 3626 3629
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 3626-3629
    • Ovaa, H.1
  • 70
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • A.E. Speers, and B.F. Cravatt Profiling enzyme activities in vivo using click chemistry methods Chem. Biol. 11 2004 535 546
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.