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Volumn 53, Issue 20, 2010, Pages 7452-7460

A new fluorogenic peptide determines proteasome activity in single cells

Author keywords

[No Author keywords available]

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CHYMOTRYPSIN; EPOXOMICIN; FLUORESCENT DYE; PEPTIDE DERIVATIVE; PROTEASOME; PROTEASOME INHIBITOR; PEPTIDE; PROTEIN SUBUNIT; TAT-EDANS-DABCYL PEPTIDE;

EID: 77958464352     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm100362x     Document Type: Article
Times cited : (19)

References (49)
  • 1
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A. L. Protein degradation and protection against misfolded or damaged proteins Nature 2003, 426, 895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 2
    • 0036777957 scopus 로고    scopus 로고
    • The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides
    • Goldberg, A. L.; Cascio, P.; Saric, T.; Rock, K. L. The importance of the proteasome and subsequent proteolytic steps in the generation of antigenic peptides Mol. Immunol. 2002, 39, 147-164
    • (2002) Mol. Immunol. , vol.39 , pp. 147-164
    • Goldberg, A.L.1    Cascio, P.2    Saric, T.3    Rock, K.L.4
  • 5
    • 38449099679 scopus 로고    scopus 로고
    • Role of proteasomes in disease
    • Dahlmann, B. Role of proteasomes in disease BMC Biochem. 2007, 8 (Suppl 1) S3
    • (2007) BMC Biochem. , vol.8 , Issue.SUPPL. 1 , pp. 3
    • Dahlmann, B.1
  • 6
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman, N. L. The ubiquitin proteasome system in neuropathology Acta Neuropathol. 2009, 118, 329-347
    • (2009) Acta Neuropathol. , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 7
    • 5344234076 scopus 로고    scopus 로고
    • The ubiquitin-mediated protein degradation pathway in cancer: Therapeutic implications
    • Burger, A. M.; Seth, A. K. The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications Eur. J. Cancer 2004, 40, 2217-2229
    • (2004) Eur. J. Cancer , vol.40 , pp. 2217-2229
    • Burger, A.M.1    Seth, A.K.2
  • 8
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams, J. The development of proteasome inhibitors as anticancer drugs Cancer Cell 2004, 5, 417-421
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 11
    • 66149146607 scopus 로고    scopus 로고
    • Bortezomib: A review of its use in patients with multiple myeloma
    • Curran, M. P.; McKeage, K. Bortezomib: a review of its use in patients with multiple myeloma Drugs 2009, 69, 859-888
    • (2009) Drugs , vol.69 , pp. 859-888
    • Curran, M.P.1    McKeage, K.2
  • 13
    • 27644518292 scopus 로고    scopus 로고
    • Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates
    • Kisselev, A. F.; Goldberg, A. L. Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates Methods Enzymol. 2005, 398, 364-378
    • (2005) Methods Enzymol. , vol.398 , pp. 364-378
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 14
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N. P.; Lindsten, K.; Glas, R.; Jellne, M.; Masucci, M. G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome- dependent proteolysis in living cells Nature Biotechnol. 2000, 18, 538-543
    • (2000) Nature Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 15
    • 0347765874 scopus 로고    scopus 로고
    • Fluorescent probes for proteolysis: Tools for drug discovery
    • Neefjes, J.; Dantuma, N. P. Fluorescent probes for proteolysis: tools for drug discovery Nature Rev. Drug Discovery 2004, 3, 58-69
    • (2004) Nature Rev. Drug Discovery , vol.3 , pp. 58-69
    • Neefjes, J.1    Dantuma, N.P.2
  • 16
    • 0033674452 scopus 로고    scopus 로고
    • A ubiquitin-based tagging system for controlled modulation of protein stability
    • Stack, J. H.; Whitney, M.; Rodems, S. M.; Pollok, B. A. A ubiquitin-based tagging system for controlled modulation of protein stability Nature Biotechnol. 2000, 18, 1298-1302
    • (2000) Nature Biotechnol. , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 17
    • 0030737501 scopus 로고    scopus 로고
    • Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation
    • Arendt, C. S.; Hochstrasser, M. Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation Proc. Natl. Acad. Sci. U.S.A 1997, 94, 7156-7161
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 7156-7161
    • Arendt, C.S.1    Hochstrasser, M.2
  • 18
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing
    • Heinemeyer, W.; Fischer, M.; Krimmer, T.; Stachon, U.; Wolf, D. H. The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing J. Biol. Chem. 1997, 272, 25200-25209
    • (1997) J. Biol. Chem. , vol.272 , pp. 25200-25209
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 19
    • 0344527769 scopus 로고    scopus 로고
    • Decelerated degradation of short peptides by the 20S proteasome
    • Dolenc, I.; Seemuller, E.; Baumeister, W. Decelerated degradation of short peptides by the 20S proteasome FEBS Lett. 1998, 434, 357-361
    • (1998) FEBS Lett. , vol.434 , pp. 357-361
    • Dolenc, I.1    Seemuller, E.2    Baumeister, W.3
  • 20
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi, D.; Calvet, S.; Trembleau, A.; Brunissen, A.; Chassaing, G.; Prochiantz, A. Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent J. Biol. Chem. 1996, 271, 18188-18193
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 21
    • 33747038452 scopus 로고    scopus 로고
    • Cell-penetrating peptides - A brief introduction
    • Jarver, P.; Langel, U. Cell-penetrating peptides - a brief introduction Biochim. Biophys. Acta 2006, 1758, 260-263
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 260-263
    • Jarver, P.1    Langel, U.2
  • 22
    • 0025099455 scopus 로고
    • Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer
    • Matayoshi, E. D.; Wang, G. T.; Krafft, G. A.; Erickson, J. Novel fluorogenic substrates for assaying retroviral proteases by resonance energy transfer Science 1990, 247, 954-958
    • (1990) Science , vol.247 , pp. 954-958
    • Matayoshi, E.D.1    Wang, G.T.2    Krafft, G.A.3    Erickson, J.4
  • 23
    • 0028434482 scopus 로고
    • Studies on chymotrypsin-like catalysis by synthetic peptides
    • discussion 210 - 212
    • Corey, M. J.; Hallakova, E.; Pugh, K.; Stewart, J. M. Studies on chymotrypsin-like catalysis by synthetic peptides. Appl. Biochem. Biotechnol. 1994, 47, 199 - 210; discussion 210 - 212.
    • (1994) Appl. Biochem. Biotechnol. , vol.47 , pp. 199-210
    • Corey, M.J.1    Hallakova, E.2    Pugh, K.3    Stewart, J.M.4
  • 24
    • 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.; Schreiber, S. L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin Science 1995, 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
  • 25
    • 0034647551 scopus 로고    scopus 로고
    • The human 26 and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
    • Emmerich, N. P.; Nussbaum, A. K.; Stevanovic, S.; Priemer, M.; Toes, R. E.; Rammensee, H. G.; Schild, H. The human 26 and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate J. Biol. Chem. 2000, 275, 21140-21148
    • (2000) J. Biol. Chem. , vol.275 , pp. 21140-21148
    • Emmerich, N.P.1    Nussbaum, A.K.2    Stevanovic, S.3    Priemer, M.4    Toes, R.E.5    Rammensee, H.G.6    Schild, H.7
  • 26
    • 0345291184 scopus 로고    scopus 로고
    • A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome
    • Holzhutter, H. G.; Frommel, C.; Kloetzel, P. M. A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome J. Mol. Biol. 1999, 286, 1251-1265
    • (1999) J. Mol. Biol. , vol.286 , pp. 1251-1265
    • Holzhutter, H.G.1    Frommel, C.2    Kloetzel, P.M.3
  • 27
    • 0024262589 scopus 로고
    • Cellular uptake of the tat protein from human immunodeficiency virus
    • Frankel, A. D.; Pabo, C. O. Cellular uptake of the tat protein from human immunodeficiency virus Cell 1988, 55, 1189-1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 28
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • Herce, H. D.; Garcia, A. E. Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes Proc. Natl. Acad. Sci. U.S.A 2007, 104, 20805-20810
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 30
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng, E. A.; Carlson, L. M.; Gutman, D. M.; Harrington, W. J., Jr.; Lee, K. P.; Boise, L. H. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells Blood 2006, 107, 4907-4916
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 31
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class i antigen presentation
    • Craiu, A.; Gaczynska, M.; Akopian, T.; Gramm, C. F.; Fenteany, G.; Goldberg, A. L.; Rock, K. L. Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation J. Biol. Chem. 1997, 272, 13437-13445
    • (1997) J. Biol. Chem. , vol.272 , pp. 13437-13445
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 32
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev, A. F.; Goldberg, A. L. Proteasome inhibitors: from research tools to drug candidates Chem. Biol. 2001, 8, 739-758
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 36
    • 34447550255 scopus 로고    scopus 로고
    • Managing and exploiting stress in the antibody factory
    • Cenci, S.; Sitia, R. Managing and exploiting stress in the antibody factory FEBS Lett. 2007, 581, 3652-3657
    • (2007) FEBS Lett. , vol.581 , pp. 3652-3657
    • Cenci, S.1    Sitia, R.2
  • 37
    • 34249864120 scopus 로고    scopus 로고
    • A proteasome for all occasions
    • Hanna, J.; Finley, D. A proteasome for all occasions FEBS Lett. 2007, 581, 2854-2861
    • (2007) FEBS Lett. , vol.581 , pp. 2854-2861
    • Hanna, J.1    Finley, D.2
  • 38
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio, P.; Hilton, C.; Kisselev, A. F.; Rock, K. L.; Goldberg, A. L. 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide EMBO J. 2001, 20, 2357-2366
    • (2001) EMBO J. , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 40
    • 28844485595 scopus 로고    scopus 로고
    • Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates
    • Menendez-Benito, V.; Heessen, S.; Dantuma, N. P. Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates Methods Enzymol. 2005, 399, 490-511
    • (2005) Methods Enzymol. , vol.399 , pp. 490-511
    • Menendez-Benito, V.1    Heessen, S.2    Dantuma, N.P.3
  • 41
    • 61849149936 scopus 로고    scopus 로고
    • Cell-based bioluminescent assays for all three proteasome activities in a homogeneous format
    • Moravec, R. A.; OBrien, M. A.; Daily, W. J.; Scurria, M. A.; Bernad, L.; Riss, T. L. Cell-based bioluminescent assays for all three proteasome activities in a homogeneous format Anal. Biochem. 2009, 387, 294-302
    • (2009) Anal. Biochem. , vol.387 , pp. 294-302
    • Moravec, R.A.1    Obrien, M.A.2    Daily, W.J.3    Scurria, M.A.4    Bernad, L.5    Riss, T.L.6
  • 46
    • 27644531336 scopus 로고    scopus 로고
    • Preparation of hybrid (19S-20S-PA28) proteasome complexes and analysis of peptides generated during protein degradation
    • Cascio, P.; Goldberg, A. L. Preparation of hybrid (19S-20S-PA28) proteasome complexes and analysis of peptides generated during protein degradation Methods Enzymol. 2005, 398, 336-352
    • (2005) Methods Enzymol. , vol.398 , pp. 336-352
    • Cascio, P.1    Goldberg, A.L.2
  • 47
    • 34249780547 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the native and partially folded states of ubiquitin: Influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics
    • Kony, D. B.; Hunenberger, P. H.; van Gunsteren, W. F. Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics Protein Sci. 2007, 16, 1101-1118
    • (2007) Protein Sci. , vol.16 , pp. 1101-1118
    • Kony, D.B.1    Hunenberger, P.H.2    Van Gunsteren, W.F.3
  • 48
    • 0037080244 scopus 로고    scopus 로고
    • Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: Applications to the molecular systems and geometric objects
    • Rocchia, W.; Sridharan, S.; Nicholls, A.; Alexov, E.; Chiabrera, A.; Honig, B. Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects J. Comput. Chem. 2002, 23, 128-137
    • (2002) J. Comput. Chem. , vol.23 , pp. 128-137
    • Rocchia, W.1    Sridharan, S.2    Nicholls, A.3    Alexov, E.4    Chiabrera, A.5    Honig, B.6
  • 49
    • 60349089810 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase binding domain-dependent phosphorylation of mitogen-activated protein kinase kinase 4 and mitogen-activated protein kinase kinase 7 and balancing cross-talk between c-Jun N-terminal kinase and extracellular signal-regulated kinase pathways in cortical neurons
    • Repici, M.; Mare, L.; Colombo, A.; Ploia, C.; Sclip, A.; Bonny, C.; Nicod, P.; Salmona, M.; Borsello, T. c-Jun N-terminal kinase binding domain-dependent phosphorylation of mitogen-activated protein kinase kinase 4 and mitogen-activated protein kinase kinase 7 and balancing cross-talk between c-Jun N-terminal kinase and extracellular signal-regulated kinase pathways in cortical neurons Neuroscience 2009, 159, 94-103
    • (2009) Neuroscience , vol.159 , pp. 94-103
    • Repici, M.1    Mare, L.2    Colombo, A.3    Ploia, C.4    Sclip, A.5    Bonny, C.6    Nicod, P.7    Salmona, M.8    Borsello, T.9


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