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Volumn 5, Issue 3, 2008, Pages 200-212

Activity based chemical proteomics: Profiling proteases as drug targets

Author keywords

Activity based probes; Cleavable linker; Click chemistry; Drug targets; Protease; Proteomics; Solid phase synthesis; Target validation

Indexed keywords

CYSTEINE PROTEINASE; METALLOPROTEINASE; PROTEINASE; SERINE PROTEINASE; THREONINE PROTEINASE;

EID: 51349154761     PISSN: 15701638     EISSN: None     Source Type: Journal    
DOI: 10.2174/157016308785739866     Document Type: Review
Times cited : (21)

References (69)
  • 1
  • 2
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics
    • Yasuda Y., Kaleta J., Bromme D.: The role of cathepsins in osteoporosis and arthritis: Rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 57(7), 973, (2005).
    • (2005) Adv. Drug Deliv. Rev , vol.57 , Issue.7 , pp. 973
    • Yasuda, Y.1    Kaleta, J.2    Bromme, D.3
  • 3
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski J.E., Ahram M., Sloane B.F.: Unraveling the role of proteases in cancer. Clin. Chim. Acta 291(2), 113, (2000).
    • (2000) Clin. Chim. Acta , vol.291 , Issue.2 , pp. 113
    • Koblinski, J.E.1    Ahram, M.2    Sloane, B.F.3
  • 4
    • 0038040768 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors for cancer therapy: The current situation and future prospects
    • Fingleton B.: Matrix metalloproteinase inhibitors for cancer therapy: the current situation and future prospects. Exp. Opin. Therap. Targets 7(3), 385, (2003).
    • (2003) Exp. Opin. Therap. Targets , vol.7 , Issue.3 , pp. 385
    • Fingleton, B.1
  • 5
    • 0142165164 scopus 로고    scopus 로고
    • Functional genomics: Identifying drug targets for parasitic diseases
    • Cowman A.F., Crabb B.S.: Functional genomics: identifying drug targets for parasitic diseases. Trends Parasitol. 19(11), 538, (2003).
    • (2003) Trends Parasitol , vol.19 , Issue.11 , pp. 538
    • Cowman, A.F.1    Crabb, B.S.2
  • 6
    • 0038184354 scopus 로고    scopus 로고
    • HIV-1 protease: Mechanism and drug discovery
    • Brik A., Wong C.H.: HIV-1 protease: mechanism and drug discovery. Org. Biomol. Chem. 1(1), 5, (2003).
    • (2003) Org. Biomol. Chem , vol.1 , Issue.1 , pp. 5
    • Brik, A.1    Wong, C.H.2
  • 8
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • Liu Y., Patricelli M.P., Cravatt B.F.: Activity-based protein profiling: The serine hydrolases. Proc. Natl. Acad. Sci. USA 96(26), 14694, (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.26 , pp. 14694
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 9
    • 33846649707 scopus 로고    scopus 로고
    • Activity-based probes for proteomic profiling of histone deacetylase complexes
    • Salisbury C.M., Cravatt B.F.: Activity-based probes for proteomic profiling of histone deacetylase complexes. Proc. Natl. Acad. Sci. USA 104(4), 1171, (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.4 , pp. 1171
    • Salisbury, C.M.1    Cravatt, B.F.2
  • 10
    • 33846167705 scopus 로고    scopus 로고
    • Activity Based Probes for Proteases: Applications to Biomarker Discovery, Molecular Imaging and Drug Screening
    • Fonović M., Bogyo M.: Activity Based Probes for Proteases: Applications to Biomarker Discovery, Molecular Imaging and Drug Screening. Curr. Pharm. Des. 13(1), 253, (2007).
    • (2007) Curr. Pharm. Des , vol.13 , Issue.1 , pp. 253
    • Fonović, M.1    Bogyo, M.2
  • 12
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases
    • Powers J.C., Asgian J.L., Ekici O.D., James K.E.: Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases Chem. Rev. 102(12), 4639, (2002).
    • (2002) Chem. Rev , vol.102 , Issue.12 , pp. 4639
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 13
    • 0036753558 scopus 로고    scopus 로고
    • In situ activation of caspases and serine proteases during apoptosis detected by affinity labeling their enzyme active centers with fluorochrome-tagged inhibitors
    • Grabareka J., Darzynkiewicz Z.: In situ activation of caspases and serine proteases during apoptosis detected by affinity labeling their enzyme active centers with fluorochrome-tagged inhibitors. Exp. Hematol. 30(9), 982, (2002).
    • (2002) Exp. Hematol , vol.30 , Issue.9 , pp. 982
    • Grabareka, J.1    Darzynkiewicz, Z.2
  • 14
    • 0026637970 scopus 로고
    • Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinases
    • Bock P.E.: Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinases. J. Biol. Chem. 267(21), 14974, (1992).
    • (1992) J. Biol. Chem , vol.267 , Issue.21 , pp. 14974
    • Bock, P.E.1
  • 15
    • 0026729111 scopus 로고
    • Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labeling
    • Bock P.E.: Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labeling. J. Biol. Chem. 267(21), 14963, (1992).
    • (1992) J. Biol. Chem , vol.267 , Issue.21 , pp. 14963
    • Bock, P.E.1
  • 16
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal b subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    • Bogyo M., McMaster J.S., Gaczynska M., Tortorella D., Goldberg A.L., Ploegh H.L.: Covalent modification of the active site threonine of proteasomal b subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94(1), 6629, (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.1 , pp. 6629
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.L.6
  • 17
    • 0034054576 scopus 로고    scopus 로고
    • Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs
    • Bogyo M., Verhelst S.H.L., Bellingard-Dubouchaud V., Toba S., Greenbaum D.: Selective targeting of lysosomal cysteine proteases with radiolabeled electrophilic substrate analogs. Chem. Biol. 7(1), 27, (2000).
    • (2000) Chem. Biol , vol.7 , Issue.1 , pp. 27
    • Bogyo, M.1    Verhelst, S.H.L.2    Bellingard-Dubouchaud, V.3    Toba, S.4    Greenbaum, D.5
  • 18
    • 21044447609 scopus 로고    scopus 로고
    • Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases
    • Verhelst S.H.L., Bogyo M.: Solid-phase synthesis of double-headed epoxysuccinyl activity-based probes for selective targeting of papain family cysteine proteases. Chem. Bio. Chem. 6(5), 824, (2005).
    • (2005) Chem. Bio. Chem , vol.6 , Issue.5 , pp. 824
    • Verhelst, S.H.L.1    Bogyo, M.2
  • 19
    • 18844466768 scopus 로고    scopus 로고
    • Identification of various lipolytic enzymes in crude porcine pancreatic lipase preparations using covalent fluorescent inhibitors
    • Birner-Grünberger R., Scholze H., Faber K., Hermetter A.: Identification of various lipolytic enzymes in crude porcine pancreatic lipase preparations using covalent fluorescent inhibitors. Biotechnol. Bioeng. 85(2). 147, (2004).
    • (2004) Biotechnol. Bioeng , vol.85 , Issue.2 , pp. 147
    • Birner-Grünberger, R.1    Scholze, H.2    Faber, K.3    Hermetter, A.4
  • 20
    • 18044378410 scopus 로고    scopus 로고
    • Class assignment of sequence-unrelated members of enzyme supetfamilies by activity-based protein profiling
    • Jessani N., Young J.A., Diaz S.L., Patricelli M.P., Varki A., Cravatt B.F.: Class assignment of sequence-unrelated members of enzyme supetfamilies by activity-based protein profiling. Angew. Chem. Int. Edit. 44(16), 2400, (2005).
    • (2005) Angew. Chem. Int. Edit , vol.44 , Issue.16 , pp. 2400
    • Jessani, N.1    Young, J.A.2    Diaz, S.L.3    Patricelli, M.P.4    Varki, A.5    Cravatt, B.F.6
  • 21
    • 0031660899 scopus 로고    scopus 로고
    • Eponemycin Analogues: Syntheses and use as Probes of Angiogenesis
    • Sin N., Meng L., Auth H., Crews C.M.: Eponemycin Analogues: Syntheses and use as Probes of Angiogenesis. Bioorg. Med. Chem. 6(1), 1209, (1998).
    • (1998) Bioorg. Med. Chem , vol.6 , Issue.1 , pp. 1209
    • Sin, N.1    Meng, L.2    Auth, H.3    Crews, C.M.4
  • 22
    • 0035801347 scopus 로고    scopus 로고
    • From split-pool libraries to spatially addressable microarrays and its application to functional proteomic profiling
    • Winssinger N., Hams J.L., Backes B.J., Schultz P.G.: From split-pool libraries to spatially addressable microarrays and its application to functional proteomic profiling. Angew. Chem. Int. Edit. 40(17), 3152, (2001).
    • (2001) Angew. Chem. Int. Edit , vol.40 , Issue.17 , pp. 3152
    • Winssinger, N.1    Hams, J.L.2    Backes, B.J.3    Schultz, P.G.4
  • 23
    • 33749076305 scopus 로고    scopus 로고
    • Dual colour, microarray-based, analysis of 10 000 protease substrates
    • Diaz-Mochon J.J., Bialy L., Bradley M.: Dual colour, microarray-based, analysis of 10 000 protease substrates. Chem. Commun. 38(38), 3984, (2006).
    • (2006) Chem. Commun , vol.38 , Issue.38 , pp. 3984
    • Diaz-Mochon, J.J.1    Bialy, L.2    Bradley, M.3
  • 24
    • 33745104981 scopus 로고    scopus 로고
    • Activity-based proteomics: Enzymatic activity profiling in complex proteomes
    • Schmidinger H., Hermetter A., Birner-Gruenberger R.: Activity-based proteomics: enzymatic activity profiling in complex proteomes. Amino Acids 30(4), 333, (2006).
    • (2006) Amino Acids , vol.30 , Issue.4 , pp. 333
    • Schmidinger, H.1    Hermetter, A.2    Birner-Gruenberger, R.3
  • 25
    • 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., Burbaum J.J.: Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes. Proteomics 1(9), 1067, (2001).
    • (2001) Proteomics , vol.1 , Issue.9 , pp. 1067
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 26
    • 32044461510 scopus 로고    scopus 로고
    • Fluorescent labels for proteomics and genomics
    • Waggoner A.: Fluorescent labels for proteomics and genomics. Curr. Opin. Chem. Biol. 10(1), 62, (2006).
    • (2006) Curr. Opin. Chem. Biol , vol.10 , Issue.1 , pp. 62
    • Waggoner, A.1
  • 27
    • 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., Aebersold R.: Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotech. 17(10), 994, (1999).
    • (1999) Nat. Biotech , vol.17 , Issue.10 , pp. 994
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 28
    • 0036246088 scopus 로고    scopus 로고
    • Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry
    • Zhou H.L., Ranish J.A., Watts J.D., Aebersold R.: Quantitative proteome analysis by solid-phase isotope tagging and mass spectrometry. Nat. Biotech. 20(5), 512, (2002).
    • (2002) Nat. Biotech , vol.20 , Issue.5 , pp. 512
    • Zhou, H.L.1    Ranish, J.A.2    Watts, J.D.3    Aebersold, R.4
  • 29
    • 0025288944 scopus 로고
    • Avidin and Streptavidin
    • Green N.M.: Avidin and Streptavidin. Methods Enz. 184(1), 51, (1990).
    • (1990) Methods Enz , vol.184 , Issue.1 , pp. 51
    • Green, N.M.1
  • 30
    • 34247273992 scopus 로고    scopus 로고
    • A mild chemically cleavable linker system for functional proteomic applications
    • Verhelst S.H.L., Fonović M., Bogyo M.: A mild chemically cleavable linker system for functional proteomic applications. Angew. Chem. Int. Edit. 46(8), 1284, (2007).
    • (2007) Angew. Chem. Int. Edit , vol.46 , Issue.8 , pp. 1284
    • Verhelst, S.H.L.1    Fonović, M.2    Bogyo, M.3
  • 31
    • 22244445882 scopus 로고    scopus 로고
    • A Tandem Orthogonal Proteolysis Strategy for High-Content Chemical Proteomics
    • Speers A.E., Cravatt B.F.: A Tandem Orthogonal Proteolysis Strategy for High-Content Chemical Proteomics. J. Am. Chem. Soc. 127(28), 10018, (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , Issue.28 , pp. 10018
    • Speers, A.E.1    Cravatt, B.F.2
  • 33
    • 29444440825 scopus 로고    scopus 로고
    • A general solid phase method for the preparation of diverse azapeptide probes directed against cysteine proteases
    • Kato D., Verhelst S.H.L., Sexton K.B., Bogyo M.: A general solid phase method for the preparation of diverse azapeptide probes directed against cysteine proteases. Org. Lett. 7(25), 5649, (2005).
    • (2005) Org. Lett , vol.7 , Issue.25 , pp. 5649
    • Kato, D.1    Verhelst, S.H.L.2    Sexton, K.B.3    Bogyo, M.4
  • 34
    • 0000096835 scopus 로고    scopus 로고
    • Click Chemistry: Diverse Chemical Function from a Few Good Reactions
    • Kolb H.C., Finn M.G., Sharpless K.B.: Click Chemistry: Diverse Chemical Function from a Few Good Reactions. Angew. Chem. Int. Edit. 40(11), 2004, (2001).
    • (2001) Angew. Chem. Int. Edit , vol.40 , Issue.11 , pp. 2004
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 35
    • 0037462106 scopus 로고    scopus 로고
    • Speers A.E., Adam G.C., Cravatt B.F.: Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125(1), 4686, (2003).
    • Speers A.E., Adam G.C., Cravatt B.F.: Activity-based protein profiling in vivo using a copper(i)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125(1), 4686, (2003).
  • 36
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers A.E., Cravatt B.F.: Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11(4), 535, (2004).
    • (2004) Chem. Biol , vol.11 , Issue.4 , pp. 535
    • Speers, A.E.1    Cravatt, B.F.2
  • 37
    • 0034677879 scopus 로고    scopus 로고
    • Saxon E., Bertozzi C.R.: Cell surface engineering by a modifed staudinger reaction. Science 287(2007), 2007, (2000).
    • Saxon E., Bertozzi C.R.: Cell surface engineering by a modifed staudinger reaction. Science 287(2007), 2007, (2000).
  • 40
    • 0035799319 scopus 로고    scopus 로고
    • Profiling serine hydrolase activities in complex proteomes
    • Kidd D., Liu Y., Cravatt B.F.: Profiling serine hydrolase activities in complex proteomes. Biochemistry 40(1), 4005, (2001).
    • (2001) Biochemistry , vol.40 , Issue.1 , pp. 4005
    • Kidd, D.1    Liu, Y.2    Cravatt, B.F.3
  • 42
    • 0032103006 scopus 로고    scopus 로고
    • Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
    • Bogyo M., Shin S., McMaster J.S., Ploegh H.L.: Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 5(1), 307, (1998).
    • (1998) Chem. Biol , vol.5 , Issue.1 , pp. 307
    • Bogyo, M.1    Shin, S.2    McMaster, J.S.3    Ploegh, H.L.4
  • 43
    • 0034819479 scopus 로고    scopus 로고
    • Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits
    • Kessler B.M., Tortorella D., Altun M., Kisselev A.F., Fiebiger E., Hekking B.G., Ploegh H.L., Overkleeft H.S.: Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits. Chem. Biol. 8(9). 913, (2001).
    • (2001) Chem. Biol , vol.8 , Issue.9 , pp. 913
    • Kessler, B.M.1    Tortorella, D.2    Altun, M.3    Kisselev, A.F.4    Fiebiger, E.5    Hekking, B.G.6    Ploegh, H.L.7    Overkleeft, H.S.8
  • 45
    • 1542604677 scopus 로고    scopus 로고
    • Cysteine proteases as disease markers
    • Berdowska I.: Cysteine proteases as disease markers. Clin. Chim. Acta 342(1-2), 41, (2004).
    • (2004) Clin. Chim. Acta , vol.342 , Issue.1-2 , pp. 41
    • Berdowska, I.1
  • 46
    • 0036931366 scopus 로고    scopus 로고
    • Caspases: Keys in the ignition of cell death
    • Denault J.B., Salvesen G.S.: Caspases: Keys in the ignition of cell death. Chem. Rev. 102(12), 4489, (2002).
    • (2002) Chem. Rev , vol.102 , Issue.12 , pp. 4489
    • Denault, J.B.1    Salvesen, G.S.2
  • 47
    • 0033835372 scopus 로고    scopus 로고
    • Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools
    • Greenbaum D., Medzihradszky K.F., Burlingame A., Bogyo M.: Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools. Chem. Biol. 7(1), 569, (2000).
    • (2000) Chem. Biol , vol.7 , Issue.1 , pp. 569
    • Greenbaum, D.1    Medzihradszky, K.F.2    Burlingame, A.3    Bogyo, M.4
  • 49
    • 33646594411 scopus 로고    scopus 로고
    • Yuan F., Verhelst S.H.L., Blum G., Coussens L.M., Bogyo M.: A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I cathepsin C. J. Am. Chem. Soc. 128(17), 5616, (2006).
    • Yuan F., Verhelst S.H.L., Blum G., Coussens L.M., Bogyo M.: A selective activity-based probe for the papain family cysteine protease dipeptidyl peptidase I cathepsin C. J. Am. Chem. Soc. 128(17), 5616, (2006).
  • 52
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A., Ewald A.J., Werb Z.: Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 8(3), 221, (2007).
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , Issue.3 , pp. 221
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 53
    • 0035500490 scopus 로고    scopus 로고
    • The many faces of metalloproteases: Cell growth, invasion, angiogenesis and metastasis
    • Chang C., Werb Z.: The many faces of metalloproteases: cell growth, invasion, angiogenesis and metastasis. Trends Cell Biol. 11(11), 37, (2001).
    • (2001) Trends Cell Biol , vol.11 , Issue.11 , pp. 37
    • Chang, C.1    Werb, Z.2
  • 55
    • 7744233875 scopus 로고    scopus 로고
    • Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases
    • Chan E.W., Chattopadhaya S., Huang X.: Developing photoactive affinity probes for proteomic profiling: hydroxamate-based probes for metalloproteases. J. Am. Chem. Soc. 126(44), 14435, (2004 ).
    • (2004) J. Am. Chem. Soc , vol.126 , Issue.44 , pp. 14435
    • Chan, E.W.1    Chattopadhaya, S.2    Huang, X.3
  • 56
    • 33646462162 scopus 로고    scopus 로고
    • Proteomic profiling of metalloprotease activities with cocktails of active-site probes
    • Sieber S.A., Niessen S., Hoover H.S., Cravatt B.F.: Proteomic profiling of metalloprotease activities with cocktails of active-site probes. Nat. Chem. Biol. 2(5), 274, (2006).
    • (2006) Nat. Chem. Biol , vol.2 , Issue.5 , pp. 274
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 57
    • 33748701072 scopus 로고    scopus 로고
    • Click synthesis of small molecule probes for activity-based fingerprinting of matrix metalloproteases
    • Wang J., Uttamchandani M., Li J.Q., Hu M.Y., Yao S.Q.: "Click" synthesis of small molecule probes for activity-based fingerprinting of matrix metalloproteases. Chem. Commun. 2006(36), 3783, (2006).
    • (2006) Chem. Commun. 2006 , vol.36 , pp. 3783
    • Wang, J.1    Uttamchandani, M.2    Li, J.Q.3    Hu, M.Y.4    Yao, S.Q.5
  • 58
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome thai depict cancer cell invasiveness
    • Jessani N., Liu Y., Humphrey M., Cravatt B.F.: Enzyme activity profiles of the secreted and membrane proteome thai depict cancer cell invasiveness. Proc. Natl. Acad. Sci. USA 99(16), 10335, (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.16 , pp. 10335
    • Jessani, N.1    Liu, Y.2    Humphrey, M.3    Cravatt, B.F.4
  • 59
    • 0041737535 scopus 로고    scopus 로고
    • Molecular mechanisms of glioma invasiveness: The role of proteases
    • Rao J.S.: Molecular mechanisms of glioma invasiveness: the role of proteases. Nat. Rev. Cancer 3(7), 489, (2003).
    • (2003) Nat. Rev. Cancer , vol.3 , Issue.7 , pp. 489
    • Rao, J.S.1
  • 60
    • 2342603891 scopus 로고    scopus 로고
    • Joyce J.A., Baruch A., Chehade K., Meyer-Morse N., Giraudo E., Tsai F.-Y., Greenbaum D., Hager j.H., et al.: Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5(5), 443, (2004).
    • Joyce J.A., Baruch A., Chehade K., Meyer-Morse N., Giraudo E., Tsai F.-Y., Greenbaum D., Hager j.H., et al.: Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5(5), 443, (2004).
  • 61
    • 34548409606 scopus 로고    scopus 로고
    • Drug-resistant malaria - an insight
    • Hyde J.E.: Drug-resistant malaria - an insight. FEBS J 274(18), 4688, (2007).
    • (2007) FEBS J , vol.274 , Issue.18 , pp. 4688
    • Hyde, J.E.1
  • 62
    • 34548126497 scopus 로고    scopus 로고
    • Drug discovery for malaria: A very challenging and timely endeavor
    • Gelb M.H.: Drug discovery for malaria: a very challenging and timely endeavor. Curr. Opin. Chem. Biol. 11(4), 440, (2007).
    • (2007) Curr. Opin. Chem. Biol , vol.11 , Issue.4 , pp. 440
    • Gelb, M.H.1
  • 63
    • 25144497589 scopus 로고    scopus 로고
    • Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe
    • Florent I., Lecaille F., Montagne J.-J., Gauthier F., Schrevel J., Lalmanach G.: Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe. Biol. Chem. 386(4), 401, (2005).
    • (2005) Biol. Chem , vol.386 , Issue.4 , pp. 401
    • Florent, I.1    Lecaille, F.2    Montagne, J.-J.3    Gauthier, F.4    Schrevel, J.5    Lalmanach, G.6
  • 65
    • 0029816035 scopus 로고    scopus 로고
    • Biotinlabelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: Targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi
    • Lalmanach G., Mayer R., Serveau C., Scharfstein J., Gauthier F.: Biotinlabelled peptidyl diazomethane inhibitors derived from the substrate-like sequence of cystatin: targeting of the active site of cruzipain, the major cysteine proteinase of Trypanosoma cruzi. Biochem. J. 318(2), 395, (1996).
    • (1996) Biochem. J , vol.318 , Issue.2 , pp. 395
    • Lalmanach, G.1    Mayer, R.2    Serveau, C.3    Scharfstein, J.4    Gauthier, F.5
  • 66
    • 33749575838 scopus 로고    scopus 로고
    • A versatile library of activity-based probes for fluorescence detection and/or affinity isolation of lipolytic enzymes
    • Susani-Etzerodt H., Schmidinger H., Riesenhuber G., Bimer-Gruenberger R., Hermetter A.: A versatile library of activity-based probes for fluorescence detection and/or affinity isolation of lipolytic enzymes. Chem. Phys. Lipids 144(1), 60, (2006).
    • (2006) Chem. Phys. Lipids , vol.144 , Issue.1 , pp. 60
    • Susani-Etzerodt, H.1    Schmidinger, H.2    Riesenhuber, G.3    Bimer-Gruenberger, R.4    Hermetter, A.5
  • 67
    • 35848965006 scopus 로고    scopus 로고
    • Activity-based protein profiling for the functional annotation of enzymes
    • Barglow K.T., Cravatt B.F.: Activity-based protein profiling for the functional annotation of enzymes. Nat. Methods 4(10), 822, (2007).
    • (2007) Nat. Methods , vol.4 , Issue.10 , pp. 822
    • Barglow, K.T.1    Cravatt, B.F.2
  • 68
    • 0036391485 scopus 로고    scopus 로고
    • Design and synthesis of class-selective activity probes for protein tyrosine phosphatases
    • Lo L.C., Pang T.L., Kuo C.H., Chiang Y.L., Wang H.Y., Lin J.J.: Design and synthesis of class-selective activity probes for protein tyrosine phosphatases. J. Proteome Res. 1(1). 35, (2002).
    • (2002) J. Proteome Res , vol.1 , Issue.1 , pp. 35
    • Lo, L.C.1    Pang, T.L.2    Kuo, C.H.3    Chiang, Y.L.4    Wang, H.Y.5    Lin, J.J.6


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