메뉴 건너뛰기




Volumn 399, Issue , 2005, Pages 490-511

Monitoring of ubiquitin-dependent proteolysis with green fluorescent protein substrates

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 28844485595     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(05)99034-4     Document Type: Review
Times cited : (27)

References (57)
  • 1
    • 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 5 2004 417 421
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 2
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel B., Wunning I., and Varshavsky A. The recognition component of the N-end rule pathway EMBO J. 9 1990 3179 3189
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel, B.1    Wunning, I.2    Varshavsky, A.3
  • 3
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W., Walz J., Zuhl F., and Seemuller E. The proteasome: Paradigm of a self-compartmentalizing protease Cell 92 1998 367 380
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 5
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 6
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta 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., and Ploegh H. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors Proc. Natl. Acad. Sci. USA 94 1997 6629 6634
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629-6634
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 7
    • 14644419638 scopus 로고    scopus 로고
    • Polyglutamine neuropathology occurs in the absence of detectable proteasome impairment and inversely correlates with nuclear inclusions
    • Bowman A.B., Yong S.Y., Dantuma N.P., and Zoghbi H.Y. Polyglutamine neuropathology occurs in the absence of detectable proteasome impairment and inversely correlates with nuclear inclusions Hum. Mol. Genet. 14 2005 679 691
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 679-691
    • Bowman, A.B.1    Yong, S.Y.2    Dantuma, N.P.3    Zoghbi, H.Y.4
  • 8
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie M., Tu Y., Euskirchen G., Ward W.W., and Prasher D.C. Green fluorescent protein as a marker for gene expression Science 263 1994 802 805
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.W.4    Prasher, D.C.5
  • 9
    • 0033616143 scopus 로고    scopus 로고
    • Deubiquitinating enzymes: Their diversity and emerging roles
    • Chung C.H., and Baek S.H. Deubiquitinating enzymes: Their diversity and emerging roles Bichem. Biophys. Res. Commun. 266 1999 633 640
    • (1999) Bichem. Biophys. Res. Commun. , vol.266 , pp. 633-640
    • Chung, C.H.1    Baek, S.H.2
  • 10
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg
    • Ciechanover A., and Brundin P. The ubiquitin proteasome system in neurodegenerative diseases: Sometimes the chicken, sometimes the egg Neuron 40 2003 427 446
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 11
    • 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.P., Heessen S., Lindsten K., Jellne M., and 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 2000 8381 8385
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.P.1    Heessen, S.2    Lindsten, K.3    Jellne, M.4    Masucci, M.G.5
  • 12
    • 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., and Masucci M.G. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome- dependent proteolysis in living cells Nat. Biotechnol. 18 2000 538 543
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 13
    • 0037010150 scopus 로고    scopus 로고
    • Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system
    • Dantuma N.P., and Masucci M.G. Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system FEBS Lett. 529 2002 22 26
    • (2002) FEBS Lett. , vol.529 , pp. 22-26
    • Dantuma, N.P.1    Masucci, M.G.2
  • 14
    • 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., and Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin Science 268 1995 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
  • 16
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon T., Chomsky O., and Kulka R.G. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae EMBO J. 17 1998 2759 2766
    • (1998) EMBO J. , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 17
    • 0033834458 scopus 로고    scopus 로고
    • Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair
    • Gilon T., Chomsky O., and Kulka R.G. Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating enzyme pair Mol. Cell Biol. 20 2000 7214 7219
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7214-7219
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 18
    • 0344464848 scopus 로고    scopus 로고
    • Inhibition of ubiquitin/proteasome-dependent proteolysis in Saccharomyces cerevisiae by a Gly-Ala repeat
    • Heessen S., Dantuma N.P., Tessarz P., Jellne M., and Masucci M.G. Inhibition of ubiquitin/proteasome-dependent proteolysis in Saccharomyces cerevisiae by a Gly-Ala repeat FEBS Lett. 555 2003 397 404
    • (2003) FEBS Lett. , vol.555 , pp. 397-404
    • Heessen, S.1    Dantuma, N.P.2    Tessarz, P.3    Jellne, M.4    Masucci, M.G.5
  • 19
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • Heessen S., Masucci M.G., and Dantuma N.P. The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation Mol. Cell 18 2005 225 235
    • (2005) Mol. Cell , vol.18 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 20
    • 0347449543 scopus 로고    scopus 로고
    • Testing the ubiquitin-proteasome hypothesis of neurodegeneration in vivo
    • Hernandez F., Diaz-Hernandez M., Avila J., and Lucas J.J. Testing the ubiquitin-proteasome hypothesis of neurodegeneration in vivo Trends Neurosci. 27 2004 66 69
    • (2004) Trends Neurosci. , vol.27 , pp. 66-69
    • Hernandez, F.1    Diaz-hernandez, M.2    Avila, J.3    Lucas, J.J.4
  • 23
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • Hoskins J.R., Singh S.K., Maurizi M.R., and Wickner S. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP Proc. Natl. Acad. Sci. USA 97 2000 8892 8897
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1    Singh, S.K.2    Maurizi, M.R.3    Wickner, S.4
  • 24
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., and Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing Cell 83 1995 129 135
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 26
    • 0037900077 scopus 로고    scopus 로고
    • Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production
    • Kessler B., Hong X., Petrovic J., Borodovsky A., Dantuma N.P., Bogyo M., Overkleeft H.S., Ploegh H., and Glas R. Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production J. Biol. Chem. 278 2003 10013 10021
    • (2003) J. Biol. Chem. , vol.278 , pp. 10013-10021
    • Kessler, B.1    Hong, X.2    Petrovic, J.3    Borodovsky, A.4    Dantuma, N.P.5    Bogyo, M.6    Overkleeft, H.S.7    Ploegh, H.8    Glas, R.9
  • 27
    • 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., and Overkleeft H.S. Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits Chem. Biol. 8 2001 913 929
    • (2001) Chem. Biol. , vol.8 , pp. 913-929
    • 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
  • 28
    • 0033525086 scopus 로고    scopus 로고
    • The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
    • Kisselev A.F., Akopian T.N., Woo K.M., and Goldberg A.L. The sizes of peptides generated from protein by mammalian 26 and 20S proteasomes. Implications for understanding the degradative mechanism and antigen presentation J. Biol. Chem. 274 1999 3363 3371
    • (1999) J. Biol. Chem. , vol.274 , pp. 3363-3371
    • Kisselev, A.F.1    Akopian, T.N.2    Woo, K.M.3    Goldberg, A.L.4
  • 29
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., and Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly Cell 96 1999 635 644
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 30
    • 0033553532 scopus 로고    scopus 로고
    • Substrate targeting in the ubiquitin system
    • Laney J., and Hochstrasser M. Substrate targeting in the ubiquitin system Cell 97 1999 427 430
    • (1999) Cell , vol.97 , pp. 427-430
    • Laney, J.1    Hochstrasser, M.2
  • 31
    • 0000870917 scopus 로고    scopus 로고
    • Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae
    • Lee D.H., and Goldberg A.L. Selective inhibitors of the proteasome-dependent and vacuolar pathways of protein degradation in Saccharomyces cerevisiae J. Biol. Chem. 271 1996 27280 27284
    • (1996) J. Biol. Chem. , vol.271 , pp. 27280-27284
    • Lee, D.H.1    Goldberg, A.L.2
  • 32
    • 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., and 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 1997 12616 12621
    • (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
  • 33
    • 0033597646 scopus 로고    scopus 로고
    • Characterization of NFκB activation by detection of green fluorescent protein-tagged IκB degradation in living cells
    • Li X., Fang Y., Zhao X., Jiang X., Duong T., and Kain S.R. Characterization of NFκB activation by detection of green fluorescent protein-tagged IκB degradation in living cells J. Biol. Chem. 274 1999 21244 21250
    • (1999) J. Biol. Chem. , vol.274 , pp. 21244-21250
    • Li, X.1    Fang, Y.2    Zhao, X.3    Jiang, X.4    Duong, T.5    Kain, S.R.6
  • 34
    • 0032567339 scopus 로고    scopus 로고
    • Generation of destabilized green fluorescent protein as a transcription reporter
    • Li X., Zhao X., Fang Y., Jiang X., Duong T., Fan C., Huang C.C., and Kain S.R. Generation of destabilized green fluorescent protein as a transcription reporter J. Biol. Chem. 273 1998 34970 34975
    • (1998) J. Biol. Chem. , vol.273 , pp. 34970-34975
    • Li, X.1    Zhao, X.2    Fang, Y.3    Jiang, X.4    Duong, T.5    Fan, C.6    Huang, C.C.7    Kain, S.R.8
  • 35
    • 0141650794 scopus 로고    scopus 로고
    • Monitoring the ubiquitin/proteasome system in conformational diseases
    • Lindsten K., and Dantuma N.P. Monitoring the ubiquitin/proteasome system in conformational diseases Ageing Res. Rev. 2 2003 433 449
    • (2003) Ageing Res. Rev. , vol.2 , pp. 433-449
    • Lindsten, K.1    Dantuma, N.P.2
  • 36
    • 0037193469 scopus 로고    scopus 로고
    • Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
    • Lindsten K., de Vrij F.M., Verhoef L.G., Fischer D.F., van Leeuwen F.W., Hol E.M., Masucci M.G., and Dantuma N.P. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation J. Cell Biol. 157 2002 417 427
    • (2002) J. Cell Biol. , vol.157 , pp. 417-427
    • Lindsten, K.1    De Vrij, F.M.2    Verhoef, L.G.3    Fischer, D.F.4    Van Leeuwen, F.W.5    Hol, E.M.6    Masucci, M.G.7    Dantuma, N.P.8
  • 39
    • 0042091963 scopus 로고    scopus 로고
    • Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13
    • Lundgren J., Masson P., Realini C.A., and Young P. Use of RNA interference and complementation to study the function of the Drosophila and human 26S proteasome subunit S13 Mol. Cell Biol. 23 2003 5320 5330
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5320-5330
    • Lundgren, J.1    Masson, P.2    Realini, C.A.3    Young, P.4
  • 42
    • 0033564512 scopus 로고    scopus 로고
    • Eponemycin exerts its antitumor effect through the inhibition of proteasome function
    • Meng L., Kwok B.H., Sin N., and Crews C.M. Eponemycin exerts its antitumor effect through the inhibition of proteasome function Cancer Res. 59 1999 2798 2801
    • (1999) Cancer Res. , vol.59 , pp. 2798-2801
    • Meng, L.1    Kwok, B.H.2    Sin, N.3    Crews, C.M.4
  • 43
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity Proc. Natl. Acad. Sci. USA 96 1999 10403 10408
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 44
    • 2342485108 scopus 로고    scopus 로고
    • Proteasome degrades soluble expanded polyglutamine completely and efficiently
    • Michalik A., and Van Broeckhoven C. Proteasome degrades soluble expanded polyglutamine completely and efficiently Neurobiol. Dis. 16 2004 202 211
    • (2004) Neurobiol. Dis. , vol.16 , pp. 202-211
    • Michalik, A.1    Van Broeckhoven, C.2
  • 45
    • 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., and Crews C.M. Lack of proteasome active site allostery as revealed by subunit-specific inhibitors Mol. Cell 7 2001 411 420
    • (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
  • 46
    • 0347765874 scopus 로고    scopus 로고
    • Fluorescent probes for proteolysis: Tools for drug discovery
    • Neefjes J., and Dantuma N.P. Fluorescent probes for proteolysis: Tools for drug discovery Nat. Rev. Drug Discov. 3 2004 58 69
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 58-69
    • Neefjes, J.1    Dantuma, N.P.2
  • 48
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 49
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
    • Reits E., Neijssen J., Herberts C., Benckhuijsen W., Janssen L., Drijfhout J.W., and Neefjes J. A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation Immunity 20 2004 495 506
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1    Neijssen, J.2    Herberts, C.3    Benckhuijsen, W.4    Janssen, L.5    Drijfhout, J.W.6    Neefjes, J.7
  • 50
    • 0031780665 scopus 로고    scopus 로고
    • Ubiquitin, E6-AP, and their role in p53 inactivation
    • Scheffner M. Ubiquitin, E6-AP, and their role in p53 inactivation Pharmacol. Ther. 78 1998 129 139
    • (1998) Pharmacol. Ther. , vol.78 , pp. 129-139
    • Scheffner, M.1
  • 51
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein Annu. Rev. Biochem. 67 1998 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 52
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker S., Sadis S., Rubin D.M., Glickman M., Fu H., Coux O., Wefes I., Finley D., and Vierstra R.D. The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover Mol. Cell Biol. 16 1996 6020 6028
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 53
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel P., and Brand A.H. Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins Nat. Cell Biol. 4 2002 E15 E20
    • (2002) Nat. Cell Biol. , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 54
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky A. The N-end rule: Functions, mysteries, uses Proc. Natl. Acad. Sci. USA 93 1996 12142 12149
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 55
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef L.G., Lindsten K., Masucci M.G., and Dantuma N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins Hum. Mol. Genet. 11 2002 2689 2700
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 56
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban E.U., Reid B.G., Miranker A.D., and Horwich A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA Nature (London) 401 1999 90 93
    • (1999) Nature (London) , vol.401 , pp. 90-93
    • Weber-ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 57
    • 3242730192 scopus 로고    scopus 로고
    • From lysosome to proteasome: The power of yeast in the dissection of proteinase function in cellular regulation and waste disposal
    • Wolf D.H. From lysosome to proteasome: The power of yeast in the dissection of proteinase function in cellular regulation and waste disposal Cell Mol. Life Sci. 61 2004 1601 1614
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 1601-1614
    • Wolf, D.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.