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Volumn 9, Issue 2, 2010, Pages 912-923

Activity-based proteome profiling of hepatoma cells during hepatitis C virus replication using protease substrate probes

Author keywords

Activity based protein profiling; Amino acid coupled quinolimine methide probes; Carboxylesterase 1; Hepatitis C; Hydrolases; Liver; Proteases; Protein disulfide isomerase

Indexed keywords

AMINO ACID; CARBOXYLESTERASE; CATHEPSIN D; CHAPERONIN; CHORISMATE MUTASE; ELECTROPHILE; GLUTAMINE; HISTIDINE; HYDROLASE; ISOMERASE; OXIDOREDUCTASE; PHENYLALANINE; PROTEIN DISULFIDE ISOMERASE; PROTEINASE; PROTEOME; SERINE; THREONINE; VIRUS RNA;

EID: 76149144007     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr900788a     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 59149085501 scopus 로고    scopus 로고
    • The global burden of hepatitis C
    • Lavanchy, D. The global burden of hepatitis C. Liver Int. 2009, 29 Suppl 1, 74-81.
    • (2009) Liver Int , vol.29 , Issue.SUPPL. 1 , pp. 74-81
    • Lavanchy, D.1
  • 2
    • 23944476834 scopus 로고    scopus 로고
    • Unravelling hepatitis C virus replication from genome to function
    • Lindenbach, B. D.; Rice, C. M. Unravelling hepatitis C virus replication from genome to function. Nature 2005, 436 (7053), 933-8.
    • (2005) Nature , vol.436 , Issue.7053 , pp. 933-938
    • Lindenbach, B.D.1    Rice, C.M.2
  • 4
    • 0030828466 scopus 로고    scopus 로고
    • Phosphorylation of the hepatitis C virus NS5A protein in vitro and in vivo: Properties of the NS5Aassociated kinase
    • Reed, K. E.; Xu, J.; Rice, C. M. Phosphorylation of the hepatitis C virus NS5A protein in vitro and in vivo: properties of the NS5Aassociated kinase. J. Virol. 1997, 71 (10), 7187-97.
    • (1997) J. Virol , vol.71 , Issue.10 , pp. 7187-7197
    • Reed, K.E.1    Xu, J.2    Rice, C.M.3
  • 5
    • 18944366522 scopus 로고    scopus 로고
    • Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication
    • Wang, C.; Gale, M., Jr.; Keller, B. C.; Huang, H.; Brown, M. S.; Goldstein, J. L.; Ye, J. Identification of FBL2 as a geranylgeranylated cellular protein required for hepatitis C virus RNA replication. Mol. Cell 2005, 18 (4), 425-34.
    • (2005) Mol. Cell , vol.18 , Issue.4 , pp. 425-434
    • Wang, C.1    Gale Jr., M.2    Keller, B.C.3    Huang, H.4    Brown, M.S.5    Goldstein, J.L.6    Ye, J.7
  • 6
    • 24644483623 scopus 로고    scopus 로고
    • Modulation of hepatitis C virus RNA abundance by a liver-specific MicroRNA
    • Jopling, C. L.; Yi, M.; Lancaster, A. M.; Lemon, S. M.; Sarnow, P. Modulation of hepatitis C virus RNA abundance by a liver-specific MicroRNA. Science 2005, 309 (5740), 1577-81.
    • (2005) Science , vol.309 , Issue.5740 , pp. 1577-1581
    • Jopling, C.L.1    Yi, M.2    Lancaster, A.M.3    Lemon, S.M.4    Sarnow, P.5
  • 7
    • 46749124698 scopus 로고    scopus 로고
    • Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome
    • Jopling, C. L.; Schutz, S.; Sarnow, P. Position-dependent function for a tandem microRNA miR-122-binding site located in the hepatitis C virus RNA genome. Cell Host Microbe 2008, 4 (1), 77-85.
    • (2008) Cell Host Microbe , vol.4 , Issue.1 , pp. 77-85
    • Jopling, C.L.1    Schutz, S.2    Sarnow, P.3
  • 8
    • 0025991559 scopus 로고
    • Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis
    • Hijikata, M.; Kato, N.; Ootsuyama, Y.; Nakagawa, M.; Shimotohno, K. Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis. Proc. Natl. Acad. Sci. U.S.A. 1991, 88 (13), 5547-51.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , Issue.13 , pp. 5547-5551
    • Hijikata, M.1    Kato, N.2    Ootsuyama, Y.3    Nakagawa, M.4    Shimotohno, K.5
  • 9
    • 0030273064 scopus 로고    scopus 로고
    • Hepatitis C virus core protein: Carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase
    • Hussy, P.; Langen, H.; Mous, J.; Jacobsen, H. Hepatitis C virus core protein: carboxy-terminal boundaries of two processed species suggest cleavage by a signal peptide peptidase. Virology 1996, 224 (1), 93-104.
    • (1996) Virology , vol.224 , Issue.1 , pp. 93-104
    • Hussy, P.1    Langen, H.2    Mous, J.3    Jacobsen, H.4
  • 11
    • 50149086906 scopus 로고    scopus 로고
    • Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation
    • Okamoto, K.; Mori, Y.; Komoda, Y.; Okamoto, T.; Okochi, M.; Takeda, M.; Suzuki, T.; Moriishi, K.; Matsuura, Y. Intramembrane processing by signal peptide peptidase regulates the membrane localization of hepatitis C virus core protein and viral propagation. J. Virol. 2008, 82 (17), 8349-61.
    • (2008) J. Virol , vol.82 , Issue.17 , pp. 8349-8361
    • Okamoto, K.1    Mori, Y.2    Komoda, Y.3    Okamoto, T.4    Okochi, M.5    Takeda, M.6    Suzuki, T.7    Moriishi, K.8    Matsuura, Y.9
  • 12
    • 0027287798 scopus 로고
    • Nonstructural protein 3 of the hepatitis C virus encodes a serinetype proteinase required for cleavage at the NS3/4 and NS4/5 junctions
    • Bartenschlager, R.; Ahlborn-Laake, L.; Mous, J.; Jacobsen, H. Nonstructural protein 3 of the hepatitis C virus encodes a serinetype proteinase required for cleavage at the NS3/4 and NS4/5 junctions. J. Virol. 1993, 67 (7), 3835-44.
    • (1993) J. Virol , vol.67 , Issue.7 , pp. 3835-3844
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Mous, J.3    Jacobsen, H.4
  • 13
    • 0027163740 scopus 로고
    • Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus
    • Hijikata, M.; Mizushima, H.; Akagi, T.; Mori, S.; Kakiuchi, N.; Kato, N.; Tanaka, T.; Kimura, K.; Shimotohno, K. Two distinct proteinase activities required for the processing of a putative nonstructural precursor protein of hepatitis C virus. J. Virol. 1993, 67 (8), 4665-75.
    • (1993) J. Virol , vol.67 , Issue.8 , pp. 4665-4675
    • Hijikata, M.1    Mizushima, H.2    Akagi, T.3    Mori, S.4    Kakiuchi, N.5    Kato, N.6    Tanaka, T.7    Kimura, K.8    Shimotohno, K.9
  • 14
    • 0028290389 scopus 로고
    • Processing in the hepatitis C virus E2-NS2 region: Identification of p7 and two distinct E2-specific products with different C termini
    • Lin, C.; Lindenbach, B. D.; Pragai, B. M.; McCourt, D. W.; Rice, C. M. Processing in the hepatitis C virus E2-NS2 region: identification of p7 and two distinct E2-specific products with different C termini. J. Virol. 1994, 68 (8), 5063-73.
    • (1994) J. Virol , vol.68 , Issue.8 , pp. 5063-5073
    • Lin, C.1    Lindenbach, B.D.2    Pragai, B.M.3    McCourt, D.W.4    Rice, C.M.5
  • 15
    • 0037803570 scopus 로고    scopus 로고
    • Human and mouse proteases: A comparative genomic approach
    • Puente, X. S.; Sanchez, L. M.; Overall, C. M.; Lopez-Otin, C. Human and mouse proteases: a comparative genomic approach. Nat. Rev. Genet. 2003, 4 (7), 544-58.
    • (2003) Nat. Rev. Genet , vol.4 , Issue.7 , pp. 544-558
    • Puente, X.S.1    Sanchez, L.M.2    Overall, C.M.3    Lopez-Otin, C.4
  • 16
    • 33748595526 scopus 로고    scopus 로고
    • Mechanism-based profiling of enzyme families
    • Evans, M. J.; Cravatt, B. F. Mechanism-based profiling of enzyme families. Chem. Rev. 2006, 106 (8), 3279-301.
    • (2006) Chem. Rev , vol.106 , Issue.8 , pp. 3279-3301
    • Evans, M.J.1    Cravatt, B.F.2
  • 18
    • 67449102606 scopus 로고    scopus 로고
    • Diversity of serine hydrolase activities of unchallenged and botrytis-infected Arabidopsis thaliana
    • Kaschani, F.; Gu, C.; Niessen, S.; Hoover, H.; Cravatt, B. F.; van der Hoorn, R. A. Diversity of serine hydrolase activities of unchallenged and botrytis-infected Arabidopsis thaliana. Mol. Cell. Proteomics 2009, 8 (5), 1082-93.
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.5 , pp. 1082-1093
    • Kaschani, F.1    Gu, C.2    Niessen, S.3    Hoover, H.4    Cravatt, B.F.5    van der Hoorn, R.A.6
  • 19
    • 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 2007, 4 (10), 822-7.
    • (2007) Nat. Methods , vol.4 , Issue.10 , pp. 822-827
    • Barglow, K.T.1    Cravatt, B.F.2
  • 20
    • 54349106665 scopus 로고    scopus 로고
    • Activity-based probes as a tool for functional proteomic analysis of proteases
    • Fonovic, M.; Bogyo, M. Activity-based probes as a tool for functional proteomic analysis of proteases. Expert Rev. Proteomic 2008, 5 (5), 721-30.
    • (2008) Expert Rev. Proteomic , vol.5 , Issue.5 , pp. 721-730
    • Fonovic, M.1    Bogyo, M.2
  • 21
    • 43149105407 scopus 로고    scopus 로고
    • Activity-based protein profiling: New developments and directions in functional proteomics
    • Uttamchandani, M.; Li, J.; Sun, H.; Yao, S. Q. Activity-based protein profiling: new developments and directions in functional proteomics. ChemBioChem 2008, 9 (5), 667-75.
    • (2008) ChemBioChem , vol.9 , Issue.5 , pp. 667-675
    • Uttamchandani, M.1    Li, J.2    Sun, H.3    Yao, S.Q.4
  • 22
    • 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. U.S.A. 1999, 96 (26), 14694-9.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , Issue.26 , pp. 14694-14699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 23
    • 2342650688 scopus 로고    scopus 로고
    • Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor
    • Marnett, A. B.; Nomura, A. M.; Shimba, N.; Ortiz de Montellano, P. R.; Craik, C. S. Communication between the active sites and dimer interface of a herpesvirus protease revealed by a transition-state inhibitor. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (18), 6870-5.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , Issue.18 , pp. 6870-6875
    • Marnett, A.B.1    Nomura, A.M.2    Shimba, N.3    Ortiz de Montellano, P.R.4    Craik, C.S.5
  • 25
    • 18844382666 scopus 로고    scopus 로고
    • An affinity-based probe for the proteomic profiling of aspartic proteases
    • Chattopadhaya, S.; Chan, E. W. S.; Yao, S. Q. An affinity-based probe for the proteomic profiling of aspartic proteases. Tetrahedron Lett. 2005, 46, 4053-6.
    • (2005) Tetrahedron Lett , vol.46 , pp. 4053-4056
    • Chattopadhaya, S.1    Chan, E.W.S.2    Yao, S.Q.3
  • 26
    • 7744233875 scopus 로고    scopus 로고
    • Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases
    • Chan, E. W.; Chattopadhaya, S.; Panicker, R. C.; Huang, X.; Yao, S. Q. Developing photoactive affinity probes for proteomic profiling: hydroxamate-based probes for metalloproteases. J. Am. Chem. Soc. 2004, 126 (44), 14435-46.
    • (2004) J. Am. Chem. Soc , vol.126 , Issue.44 , pp. 14435-14446
    • Chan, E.W.1    Chattopadhaya, S.2    Panicker, R.C.3    Huang, X.4    Yao, S.Q.5
  • 27
    • 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. 2006, 2 (5), 274-81.
    • (2006) Nat. Chem. Biol , vol.2 , Issue.5 , pp. 274-281
    • Sieber, S.A.1    Niessen, S.2    Hoover, H.S.3    Cravatt, B.F.4
  • 28
    • 0035113229 scopus 로고    scopus 로고
    • Profiling the specific reactivity of the proteome with non-directed activity-based probes
    • Adam, G. C.; Cravatt, B. F.; Sorensen, E. J. Profiling the specific reactivity of the proteome with non-directed activity-based probes. Chem. Biol. 2001, 8 (1), 81-95.
    • (2001) Chem. Biol , vol.8 , Issue.1 , pp. 81-95
    • Adam, G.C.1    Cravatt, B.F.2    Sorensen, E.J.3
  • 29
    • 8844268481 scopus 로고    scopus 로고
    • Discovering disease-associated enzymes by proteome reactivity profiling
    • Barglow, K. T.; Cravatt, B. F. Discovering disease-associated enzymes by proteome reactivity profiling. Chem. Biol. 2004, 11 (11), 1523-31.
    • (2004) Chem. Biol , vol.11 , Issue.11 , pp. 1523-1531
    • Barglow, K.T.1    Cravatt, B.F.2
  • 31
    • 3242753474 scopus 로고    scopus 로고
    • Developing novel activity-based fluorescent probes that target different classes of proteases
    • Zhu, Q.; Girish, A.; Chattopadhaya, S.; Yao, S. Q. Developing novel activity-based fluorescent probes that target different classes of proteases. Chem. Commun. 2004, 7 (13), 1512-3.
    • (2004) Chem. Commun , vol.7 , Issue.13 , pp. 1512-1513
    • Zhu, Q.1    Girish, A.2    Chattopadhaya, S.3    Yao, S.Q.4
  • 32
    • 30444453443 scopus 로고    scopus 로고
    • Activity-based fingerprinting of proteases
    • Srinivasan, R.; Huang, X.; Ng, S. L.; Yao, S. Q. Activity-based fingerprinting of proteases. ChemBioChem 2006, 7 (1), 32-6.
    • (2006) ChemBioChem , vol.7 , Issue.1 , pp. 32-36
    • Srinivasan, R.1    Huang, X.2    Ng, S.L.3    Yao, S.Q.4
  • 33
    • 0031789165 scopus 로고    scopus 로고
    • Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease
    • Taremi, S. S.; Beyer, B.; Maher, M.; Yao, N.; Prosise, W.; Weber, P. C.; Malcolm, B. A. Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease. Protein Sci. 1998, 7 (10), 2143-9.
    • (1998) Protein Sci , vol.7 , Issue.10 , pp. 2143-2149
    • Taremi, S.S.1    Beyer, B.2    Maher, M.3    Yao, N.4    Prosise, W.5    Weber, P.C.6    Malcolm, B.A.7
  • 34
    • 0242689518 scopus 로고
    • Human anti-endoplasmic reticulum antibodies in sera of patients with halothane-induced hepatitis are directed against a trifluoroacetylated carboxylesterase
    • Satoh, H.; Martin, B. M.; Schulick, A. H.; Christ, D. D.; Kenna, J. G.; Pohl, L. R. Human anti-endoplasmic reticulum antibodies in sera of patients with halothane-induced hepatitis are directed against a trifluoroacetylated carboxylesterase. Proc. Natl. Acad. Sci. U.S.A. 1989, 86 (1), 322-6.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , Issue.1 , pp. 322-326
    • Satoh, H.1    Martin, B.M.2    Schulick, A.H.3    Christ, D.D.4    Kenna, J.G.5    Pohl, L.R.6
  • 35
    • 0345188811 scopus 로고    scopus 로고
    • Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line
    • Lohmann, V.; Korner, F.; Koch, J.; Herian, U.; Theilmann, L.; Bartenschlager, R. Replication of subgenomic hepatitis C virus RNAs in a hepatoma cell line. Science 1999, 285 (5424), 110-3.
    • (1999) Science , vol.285 , Issue.5424 , pp. 110-113
    • Lohmann, V.1    Korner, F.2    Koch, J.3    Herian, U.4    Theilmann, L.5    Bartenschlager, R.6
  • 36
    • 38049141270 scopus 로고    scopus 로고
    • Identification of human kinases involved in hepatitis C virus replication by small interference RNA library screening
    • Supekova, L.; Supek, F.; Lee, J.; Chen, S.; Gray, N.; Pezacki, J. P.; Schlapbach, A.; Schultz, P. G. Identification of human kinases involved in hepatitis C virus replication by small interference RNA library screening. J. Biol. Chem. 2008, 283 (1), 29-36.
    • (2008) J. Biol. Chem , vol.283 , Issue.1 , pp. 29-36
    • Supekova, L.1    Supek, F.2    Lee, J.3    Chen, S.4    Gray, N.5    Pezacki, J.P.6    Schlapbach, A.7    Schultz, P.G.8
  • 38
    • 33748576909 scopus 로고    scopus 로고
    • Bleomycin is a potent small-molecule inhibitor of hepatitis C virus replication
    • Rakic, B.; Brulotte, M.; Rouleau, Y.; Belanger, S.; Pezacki, J. P. Bleomycin is a potent small-molecule inhibitor of hepatitis C virus replication. ChemBioChem 2006, 7 (9), 1330-3.
    • (2006) ChemBioChem , vol.7 , Issue.9 , pp. 1330-1333
    • Rakic, B.1    Brulotte, M.2    Rouleau, Y.3    Belanger, S.4    Pezacki, J.P.5
  • 39
    • 33644689234 scopus 로고    scopus 로고
    • Simultaneous quantitative measurement of luciferase reporter activity and cell number in two- and three-dimensional cultures of hepatitis C virus replicons
    • Tonary, A. M.; Pezacki, J. P. Simultaneous quantitative measurement of luciferase reporter activity and cell number in two- and three-dimensional cultures of hepatitis C virus replicons. Anal. Biochem. 2006, 350 (2), 239-48.
    • (2006) Anal. Biochem , vol.350 , Issue.2 , pp. 239-248
    • Tonary, A.M.1    Pezacki, J.P.2
  • 40
    • 30744445243 scopus 로고    scopus 로고
    • The influence of cholesterol and lipid metabolism on host cell structure and hepatitis C virus replication
    • Sagan, S. M.; Rouleau, Y.; Leggiadro, C.; Supekova, L.; Schultz, P. G.; Su, A. I.; Pezacki, J. P. The influence of cholesterol and lipid metabolism on host cell structure and hepatitis C virus replication. Biochem. Cell. Biol. 2006, 84 (1), 67-79.
    • (2006) Biochem. Cell. Biol , vol.84 , Issue.1 , pp. 67-79
    • Sagan, S.M.1    Rouleau, Y.2    Leggiadro, C.3    Supekova, L.4    Schultz, P.G.5    Su, A.I.6    Pezacki, J.P.7
  • 41
    • 30744432858 scopus 로고    scopus 로고
    • Peroxisome proliferatoractivated receptor alpha antagonism inhibits hepatitis C virus replication
    • Rakic, B.; Sagan, S. M.; Noestheden, M.; Belanger, S.; Nan, X. L.; Evans, C. L.; Xie, X. S.; Pezacki, J. P. Peroxisome proliferatoractivated receptor alpha antagonism inhibits hepatitis C virus replication. Chem. Biol. 2006, 13 (1), 23-30.
    • (2006) Chem. Biol , vol.13 , Issue.1 , pp. 23-30
    • Rakic, B.1    Sagan, S.M.2    Noestheden, M.3    Belanger, S.4    Nan, X.L.5    Evans, C.L.6    Xie, X.S.7    Pezacki, J.P.8
  • 42
    • 76149098993 scopus 로고    scopus 로고
    • Carboxylesterase 1 enzyme on lipid droplets aids hepatitis C virus propagation
    • Submitted for publication
    • Blais, D. R.; Lyn, R. K.; Joyce, M.; Rouleau, Y.; Pegoraro, A.; Stolow, A.; Tyrrell, D. L.; Pezacki, J. P., Carboxylesterase 1 enzyme on lipid droplets aids hepatitis C virus propagation. Submitted for publication, 2009.
    • (2009)
    • Blais, D.R.1    Lyn, R.K.2    Joyce, M.3    Rouleau, Y.4    Pegoraro, A.5    Stolow, A.6    Tyrrell, D.L.7    Pezacki, J.P.8
  • 45
    • 0027400775 scopus 로고
    • Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling
    • Scarborough, P. E.; Guruprasad, K.; Topham, C.; Richo, G. R.; Conner, G. E.; Blundell, T. L.; Dunn, B. M. Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling. Protein Sci. 1993, 2 (2), 264-76.
    • (1993) Protein Sci , vol.2 , Issue.2 , pp. 264-276
    • Scarborough, P.E.1    Guruprasad, K.2    Topham, C.3    Richo, G.R.4    Conner, G.E.5    Blundell, T.L.6    Dunn, B.M.7
  • 46
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • Groll, M.; Huber, R. Substrate access and processing by the 20S proteasome core particle. Int. J. Biochem. Cell Biol. 2003, 35 (5), 606-16.
    • (2003) Int. J. Biochem. Cell Biol , vol.35 , Issue.5 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 47
    • 27744516748 scopus 로고    scopus 로고
    • Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
    • Hu, M.; Li, P.; Song, L.; Jeffrey, P. D.; Chenova, T. A.; Wilkinson, K. D.; Cohen, R. E.; Shi, Y. Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14. EMBO J. 2005, 24 (21), 3747-56.
    • (2005) EMBO J , vol.24 , Issue.21 , pp. 3747-3756
    • Hu, M.1    Li, P.2    Song, L.3    Jeffrey, P.D.4    Chenova, T.A.5    Wilkinson, K.D.6    Cohen, R.E.7    Shi, Y.8
  • 48
    • 0037036431 scopus 로고    scopus 로고
    • Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP
    • Kang, S. G.; Ortega, J.; Singh, S. K.; Wang, N.; Huang, N. N.; Steven, A. C.; Maurizi, M. R. Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP. J. Biol. Chem. 2002, 277 (23), 21095-102.
    • (2002) J. Biol. Chem , vol.277 , Issue.23 , pp. 21095-21102
    • Kang, S.G.1    Ortega, J.2    Singh, S.K.3    Wang, N.4    Huang, N.N.5    Steven, A.C.6    Maurizi, M.R.7
  • 49
    • 12044253640 scopus 로고
    • The refined 2.15-A X-Ray crystal-structure of human liver cathepsin B - The structural basis for its specificity
    • Musil, D.; Zucic, D.; Turk, D.; Engh, R. A.; Mayr, I.; Huber, R.; Popovic, T.; Turk, V.; Towatari, T.; Katunuma, N.; Bode, W. The refined 2.15-A X-Ray crystal-structure of human liver cathepsin B - The structural basis for its specificity. EMBO J. 1991, 10 (9), 2321-2330.
    • (1991) EMBO J , vol.10 , Issue.9 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5    Huber, R.6    Popovic, T.7    Turk, V.8    Towatari, T.9    Katunuma, N.10    Bode, W.11
  • 50
    • 0037307787 scopus 로고    scopus 로고
    • Chemical proteomics and its application to drug discovery
    • Jeffery, D. A.; Bogyo, M. Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 2003, 14 (1), 87-95.
    • (2003) Curr. Opin. Biotechnol , vol.14 , Issue.1 , pp. 87-95
    • Jeffery, D.A.1    Bogyo, M.2
  • 51
    • 35648998466 scopus 로고    scopus 로고
    • Proteomics evaluation of chemically cleavable activity-based probes
    • Fonovic, M.; Verhelst, S. H. L.; Sorum, M. T.; Bogyo, M. Proteomics evaluation of chemically cleavable activity-based probes. Mol. Cell. Proteomics 2007, 6 (10), 1761-70.
    • (2007) Mol. Cell. Proteomics , vol.6 , Issue.10 , pp. 1761-1770
    • Fonovic, M.1    Verhelst, S.H.L.2    Sorum, M.T.3    Bogyo, M.4
  • 52
    • 0028908783 scopus 로고
    • Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase
    • Bartenschlager, R.; Ahlborn-Laake, L.; Yasargil, K.; Mous, J.; Jacobsen, H. Substrate determinants for cleavage in cis and in trans by the hepatitis C virus NS3 proteinase. J. Virol. 1995, 69 (1), 198-205.
    • (1995) J. Virol , vol.69 , Issue.1 , pp. 198-205
    • Bartenschlager, R.1    Ahlborn-Laake, L.2    Yasargil, K.3    Mous, J.4    Jacobsen, H.5
  • 53
    • 50649106648 scopus 로고    scopus 로고
    • Cathepsin D-Many functions of one aspartic protease
    • Benes, P.; Vetvicka, V.; Fusek, M. Cathepsin D-Many functions of one aspartic protease. Crit. Rev. Oncol. Hemat. 2008, 68 (1), 12-28.
    • (2008) Crit. Rev. Oncol. Hemat , vol.68 , Issue.1 , pp. 12-28
    • Benes, P.1    Vetvicka, V.2    Fusek, M.3
  • 54
    • 32444435210 scopus 로고    scopus 로고
    • Time- and temperature-dependent activation of hepatitis C virus for low-pH-triggered entry
    • Tscherne, D. M.; Jones, C. T.; Evans, M. J.; Lindenbach, B. D.; McKeating, J. A.; Rice, C. M. Time- and temperature-dependent activation of hepatitis C virus for low-pH-triggered entry. J. Virol. 2006, 80 (4), 1734-41.
    • (2006) J. Virol , vol.80 , Issue.4 , pp. 1734-1741
    • Tscherne, D.M.1    Jones, C.T.2    Evans, M.J.3    Lindenbach, B.D.4    McKeating, J.A.5    Rice, C.M.6
  • 55
    • 59449103206 scopus 로고    scopus 로고
    • Nuclear localization mechanism of Hsp105 and its possible function in mammalian cells
    • Saito, Y.; Yamagishi, N.; Hatayama, T. Nuclear localization mechanism of Hsp105 and its possible function in mammalian cells. J. Biochem. 2009, 145 (2), 185-191.
    • (2009) J. Biochem , vol.145 , Issue.2 , pp. 185-191
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3


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