메뉴 건너뛰기




Volumn 1, Issue 2, 2002, Pages 151-158

Activity-based probes for functional proteomics

Author keywords

Active site; Activity based probe; Affinity label; Electrophoresis; Enzyme; Proteomics

Indexed keywords

AFFINITY LABELING; ARTICLE; GENOMICS; PROTEOMICS;

EID: 3242808516     PISSN: 14739550     EISSN: 14774062     Source Type: Journal    
DOI: 10.1093/bfgp/1.2.151     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0034659898 scopus 로고    scopus 로고
    • Genomics, gene expression and DNA arrays
    • Lockhart, D. J., and Winzeler, E. A. (2000), 'Genomics, gene expression and DNA arrays', Nature, Vol. 405, pp. 827-836.
    • (2000) Nature , vol.405 , pp. 827-836
    • Lockhart, D.J.1    Winzeler, E.A.2
  • 2
    • 0034910345 scopus 로고    scopus 로고
    • Navigating gene expression using microarrays - A technology review
    • Schulze, A. and Downward, J. (2001), 'Navigating gene expression using microarrays - a technology review', Nat. Cell Biol., Vol. 3, pp. E190-195.
    • (2001) Nat. Cell Biol. , vol.3
    • Schulze, A.1    Downward, J.2
  • 3
    • 0031848226 scopus 로고    scopus 로고
    • Proteome and proteomics: New technologies, new concepts, and new words
    • Anderson, N. L. and Anderson, N. G. (1998), 'Proteome and proteomics: new technologies, new concepts, and new words', Electrophoresis, Vol. 19, pp. 1853-1861.
    • (1998) Electrophoresis , vol.19 , pp. 1853-1861
    • Anderson, N.L.1    Anderson, N.G.2
  • 4
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A. and Mann, M. (2000), 'Proteomics to study genes and genomes', Nature, Vol. 405, pp. 837-846.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 5
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • Corthals, G. L., Wasinger, V. C, Hochstrasser, D. F. and Sanchez, J. C. (2000), The dynamic range of protein expression: a challenge for proteomic research', Electrophoresis, Vol. 21, pp. 1104-1115.
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Corthals, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 6
    • 0033772588 scopus 로고    scopus 로고
    • Mass spectrometry and proteomics
    • Gygi, S. P. and Aebersold, R. (2000), 'Mass spectrometry and proteomics', Curr. Opin. Chem. Biol, Vol. 4, pp. 489-494.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 489-494
    • Gygi, S.P.1    Aebersold, R.2
  • 7
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson, L. and Seilhamer, J. (1997), 'A comparison of selected mRNA and protein abundances in human liver', Electrophoresis, Vol. 18, pp. 533-537.
    • (1997) Electrophoresis , vol.18 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 8
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S. P., Rochon, Y., Franza, B. R. and Aebersold, R. (1999), 'Correlation between protein and mRNA abundance in yeast', Mol. Cell Biol, Vol. 19, pp. 1720-1730.
    • (1999) Mol. Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 9
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter, T. (1995), 'Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling', Cell Vol. 80, 225-236.
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 10
    • 0033604499 scopus 로고    scopus 로고
    • Active site-directed protein regulation
    • Kobe, B. and Kemp, B. E. (1999), 'Active site-directed protein regulation', Nature, Vol. 402, pp. 373-376.
    • (1999) Nature , vol.402 , pp. 373-376
    • Kobe, B.1    Kemp, B.E.2
  • 11
    • 0033636862 scopus 로고    scopus 로고
    • Chemical strategies for the global analysis of protein function
    • Cravatt, B. F. and Sorensen, E.J. (2000), 'Chemical strategies for the global analysis of protein function', Curr. Opin. Chem. Biol., Vol. 4, pp. 663-668.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 663-668
    • Cravatt, B.F.1    Sorensen, E.J.2
  • 12
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • Liu, Y., Patricelli, M. P. and Cravatt, B. F. (1999), 'Activity-based protein profiling: the serine hydrolases', Proc. Natl. Acad. Sci. USA, Vol. 96, pp. 14694-14699.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 13
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum, D., Medzihradszky, K. F., Burlingame, A. and Bogyo, M. (2000), 'Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools', Chem. Biol, Vol. 7, pp. 569-581.
    • (2000) Chem. Biol , vol.7 , pp. 569-581
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 14
    • 0030973417 scopus 로고    scopus 로고
    • Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells
    • Faleiro, L., Kobayashi, R., Fearnhead, H. and Lazebmk, Y. (1997), 'Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells', Embo J., Vol. 16, pp. 2271-2281.
    • (1997) Embo J. , vol.16 , pp. 2271-2281
    • Faleiro, L.1    Kobayashi, R.2    Fearnhead, H.3    Lazebmk, Y.4
  • 15
    • 0032211157 scopus 로고    scopus 로고
    • Phosphorylated forms of activated caspases are present in cytosol from HL-60 cells during etoposide-induced apoptosis
    • Martins, L. M., Kottke, T. J., Kaufmann, S. H. and Earnshaw, W. C. (1998), 'Phosphorylated forms of activated caspases are present in cytosol from HL-60 cells during etoposide-induced apoptosis', Blood, Vol. 92, pp. 3042-3049.
    • (1998) Blood , vol.92 , pp. 3042-3049
    • Martins, L.M.1    Kottke, T.J.2    Kaufmann, S.H.3    Earnshaw, W.C.4
  • 16
    • 0035818888 scopus 로고    scopus 로고
    • Novel tropane-based irreversible ligands for the dopamine transporter
    • Zou, M. F., Kopajtic, T., Katz, J. L. et al. (2001), 'Novel tropane-based irreversible ligands for the dopamine transporter', J. Med. Chem., Vol. 44, pp. 4453-4461.
    • (2001) J. Med. Chem. , vol.44 , pp. 4453-4461
    • Zou, M.F.1    Kopajtic, T.2    Katz, J.L.3
  • 17
    • 0034687249 scopus 로고    scopus 로고
    • Synthesis and evaluation of N,N-dialkyl enkephalin-based affinity labels for delta opioid receptors
    • Maeda, D. Y., Ishmael, J. E., Murray, T. F. and Aldrich, J. V. (2000), 'Synthesis and evaluation of N,N-dialkyl enkephalin-based affinity labels for delta opioid receptors', J. Med. Chem., Vol. 43, pp. 3941-3948.
    • (2000) J. Med. Chem. , vol.43 , pp. 3941-3948
    • Maeda, D.Y.1    Ishmael, J.E.2    Murray, T.F.3    Aldrich, J.V.4
  • 18
    • 0034070580 scopus 로고    scopus 로고
    • Use of a novel impermeable biotinylated photolabeling reagent to assess insulin- and hypoxia-stimulated cell surface GLUT4 content in skeletal muscle from type 2 diabetic patients
    • Ryder, J. W., Yang, J., Galuska, D. et al. (2000), 'Use of a novel impermeable biotinylated photolabeling reagent to assess insulin- and hypoxia-stimulated cell surface GLUT4 content in skeletal muscle from type 2 diabetic patients', Diabetes, Vol. 49, pp. 647-654.
    • (2000) Diabetes , vol.49 , pp. 647-654
    • Ryder, J.W.1    Yang, J.2    Galuska, D.3
  • 19
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd, D., Liu, Y. and Cravatt, B. F. (2001), 'Profiling serine hydrolase activities in complex proteomes', Biochemistry, Vol. 40, pp. 4005-4015.
    • (2001) Biochemistry , vol.40 , pp. 4005-4015
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 20
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes
    • Patricelli, M. P., Giang, D. K., Stamp, L. M. and Burbaum, J. J. (2001), 'Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes', Proteomics, Vol. 1, pp. 1067-1071.
    • (2001) Proteomics , vol.1 , pp. 1067-1071
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 21
    • 0028179134 scopus 로고
    • Inactivation of interleukin-1 beta converting enzyme by peptide (acyloxy)methyl ketones
    • Thornberry, N. A., Peterson, E. P., Zhao, J. J., Howard, A. D., Griffin, P. R. and Chapman, K. T. (1994), 'Inactivation of interleukin-1 beta converting enzyme by peptide (acyloxy)methyl ketones', Biochemistry, Vol. 33, pp. 3934-3940.
    • (1994) Biochemistry , vol.33 , pp. 3934-3940
    • Thornberry, N.A.1    Peterson, E.P.2    Zhao, J.J.3    Howard, A.D.4    Griffin, P.R.5    Chapman, K.T.6
  • 22
    • 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., Vol. 7, pp. 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
  • 23
    • 0035113229 scopus 로고    scopus 로고
    • Profiling the specific reactivity of the proteome with non-directed activity-based probes
    • Adam, G. C, Cravatt, B. F. and Sorensen, E.J. (2001), 'Profiling the specific reactivity of the proteome with non-directed activity-based probes', Chem. Biol., Vol. 8, pp. 81-95.
    • (2001) Chem. Biol. , vol.8 , pp. 81-95
    • Adam, G.C.1    Cravatt, B.F.2    Sorensen, E.J.3
  • 24
    • 0028063448 scopus 로고
    • Photoaffinity labeling of rat liver microsomal steroid 5 alpha-reductase by 2-azido-NADP+
    • Bhattacharyya, A. K., Chavan, A. J., Shuffett, M., Haley, B. E. and Collins, D. C. (1994), 'Photoaffinity labeling of rat liver microsomal steroid 5 alpha-reductase by 2-azido-NADP+', Steroids, Vol. 59, pp. 634-641.
    • (1994) Steroids , vol.59 , pp. 634-641
    • Bhattacharyya, A.K.1    Chavan, A.J.2    Shuffett, M.3    Haley, B.E.4    Collins, D.C.5
  • 25
    • 0032030854 scopus 로고    scopus 로고
    • Abnormal properties of creatine kinase in Alzheimer's disease brain: Correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning
    • David, S., Shoemaker, M. and Haley, B. E. (1998), 'Abnormal properties of creatine kinase in Alzheimer's disease brain: correlation of reduced enzyme activity and active site photolabeling with aberrant cytosol-membrane partitioning', Brain Res. Mol. Brain Res., Vol. 54, pp. 276-287.
    • (1998) Brain Res. Mol. Brain Res. , vol.54 , pp. 276-287
    • David, S.1    Shoemaker, M.2    Haley, B.E.3
  • 26
    • 0035800832 scopus 로고    scopus 로고
    • Defining a link between gap junction communication, proteolysis, and cataract formation
    • Baruch, A., Greenbaum, D., Levy, E. T. et al. (2001), 'Defining a link between gap junction communication, proteolysis, and cataract formation', J. Biol. Chem., Vol. 276, pp. 28999-29006.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28999-29006
    • Baruch, A.1    Greenbaum, D.2    Levy, E.T.3
  • 28
    • 0033520099 scopus 로고    scopus 로고
    • Chemical and mutagenic investigations of fatty acid amide hydrolase: Evidence for a family of serine hydrolases with distinct catalytic properties
    • Patricelli, M. P., Lovato, M. A. and Cravatt, B. F. (1999), 'Chemical and mutagenic investigations of fatty acid amide hydrolase: evidence for a family of serine hydrolases with distinct catalytic properties', Biochemistry, Vol. 38, pp. 9804-9812.
    • (1999) Biochemistry , vol.38 , pp. 9804-9812
    • Patricelli, M.P.1    Lovato, M.A.2    Cravatt, B.F.3
  • 30
    • 0019948262 scopus 로고
    • L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett, A. J., Kembhavi, A. A., Brown, M. A. et al. (1982), 'L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L', Biochem. J., Vol. 201, pp. 189-198.
    • (1982) Biochem. J. , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3
  • 31
    • 0029094754 scopus 로고
    • Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1
    • Goldberg, J., Huang, H. B., Kwon, Y. G., Greengard, P., Nairn, A. C. and Kuriyan, J. (1995), 'Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1'. Nature, Vol. 376, pp. 745-753.
    • (1995) Nature , vol.376 , pp. 745-753
    • Goldberg, J.1    Huang, H.B.2    Kwon, Y.G.3    Greengard, P.4    Nairn, A.C.5    Kuriyan, J.6
  • 32
    • 0032514659 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase
    • Lowther, W. T., McMillen, D. A., Orville, A. M. and Matthews, B. W. (1998), 'The anti-angiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase', Proc. Natl. Acad. Sci. USA, Vol. 95, pp. 12153-12157.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12153-12157
    • Lowther, W.T.1    McMillen, D.A.2    Orville, A.M.3    Matthews, B.W.4
  • 33
    • 0033634827 scopus 로고    scopus 로고
    • Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine
    • Walker, E. H., Pacold, M. E., Perisic, O. et al. (2000), 'Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine', Mol. Cell., Vol. 6, pp. 909-919.
    • (2000) Mol. Cell. , vol.6 , pp. 909-919
    • Walker, E.H.1    Pacold, M.E.2    Perisic, O.3
  • 34
    • 0030932349 scopus 로고    scopus 로고
    • Chemical arrows for enzymatic targets
    • Colman, R. F. (1997), 'Chemical arrows for enzymatic targets', FASEB J., Vol. 11, pp. 217-226.
    • (1997) FASEB J. , vol.11 , pp. 217-226
    • Colman, R.F.1
  • 35
    • 0026349175 scopus 로고
    • Nucleotide photoaffinity labeling of protein kinase subunits
    • Haley, B. E. (1991), 'Nucleotide photoaffinity labeling of protein kinase subunits', Methods Enzymol., Vol. 200, pp. 477-487.
    • (1991) Methods Enzymol. , vol.200 , pp. 477-487
    • Haley, B.E.1
  • 36
    • 0031009863 scopus 로고    scopus 로고
    • A comparison of changes in nucleotide-protein interactions in the striatal, hippocampus and paramedian cortex after cerebral ischemia and reperfusion: Correlations to regional vulnerability
    • Sankaran, B., Clemens, J. and Haley, B. E. (1997), 'A comparison of changes in nucleotide-protein interactions in the striatal, hippocampus and paramedian cortex after cerebral ischemia and reperfusion: correlations to regional vulnerability', Brain Res. Mol. Brain Res., Vol. 47, pp. 237-250.
    • (1997) Brain Res. Mol. Brain Res. , vol.47 , pp. 237-250
    • Sankaran, B.1    Clemens, J.2    Haley, B.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.