메뉴 건너뛰기




Volumn 3, Issue 1, 2004, Pages 58-69

Fluorescent probes for proteolysis: Tools for drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

3 [2 [(2 TERT BUTYLPHENYLAMINOOXALYL)AMINO]PROPIONYLAMINO] 4 OXO 5 (2,3,5,6 TETRAFLUOROPHENOXY)PENTANOIC ACID; ANTIRETROVIRUS AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CASPASE 8 INHIBITOR; CATHEPSIN S; CELL ENZYME; EPOXOMICIN; FLUORESCENT DYE; GREEN FLUORESCENT PROTEIN; INDINAVIR; INTERLEUKIN 1BETA CONVERTING ENZYME; INTERLEUKIN 1BETA CONVERTING ENZYME INHIBITOR; LACTONE; LACTONE DERIVATIVE; LOPINAVIR; LOPINAVIR PLUS RITONAVIR; MARIMASTAT; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; NELFINAVIR; PRALNACASAN; PRINOMASTAT; PROTEASOME INHIBITOR; PROTEINASE; PROTEINASE INHIBITOR; REBIMASTAT; RITONAVIR; SAQUINAVIR; TANOMASTAT; UNCLASSIFIED DRUG;

EID: 0347765874     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1282     Document Type: Review
Times cited : (123)

References (128)
  • 1
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T. J. et al. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135 (1995).
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1
  • 2
    • 0034643348 scopus 로고    scopus 로고
    • The major substrates for TAP in vivo are derived from newly synthesized proteins
    • Reits, E. A., Vos, J. C., Gromme, M. & Neefjes, J. The major substrates for TAP in vivo are derived from newly synthesized proteins. Nature 404, 774-778 (2000).
    • (2000) Nature , vol.404 , pp. 774-778
    • Reits, E.A.1    Vos, J.C.2    Gromme, M.3    Neefjes, J.4
  • 3
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert, U. et al. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature 404, 770-774 (2000).
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1
  • 4
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPS): A major source of antigenic peptides for MHC class I molecules?
    • Yewdell, J. W., Anton, L. C. & Bennink, J. R. Defective ribosomal products (DRiPS): a major source of antigenic peptides for MHC class I molecules? J. Immunol. 157, 1823-1826 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 1823-1826
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 5
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y. & Goldberg, A. L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001).
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 6
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nature Rev. Neurosci. 4, 49-60 (2003).
    • (2003) Nature Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 8
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister, W., Walz, J., Zuhl, F. & Seemuller, E. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-380 (1998).
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 9
    • 0033198680 scopus 로고    scopus 로고
    • Tripeptidyl peptidases: Enzymes that count
    • Tomkison, B. Tripeptidyl peptidases: enzymes that count. Trends Biochem. Sci. 24, 355-359 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 355-359
    • Tomkison, B.1
  • 10
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., Rock, K. L. & Goldberg, A. L. Interferon-γ can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273, 18734-18742 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 11
    • 0037341473 scopus 로고    scopus 로고
    • The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation
    • York, I. A. et al. The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation. Immunity 18, 429-440 (2003).
    • (2003) Immunity , vol.18 , pp. 429-440
    • York, I.A.1
  • 12
    • 0038056180 scopus 로고    scopus 로고
    • Proteases in blood clotting
    • Walsh, P. N. & Ahmad, S. S. Proteases in blood clotting. Essays Biochem. 38, 95-111 (2002).
    • (2002) Essays Biochem. , vol.38 , pp. 95-111
    • Walsh, P.N.1    Ahmad, S.S.2
  • 14
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: A tail of a frog that became a prince
    • Brinckerhoff, C. E. & Matrisian, L. M. Matrix metalloproteinases: a tail of a frog that became a prince. Nature Rev. Mol. Cell Biol. 3, 207-214 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 15
    • 0042671326 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilin and presenilin-like proteases
    • Xia, W. & Wolfe, M. S. Intramembrane proteolysis by presenilin and presenilin-like proteases. J Cell Sci. 116, 2839-2844 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2839-2844
    • Xia, W.1    Wolfe, M.S.2
  • 16
    • 0038461962 scopus 로고    scopus 로고
    • Curbing activation: Proprotein convertases in homeostasis and pathology
    • Taylor, N. A., Van De Ven, W. J. & Creemers, J. W. Curbing activation: proprotein convertases in homeostasis and pathology. FASEB J. 17, 1215-1227 (2003).
    • (2003) FASEB J. , vol.17 , pp. 1215-1227
    • Taylor, N.A.1    Van De Ven, W.J.2    Creemers, J.W.3
  • 17
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover, A. & Brundin, P. The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427-446 (2003).
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 18
    • 0033016291 scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz, A. L. & Ciechanover, A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu. Rev. Med. 50, 57-74 (1990).
    • (1990) Annu. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 19
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt, Y., Maya, R., Kazaz, A. & Oren, M. Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299 (1997).
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 20
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner, M., Werness, B. A., Huibregtse, J. M., Levine, A. J. & Howley, P. M. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 63, 1129-1136 (1990).
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 21
    • 0142165038 scopus 로고    scopus 로고
    • When protein destruction runs amok, malignancy is on the loose
    • Pagano, M. & Benmaamar, R. When protein destruction runs amok, malignancy is on the loose. Cancer Cell 4. 251-256 (2003).
    • (2003) Cancer Cell , vol.4 , pp. 251-256
    • Pagano, M.1    Benmaamar, R.2
  • 22
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K. L. & Goldberg, A. L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17, 739-779 (1999).
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739-779
    • Rock, K.L.1    Goldberg, A.L.2
  • 23
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: Quantitating MHC class I antigen presentation
    • Yewdell, J. W., Reits, E. & Neefjes, J. Making sense of mass destruction: quantitating MHC class I antigen presentation. Nature Rev. Immunol. 3, 952-961 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 24
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin, M. & Ben-Neriah, Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu. Rev. Immunol. 18, 621-663 (2000).
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 25
    • 0036735298 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model
    • LeBlanc, R. et al. Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model. Cancer Res. 62, 4996-5000 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 4996-5000
    • LeBlanc, R.1
  • 26
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin; a potent and selective proteasome inhibitor, exhibits in vivo antinflammatory activity
    • Meng. L. et al. Epoxomicin; a potent and selective proteasome inhibitor, exhibits in vivo antinflammatory activity. Proc. Natl Acad. Sci. USA 96, 10403-10408 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1
  • 27
    • 0034902354 scopus 로고    scopus 로고
    • Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-κB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma
    • Sunwoo, J. B. et al. Novel proteasome inhibitor PS-341 inhibits activation of nuclear factor-κB, cell survival, tumor growth, and angiogenesis in squamous cell carcinoma. Clin. Cancer Res. 7, 1419-1428 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1419-1428
    • Sunwoo, J.B.1
  • 28
    • 0034659804 scopus 로고    scopus 로고
    • The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses
    • Schwarz, K. et al. The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses. J. Immunol. 164, 6147-6157 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 6147-6157
    • Schwarz, K.1
  • 30
    • 0036023407 scopus 로고    scopus 로고
    • A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies
    • Aghajanian, C. et al. A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin. Cancer Res. 8, 2505-2511 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2505-2511
    • Aghajanian, C.1
  • 31
    • 13144266673 scopus 로고    scopus 로고
    • An inhibitor of HIV-1 protease modulates proteasome activity, antigen presetation, and T cell responses
    • Andre, P. et al. An inhibitor of HIV-1 protease modulates proteasome activity, antigen presetation, and T cell responses. Proc. Natl Acad. Sci. USA 95, 13120-13124 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13120-13124
    • Andre, P.1
  • 32
    • 0035661381 scopus 로고    scopus 로고
    • HIV protease inhibitors protect apolipoprotein B from degradation by the proteasome: A potential mechanism for protease inhibitor-induced hyperlipidemia
    • Liang, J. S. et al. HIV protease inhibitors protect apolipoprotein B from degradation by the proteasome: a potential mechanism for protease inhibitor-induced hyperlipidemia. Nature Med. 7, 1327-1331 (2001).
    • (2001) Nature Med. , vol.7 , pp. 1327-1331
    • Liang, J.S.1
  • 33
    • 0037093067 scopus 로고    scopus 로고
    • Antitumorigenic effects of HIV protease inhibitor ritonavir: Inhibition of Kaposi sarcoma
    • Pati, S. et al. Antitumorigenic effects of HIV protease inhibitor ritonavir: inhibition of Kaposi sarcoma. Blood 99, 3771-3779 (2002)>
    • (2002) Blood , vol.99 , pp. 3771-3779
    • Pati, S.1
  • 34
    • 0037105651 scopus 로고    scopus 로고
    • The human immunodeficiency virus (HIV)-1 protease inhibitor saquinavir inhibits proteasome function and causes apoptosis and radiosensitization in non-HIV-associated human cancer cells
    • Pajonk, F., Himmelsbach, J., Riess, K., Sommer, A. & McBride, W. H. The human immunodeficiency virus (HIV)-1 protease inhibitor saquinavir inhibits proteasome function and causes apoptosis and radiosensitization in non-HIV-associated human cancer cells. Cancer Res. 62, 5230-5235 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 5230-5235
    • Pajonk, F.1    Himmelsbach, J.2    Riess, K.3    Sommer, A.4    McBride, W.H.5
  • 35
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HsIV by a new class of inhibitors
    • Bogyo, M. et al. Covalent modification of the active site threonine of proteasomal β subunits and the Escherichia coli homolog HsIV by a new class of inhibitors. Proc. Natl Acad. Sci. USA 94, 6629-6634 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1
  • 36
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunits-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G. et al. Inhibition of proteasome activities and subunits-specific amino-terminal threonine modification by lactacystin. Science 268, 726-731 (1995).
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1
  • 37
    • 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. 8, 739-758 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 38
  • 39
    • 0032531925 scopus 로고    scopus 로고
    • A novel site for ubiquitination: The N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein
    • Breitschopf, K., Bengal, E., Ziv, T., Admon, A. & Ciechanover, A. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 17, 5964-5973 (1998).
    • (1998) EMBO J. , vol.17 , pp. 5964-5973
    • Breitschopf, K.1    Bengal, E.2    Ziv, T.3    Admon, A.4    Ciechanover, A.5
  • 40
    • 0141987892 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation
    • Bloom, J., Amador, V., Bartolini, F., DeMartino, G. & Pagano, M. Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation. Cell 115, 71-82 (2003).
    • (2003) Cell , vol.115 , pp. 71-82
    • Bloom, J.1    Amador, V.2    Bartolini, F.3    DeMartino, G.4    Pagano, M.5
  • 41
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C. M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70, 503-533 (2001).
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 42
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney, J. & Hochstrasser, M. Substrate targeting in the ubiquitin system. Cell 97, 427-430 (1999).
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.1    Hochstrasser, M.2
  • 43
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W. W. & Prasher, D. C. Green fluorescent protein as a marker for gene expression. Science 263, 802-805 (1994).
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 44
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N. P., Lindsten, K., Glas, R., Jeline, M. & Masuccie, M. G. Short-lived green fluorescent proteins for quantification of ubiquitin/proteasome-dependent proteolysis in living cells. Nature Biotechnol. 18, 538-543 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jeline, M.4    Masuccie, M.G.5
  • 45
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., Finley, D. & Varshavsky, A. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234, 179-186 (1986).
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 46
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., Ma, P. C., Ota, I. M. & Varshavsky, A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 47
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. The N-end rule: functions, mysteries, uses. Proc. Natl Acad. Scie USA 93, 12142-12149 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 48
    • 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. 18, 1298-1302 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 49
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon, T., Chomsky, O. & Kulka, R. G. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J. 17, 2759-2766 (1998).
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 50
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N. F., Sampat, R. M. & Kopito, R. R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292, 1552-1555 (2001).
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 51
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • Gilon, T., Chomsky, O. & Kulka, R. G. Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair. Mol. Cell. Biol. 20, 7214-7219 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 52
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • Plemper, R. K. & Wolf, D. H. Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci. 24, 266-270 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 53
    • 0032503029 scopus 로고    scopus 로고
    • Viral strategies of immune evasion
    • Ploegh, H. L. Viral strategies of immune evasion. Science 280, 248-253 (1998).
    • (1998) Science , vol.280 , pp. 248-253
    • Ploegh, H.L.1
  • 54
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J. et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384, 432-438 (1996).
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1
  • 55
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E. J. et al. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779 (1996).
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1
  • 56
    • 0034819479 scopus 로고    scopus 로고
    • Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic β-subunits
    • Kessler, B. M. et al. Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic β-subunits. Chem. Biol. 8, 913-929 (2001).
    • (2001) Chem. Biol. , vol.8 , pp. 913-929
    • Kessler, B.M.1
  • 57
    • 0035099055 scopus 로고    scopus 로고
    • Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
    • Myung, J., Kim, K. B., Lindsten, K., Dantuma, N. P. & Crews, C. M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors. Mol. Cell 7, 411-420 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 411-420
    • Myung, J.1    Kim, K.B.2    Lindsten, K.3    Dantuma, N.P.4    Crews, C.M.5
  • 58
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H. & Goldberg, A. L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8, 397-403 (1998).
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 59
    • 0042025074 scopus 로고    scopus 로고
    • Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction
    • Friant, S., Meier, K. D. & Riezman, H. Increased ubiquitin-dependent degradation can replace the essential requirement for heat shock protein induction. EMBO J. 22, 3783-3791 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3783-3791
    • Friant, S.1    Meier, K.D.2    Riezman, H.3
  • 60
    • 0034682502 scopus 로고    scopus 로고
    • Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal
    • Dantuma, N., Heessen, S., Lindsten, K., Jeline, M. & Masucci, M. G. Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal. Proc. Natl Acad. Sci. USA 97, 8381-8385 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.1    Heessen, S.2    Lindsten, K.3    Jeline, M.4    Masucci, M.G.5
  • 61
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef, L. G., Lindsten, K., Masucci, M. G. & Dantuma, N. P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11, 2689-2700 (2002).
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 62
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi, H. Y. & Orr, H. T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23, 217-247 (2000).
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 63
    • 0030775380 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1
    • Levitskaya, J., Sharipo, A., Leonchiks, A., Ciechanover, A. & Masucci, M. G. Inhibition of ubiquitin/proteasome-dependent protein degradation by the Gly-Ala repeat domain of the Epstein-Barr virus nuclear antigen 1. Proc. Natl Acad. Sci. USA 94, 12616-12621 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12616-12621
    • Levitskaya, J.1    Sharipo, A.2    Leonchiks, A.3    Ciechanover, A.4    Masucci, M.G.5
  • 64
    • 0031904016 scopus 로고    scopus 로고
    • A minimal glycine-alanine repeat prevents the interaction of ubiquitinated IκBα with the proteasome: A new mechanism for selective inhibition of proteolysis
    • Sharipo, A., Imreh, M., Leonchiks, A., Imreh, S. & Masucci, M. G. A minimal glycine-alanine repeat prevents the interaction of ubiquitinated IκBα with the proteasome: a new mechanism for selective inhibition of proteolysis. Nature Med. 4, 939-944 (1998).
    • (1998) Nature Med. , vol.4 , pp. 939-944
    • Sharipo, A.1    Imreh, M.2    Leonchiks, A.3    Imreh, S.4    Masucci, M.G.5
  • 65
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings, C. J. et al. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 24, 879-892 (1999).
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1
  • 66
    • 0037010150 scopus 로고    scopus 로고
    • Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system
    • Dantuma, N. P. & Masucci, M. g. Stabilization signals: a novel regulatory mechanism in the ubiquitin/proteasome system. FEBS Lett. 529, 22-26 (2002).
    • (2002) FEBS Lett. , vol.529 , pp. 22-26
    • Dantuma, N.P.1    Masucci, M.G.2
  • 68
    • 0035102090 scopus 로고    scopus 로고
    • The color of mice: In the light of GFP-variant reporters
    • Hadjantonakis, A. K. & Nagy, A. The color of mice: in the light of GFP-variant reporters. Histochem. Cell Biol. 115, 49-58 (2001).
    • (2001) Histochem. Cell Biol. , vol.115 , pp. 49-58
    • Hadjantonakis, A.K.1    Nagy, A.2
  • 69
    • 0034106175 scopus 로고    scopus 로고
    • Transgenic expression of green fluorescence protein can cause dilated cardiomyopathy
    • Huang, W. Y., Aramburu, J., Douglas, P. S. & Izumo, S. Transgenic expression of green fluorescence protein can cause dilated cardiomyopathy. Nature Med. 6, 482-483 (2000).
    • (2000) Nature Med. , vol.6 , pp. 482-483
    • Huang, W.Y.1    Aramburu, J.2    Douglas, P.S.3    Izumo, S.4
  • 71
  • 73
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant α-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli, L. et al. Parkin protects against the toxicity associated with mutant α-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 36, 1007-1019 (2002).
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1
  • 74
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten, K. et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J. Cell Biol. 157, 417-427 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1
  • 75
    • 0141650794 scopus 로고    scopus 로고
    • Monitoring the ubiquitin/proteasome system in conformational diseases
    • Lindsten, K. & Dantuma, N. P. Monitoring the ubiquitin/proteasome system in conformational diseases. Ageing Res. Rev. 2, 433-449 (2003).
    • (2003) Ageing Res. Rev. , vol.2 , pp. 433-449
    • Lindsten, K.1    Dantuma, N.P.2
  • 76
    • 0036533795 scopus 로고    scopus 로고
    • Lessons from animal models of Hungtington's disease
    • Rubinsztein, D. C. Lessons from animal models of Hungtington's disease. Trends Genet. 18, 202-209 (2002).
    • (2002) Trends Genet. , vol.18 , pp. 202-209
    • Rubinsztein, D.C.1
  • 77
    • 0036303818 scopus 로고    scopus 로고
    • Genetically engineered mouse models of neurodegenerative diseases
    • Wong, P. C., Cai, H., Borchelt, D. R. & Price, D. L. Genetically engineered mouse models of neurodegenerative diseases. Nature Neurosci. 5, 633-639 (2002).
    • (2002) Nature Neurosci. , vol.5 , pp. 633-639
    • Wong, P.C.1    Cai, H.2    Borchelt, D.R.3    Price, D.L.4
  • 78
    • 0141891215 scopus 로고    scopus 로고
    • Pathogenesis of polyglutamine disorders: Aggregation revisited
    • Michalik, A. & Van Broeckhoven, C. Pathogenesis of polyglutamine disorders: aggregation revisited. Hum. Mol. Genet. 12, R173-186 (2003).
    • (2003) Hum. Mol. Genet. , vol.12
    • Michalik, A.1    Van Broeckhoven, C.2
  • 80
    • 0037242017 scopus 로고    scopus 로고
    • Peptide diffusion, protection, and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I
    • Reits, E. et al. Peptide diffusion, protection, and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I. Immunity 18, 97-108 (2003).
    • (2003) Immunity , vol.18 , pp. 97-108
    • Reits, E.1
  • 81
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K. & Rudensky, A. Y. Lysosomal cysteine proteases regulate antigen presentation. Nature Rev. Immunol. 3, 472-482 (2003).
    • (2003) Nature Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 82
    • 0036895451 scopus 로고    scopus 로고
    • Enzyme replacement and enhancement therapies: Lessons from lysosomal disorders
    • Desnick, R. J. & Schuchman, E. H. Enzyme replacement and enhancement therapies: lessons from lysosomal disorders. Nature Rev. Genet. 3, 954-966 (2002).
    • (2002) Nature Rev. Genet. , vol.3 , pp. 954-966
    • Desnick, R.J.1    Schuchman, E.H.2
  • 83
    • 0032490741 scopus 로고    scopus 로고
    • Cancer. Proteases - Invasion and more
    • Edwards, D. R. & Murphy, G. Cancer. Proteases - invasion and more. Nature 394, 527-528 (1998).
    • (1998) Nature , vol.394 , pp. 527-528
    • Edwards, D.R.1    Murphy, G.2
  • 84
    • 0346562591 scopus 로고    scopus 로고
    • Identification of a potent and selective noncovalent cathepsin S inhibitor
    • Thurmond, R. L. et al. Identification of a potent and selective noncovalent cathepsin S inhibitor. J. Pharmacol. Exp. Ther. 17, 17 (2003).
    • (2003) J. Pharmacol. Exp. Ther. , vol.17 , pp. 17
    • Thurmond, R.L.1
  • 85
    • 0036329099 scopus 로고    scopus 로고
    • Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity
    • Saegusa, K. et al. Cathepsin S inhibitor prevents autoantigen presentation and autoimmunity. J. Clin. Invest. 110, 361-369 (2002).
    • (2002) J. Clin. Invest. , vol.110 , pp. 361-369
    • Saegusa, K.1
  • 86
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens, L. M., Fingleton, B. & Matrisian, L. M. Matrix metalloproteinase inhibitors and cancer; trials and tribulations. Science 295, 2387-2392 (2002).
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 87
    • 0036716282 scopus 로고    scopus 로고
    • Strategies for MMP inhibition in cancer: Innovations for the post-trial era
    • Overall, C. M. & Lopez-Otin, C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nature Rev. Cancer 2, 657-672 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 657-672
    • Overall, C.M.1    Lopez-Otin, C.2
  • 88
    • 0032951071 scopus 로고    scopus 로고
    • In vivo imaging of tumors with protease-activated near-infrared fluorescent probes
    • Weissleder, R., Tung, C. H., Mahmood, U. & Bogdanov, A. Jr. In vivo imaging of tumors with protease-activated near-infrared fluorescent probes. Nature Biotechnol. 17, 375-378 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 375-378
    • Weissleder, R.1    Tung, C.H.2    Mahmood, U.3    Bogdanov Jr., A.4
  • 89
    • 0031859906 scopus 로고    scopus 로고
    • Preclinical evaluation and phase I clinical trial of a 99mTc-labeled synthetic polymer used in blood pool imaging
    • Callahan, R. J., Bogdanov, A. Jr, Fischman, A. J., Brady, T. J. & Weissleder, R. Preclinical evaluation and phase I clinical trial of a 99mTc-labeled synthetic polymer used in blood pool imaging. Am. J. Roentgenol. 171, 137-143 (1998).
    • (1998) Am. J. Roentgenol. , vol.171 , pp. 137-143
    • Callahan, R.J.1    Bogdanov Jr., A.2    Fischman, A.J.3    Brady, T.J.4    Weissleder, R.5
  • 90
    • 0032697682 scopus 로고    scopus 로고
    • Near-infrared optical imaging of protease activity for tumor detection
    • Mahmood, U., Tung, C. H., Bogdanov, A. Jr & Weissleder, R. Near-infrared optical imaging of protease activity for tumor detection. Radiology 213, 866-870 (1999).
    • (1999) Radiology , vol.213 , pp. 866-870
    • Mahmood, U.1    Tung, C.H.2    Bogdanov Jr., A.3    Weissleder, R.4
  • 91
    • 0036125256 scopus 로고    scopus 로고
    • Imaging of differential protease expression in breast cancers for detection of aggressive tumor phenotypes
    • Bremer, C., Tung, C. H., Bogdanov, A. Jr & Weissleder, R. Imaging of differential protease expression in breast cancers for detection of aggressive tumor phenotypes. Radiology 222, 814-818 (2002).
    • (2002) Radiology , vol.222 , pp. 814-818
    • Bremer, C.1    Tung, C.H.2    Bogdanov Jr., A.3    Weissleder, R.4
  • 92
    • 0037062686 scopus 로고    scopus 로고
    • In vivo imaging of proteolytic activity in ahterosclerosis
    • Chen, J. et al. In vivo imaging of proteolytic activity in ahterosclerosis. Circulation 105, 2766-2771 (2002).
    • (2002) Circulation , vol.105 , pp. 2766-2771
    • Chen, J.1
  • 93
    • 0034283034 scopus 로고    scopus 로고
    • In vivo imaging of proteolytic enzyme activity using a novel molecular reporter
    • Tung. C. H., Mahmood, U., Bredow, S. & Weissleder, R. In vivo imaging of proteolytic enzyme activity using a novel molecular reporter. Cancer Res. 60, 4953-4958 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 4953-4958
    • Tung, C.H.1    Mahmood, U.2    Bredow, S.3    Weissleder, R.4
  • 94
    • 0034954524 scopus 로고    scopus 로고
    • In vivo molecular target assessmet of matrix metalloproteinase inhibition
    • Bremer, C., Tung, C. H. & Weissleder, R. In vivo molecular target assessmet of matrix metalloproteinase inhibition. Nature Med. 7, 743-748 (2001).
    • (2001) Nature Med. , vol.7 , pp. 743-748
    • Bremer, C.1    Tung, C.H.2    Weissleder, R.3
  • 95
    • 0034953171 scopus 로고    scopus 로고
    • Imaging metalloproteinase activity in vivo
    • Zucker, S. & Cao, J. Imaging metalloproteinase activity in vivo. Nature Med. 7, 655-656 (2001).
    • (2001) Nature Med. , vol.7 , pp. 655-656
    • Zucker, S.1    Cao, J.2
  • 96
    • 0041973866 scopus 로고    scopus 로고
    • Pan and sentinel lymph node visualization using a near-infrared fluorescent probe
    • Josephson, L., Mahmood, U., Wunderbaldinger, P., Tang, Y. & Weissleder, R. Pan and sentinel lymph node visualization using a near-infrared fluorescent probe. Mol. Imaging 2, 18-23 (2003).
    • (2003) Mol. Imaging , vol.2 , pp. 18-23
    • Josephson, L.1    Mahmood, U.2    Wunderbaldinger, P.3    Tang, Y.4    Weissleder, R.5
  • 97
    • 0041326344 scopus 로고    scopus 로고
    • Near-infrared fluorescence imaging of lymph nodes using a new enzyme sensing activatable macromolecular optical probe
    • Wunderbaldinger, P., Turetschek, K. & Bremer, C. Near-infrared fluorescence imaging of lymph nodes using a new enzyme sensing activatable macromolecular optical probe. Eur. Radiol 13, 2206-2211 (2003).
    • (2003) Eur. Radiol. , vol.13 , pp. 2206-2211
    • Wunderbaldinger, P.1    Turetschek, K.2    Bremer, C.3
  • 98
    • 0034486945 scopus 로고    scopus 로고
    • Imaging proteolysis by living human breasts cancer cells
    • Sameni, M., Moin, K. & Sloane, B. F. Imaging proteolysis by living human breasts cancer cells. Neoplasia 2, 496-504 (2000).
    • (2000) Neoplasia , vol.2 , pp. 496-504
    • Sameni, M.1    Moin, K.2    Sloane, B.F.3
  • 99
    • 0025672647 scopus 로고
    • β-Galactosidase containing a human immunodeficiency virus protease cleavage site is cleaved and inactivated by human immunodeficiency virus protease
    • Baum, E. Z., Bebernitz, G. A. & Gluzman, Y β-Galactosidase containing a human immunodeficiency virus protease cleavage site is cleaved and inactivated by human immunodeficiency virus protease. Proc. Natl Acad. Sci. USA 87, 10023-10027 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 10023-10027
    • Baum, E.Z.1    Bebernitz, G.A.2    Gluzman, Y.3
  • 100
    • 0025687320 scopus 로고
    • Novel bacteriological assay for detection of potential antiviaral agents
    • Block, T. M. & Grafstrom, R. H. Novel bacteriological assay for detection of potential antiviaral agents. Antimicrob. Agents Chemother. 34, 2337-2341 (1990).
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 2337-2341
    • Block, T.M.1    Grafstrom, R.H.2
  • 101
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. The green fluorescent protein. Annu Rev. Biochem. 67, 509-544 (1998).
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 102
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan, J. & Yankner, B. A. Apoptosis in the nervous system. Nature 407, 802-809 (2000).
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 103
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone, R. W., Ruefli, A. A. & Lowe, S. W. Apoptosis: a link between cancer genetics and chemotherapy. Cell 108, 153-164 (2002).
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 104
    • 0034953632 scopus 로고    scopus 로고
    • Apoptosis-regulating proteins as targets for drug discovery
    • Reed, J. C. Apoptosis-regulating proteins as targets for drug discovery. Trends Mol. Med. 7, 314-319 (2001).
    • (2001) Trends Mol. Med. , vol.7 , pp. 314-319
    • Reed, J.C.1
  • 105
    • 0032522223 scopus 로고    scopus 로고
    • Detection of programmed cell death using fluorescence energy transfer
    • Xu, X. et al. Detection of programmed cell death using fluorescence energy transfer. Nucleic Acids Res. 26, 2034-2035 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2034-2035
    • Xu, X.1
  • 106
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel, P. & Brand, A. H. Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins. Nature Cell Biol. 4, E15-20 (2002).
    • (2002) Nature Cell Biol. , vol.4
    • van Roessel, P.1    Brand, A.H.2
  • 107
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a process. Role of caspase-3
    • Rehm, M. et al. Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a process. Role of caspase-3. J. Biol. Chem. 277, 24506-24514 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1
  • 108
    • 0037069360 scopus 로고    scopus 로고
    • Confirmation by FRET in individual living cells of the absence of significant amyloid β-mediated caspase 8 activation
    • Onuki, R. et al. Confirmation by FRET in individual living cells of the absence of significant amyloid β-mediated caspase 8 activation. Proc. Natl Acad. Sci. USA 99, 14716-14721 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14716-14721
    • Onuki, R.1
  • 109
    • 0035122528 scopus 로고    scopus 로고
    • Imaging FRET between spectrally similar GFP molecules in single cells
    • Harpur, A. G., Wouters, F. S. & Bastiaens, P. I. Imaging FRET between spectrally similar GFP molecules in single cells. Nature Biotechnol. 19, 167-169 (2001).
    • (2001) Nature Biotechnol. , vol.19 , pp. 167-169
    • Harpur, A.G.1    Wouters, F.S.2    Bastiaens, P.I.3
  • 110
    • 0036913248 scopus 로고    scopus 로고
    • Marker for real-time analysis of caspase activity in intact cells
    • 1284-1287
    • Lee, P., Beem, E. & Segal, M. S. Marker for real-time analysis of caspase activity in intact cells. Biotechniques 33, 1284-1287, 1289-1291 (2002).
    • (2002) Biotechniques , vol.33 , pp. 1289-1291
    • Lee, P.1    Beem, E.2    Segal, M.S.3
  • 111
    • 0028709492 scopus 로고
    • Assay methods for retroviral proteases
    • Hellen, C. U. Assay methods for retroviral proteases. Methods Enzymol 241, 46-58 (1994).
    • (1994) Methods Enzymol. , vol.241 , pp. 46-58
    • Hellen, C.U.1
  • 112
    • 0030419901 scopus 로고    scopus 로고
    • Proteolytic processing and particle maturation
    • Vogt, V. M. Proteolytic processing and particle maturation. Curr. Top. Microbiol. Immunol 214, 95-131 (1996).
    • (1996) Curr. Top. Microbiol. Immunol. , vol.214 , pp. 95-131
    • Vogt, V.M.1
  • 113
    • 0043069555 scopus 로고    scopus 로고
    • Toxicity of antiretroviral therapy and implications for drug development
    • Carr, A. Toxicity of antiretroviral therapy and implications for drug development. Nature Rev. Drug Discov. 2, 624-634 (2003).
    • (2003) Nature Rev. Drug Discov. , vol.2 , pp. 624-634
    • Carr, A.1
  • 114
    • 15444377672 scopus 로고    scopus 로고
    • Ordered accumulation of mutations in HIV protease confers resistance to ritonavir
    • Molla, A. et al. Ordered accumulation of mutations in HIV protease confers resistance to ritonavir. Nature Med. 2, 760-766 (1996).
    • (1996) Nature Med. , vol.2 , pp. 760-766
    • Molla, A.1
  • 115
    • 9544225179 scopus 로고    scopus 로고
    • Apoptosis mediated by HIV protease is preceded by cleavage of Bcl-2
    • Strack, P. R. et al. Apoptosis mediated by HIV protease is preceded by cleavage of Bcl-2. Proc. Natl Acad. Sci. USA 93, 9571-9576 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9571-9576
    • Strack, P.R.1
  • 116
    • 0025088659 scopus 로고
    • Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrilary acidic protein
    • Shoeman, R. L. et al. Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrilary acidic protein. Proc. Natl Acad. Sci. USA 87, 6336-6340 (1990).
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6336-6340
    • Shoeman, R.L.1
  • 118
    • 0344201903 scopus 로고    scopus 로고
    • An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus
    • Lamarre, D. et al. An NS3 protease inhibitor with antiviral effects in humans infected with hepatitis C virus. Nature 26, 186-189 (2003).
    • (2003) Nature , vol.26 , pp. 186-189
    • Lamarre, D.1
  • 119
    • 0038120984 scopus 로고    scopus 로고
    • Coronavirus main proteinase (3CLpro) structure: Basis for design of anti-SARS drugs
    • Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J. R. & Hilgenfeld, R. Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 300, 1763-1767 (2003).
    • (2003) Science , vol.300 , pp. 1763-1767
    • Anand, K.1    Ziebuhr, J.2    Wadhwani, P.3    Mesters, J.R.4    Hilgenfeld, R.5
  • 120
    • 0034502493 scopus 로고    scopus 로고
    • How does TAP pump peptides? Insights from DNA repair and traffic ATPases
    • Reits, E. A., Griekspoor, A. C. & Neefjes, J. How does TAP pump peptides? Insights from DNA repair and traffic ATPases. Immunol. Today 21, 598-600 (2000).
    • (2000) Immunol. Today , vol.21 , pp. 598-600
    • Reits, E.A.1    Griekspoor, A.C.2    Neefjes, J.3
  • 121
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits, E. A. & Neefjes, J. J. From fixed to FRAP: measuring protein mobility and activity in living cells. Nature Cell Biol. 3, E145-147 (2001).
    • (2001) Nature Cell Biol. , vol.3
    • Reits, E.A.1    Neefjes, J.J.2
  • 122
    • 0037686295 scopus 로고    scopus 로고
    • Killing the messenger: Short RNAs that silence gene expression
    • Dykxhoorn, D. M., Novina, C. D. & Sharp, P. A. Killing the messenger: short RNAs that silence gene expression. Nature Rev. Mol. Cell Biol. 4, 457-467 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 457-467
    • Dykxhoorn, D.M.1    Novina, C.D.2    Sharp, P.A.3
  • 123
    • 0037900077 scopus 로고    scopus 로고
    • Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production
    • Kessler, B. et al. Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production. J. Biol. Chem. 278, 10013-10021 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 10013-10021
    • Kessler, B.1
  • 124
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewandering und fluoreszenz
    • Föster, T. Zwischenmolekulare energiewandering und fluoreszenz. Annalen Physik. 6, 55-75 (1948).
    • (1948) Annalen Physik. , vol.6 , pp. 55-75
    • Föster, T.1
  • 125
    • 0141727395 scopus 로고    scopus 로고
    • Prainacasan, an inhibitor of interleukin-1β converting enzyme, reduces joint damage in two murine models of osteoarthritis
    • Rudolphi, K., Gerwin, N., Verzil, N., van der Kraan, P. & van den Berg, W. Prainacasan, an inhibitor of interleukin-1β converting enzyme, reduces joint damage in two murine models of osteoarthritis. Osteoarthritis Cartilage 11, 738-746 (2003).
    • (2003) Osteoarthritis Cartilage , vol.11 , pp. 738-746
    • Rudolphi, K.1    Gerwin, N.2    Verzil, N.3    van der Kraan, P.4    van den Berg, W.5
  • 126
    • 0037088990 scopus 로고    scopus 로고
    • Caspase inhibitors for liver disease
    • Whelan, J. Caspase inhibitors for liver disease. Drug Discov. Today 7, 444-445 (2002).
    • (2002) Drug Discov. Today , vol.7 , pp. 444-445
    • Whelan, J.1
  • 127
    • 0036696712 scopus 로고    scopus 로고
    • Targeting HIV: Antiretroviral therapy and development of drug resistance
    • Menendez-Arias, L. Targeting HIV: antiretroviral therapy and development of drug resistance. Trends Pharmacol. Sci. 23, 381-388 (2002).
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 381-388
    • Menendez-Arias, L.1
  • 128
    • 0032867477 scopus 로고    scopus 로고
    • Fluorescent proteins from nonbioluminescent Anthozoa species
    • Matz, M. V. et al. Fluorescent proteins from nonbioluminescent Anthozoa species. Nature Biotechnol. 17, 969-973 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 969-973
    • Matz, M.V.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.