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Volumn 10, Issue 11, 2015, Pages 2537-2543

Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation Regions

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEASOME; INITIATION FACTOR; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84947760173     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.5b00554     Document Type: Article
Times cited : (12)

References (31)
  • 2
    • 84927176668 scopus 로고    scopus 로고
    • SCF ubiquitin ligase-targeted therapies
    • Skaar, J. R., Pagan, J. K., and Pagano, M. (2014) SCF ubiquitin ligase-targeted therapies Nat. Rev. Drug Discovery 13, 889-903 10.1038/nrd4432
    • (2014) Nat. Rev. Drug Discovery , vol.13 , pp. 889-903
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 3
    • 84938912227 scopus 로고    scopus 로고
    • An inhibitor of ubiquitin conjugation and aggresome formation
    • An, H. and Statsyuk, A. V. (2015) An inhibitor of ubiquitin conjugation and aggresome formation Chem. Sci. 6, 5235 10.1039/C5SC01351H
    • (2015) Chem. Sci. , vol.6 , pp. 5235
    • An, H.1    Statsyuk, A.V.2
  • 4
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., and Matouschek, A. (2004) An unstructured initiation site is required for efficient proteasome-mediated degradation Nat. Struct. Mol. Biol. 11, 830-837 10.1038/nsmb814
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 5
    • 84896032345 scopus 로고    scopus 로고
    • Paradigms of protein degradation by the proteasome
    • Inobe, T. and Matouschek, A. (2014) Paradigms of protein degradation by the proteasome Curr. Opin. Struct. Biol. 24, 156-164 10.1016/j.sbi.2014.02.002
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 156-164
    • Inobe, T.1    Matouschek, A.2
  • 6
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M. P., Prakash, S., Iwakura, M., and Matouschek, A. (2001) ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal Mol. Cell 7, 627-637 10.1016/S1097-2765(01)00209-X
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 7
    • 79951850741 scopus 로고    scopus 로고
    • Defining the geometry of the two-component proteasome degron
    • Inobe, T., Fishbain, S., Prakash, S., and Matouschek, A. (2011) Defining the geometry of the two-component proteasome degron Nat. Chem. Biol. 7, 161-167 10.1038/nchembio.521
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 161-167
    • Inobe, T.1    Fishbain, S.2    Prakash, S.3    Matouschek, A.4
  • 9
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells Science 281, 269-272 10.1126/science.281.5374.269
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 10
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin, B. R., Giepmans, B. N., Adams, S. R., and Tsien, R. Y. (2005) Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity Nat. Biotechnol. 23, 1308-1314 10.1038/nbt1136
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.2    Adams, S.R.3    Tsien, R.Y.4
  • 11
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams, S. R., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., and Tsien, R. Y. (2002) New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications J. Am. Chem. Soc. 124, 6063-6076 10.1021/ja017687n
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 12
    • 0037144567 scopus 로고    scopus 로고
    • Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
    • Lee, C., Prakash, S., and Matouschek, A. (2002) Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel J. Biol. Chem. 277, 34760-34765 10.1074/jbc.M204750200
    • (2002) J. Biol. Chem. , vol.277 , pp. 34760-34765
    • Lee, C.1    Prakash, S.2    Matouschek, A.3
  • 13
    • 47349126421 scopus 로고    scopus 로고
    • Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants
    • Onitsuka, M., Kamikubo, H., Yamazaki, Y., and Kataoka, M. (2008) Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants Proteins: Struct., Funct., Genet. 72, 837-847 10.1002/prot.21978
    • (2008) Proteins: Struct., Funct., Genet. , vol.72 , pp. 837-847
    • Onitsuka, M.1    Kamikubo, H.2    Yamazaki, Y.3    Kataoka, M.4
  • 14
    • 84866717363 scopus 로고    scopus 로고
    • Rapid production of antigen-specific monoclonal antibodies from a variety of animals
    • Kurosawa, N., Yoshioka, M., Fujimoto, R., Yamagishi, F., and Isobe, M. (2012) Rapid production of antigen-specific monoclonal antibodies from a variety of animals BMC Biol. 10, 80 10.1186/1741-7007-10-80
    • (2012) BMC Biol. , vol.10 , pp. 80
    • Kurosawa, N.1    Yoshioka, M.2    Fujimoto, R.3    Yamagishi, F.4    Isobe, M.5
  • 15
    • 0033674452 scopus 로고    scopus 로고
    • A ubiquitin-based tagging system for controlled modulation of protein stability
    • Stack, J. H., Whitney, M., Rodems, S. M., and Pollok, B. A. (2000) A ubiquitin-based tagging system for controlled modulation of protein stability Nat. Biotechnol. 18, 1298-1302 10.1038/82422
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1298-1302
    • Stack, J.H.1    Whitney, M.2    Rodems, S.M.3    Pollok, B.A.4
  • 16
    • 59649115172 scopus 로고    scopus 로고
    • Proteasomes Can Degrade a Significant Proportion of Cellular Proteins Independent of Ubiquitination
    • Baugh, J. M., Viktorova, E. G., and Pilipenko, E. V. (2009) Proteasomes Can Degrade a Significant Proportion of Cellular Proteins Independent of Ubiquitination J. Mol. Biol. 386, 814-827 10.1016/j.jmb.2008.12.081
    • (2009) J. Mol. Biol. , vol.386 , pp. 814-827
    • Baugh, J.M.1    Viktorova, E.G.2    Pilipenko, E.V.3
  • 17
    • 0033453239 scopus 로고    scopus 로고
    • Attenuation of green fluorescent protein half-life in mammalian cells
    • Corish, P. and Tyler-Smith, C. (1999) Attenuation of green fluorescent protein half-life in mammalian cells Protein Eng., Des. Sel. 12, 1035-1040 10.1093/protein/12.12.1035
    • (1999) Protein Eng., Des. Sel. , vol.12 , pp. 1035-1040
    • Corish, P.1    Tyler-Smith, C.2
  • 18
    • 0345701307 scopus 로고    scopus 로고
    • Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate
    • Zhang, M., Pickart, C. M., and Coffino, P. (2003) Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate EMBO J. 22, 1488-1496 10.1093/emboj/cdg158
    • (2003) EMBO J. , vol.22 , pp. 1488-1496
    • Zhang, M.1    Pickart, C.M.2    Coffino, P.3
  • 19
    • 84880917833 scopus 로고    scopus 로고
    • The role of SRY-related HMG box transcription factor 4 (SOX4) in tumorigenesis and metastasis: Friend or foe?
    • Vervoort, S. J., van Boxtel, R., and Coffer, P. J. (2013) The role of SRY-related HMG box transcription factor 4 (SOX4) in tumorigenesis and metastasis: friend or foe? Oncogene 32, 3397-3409 10.1038/onc.2012.506
    • (2013) Oncogene , vol.32 , pp. 3397-3409
    • Vervoort, S.J.1    Van Boxtel, R.2    Coffer, P.J.3
  • 24
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • Gsponer, J., Futschik, M. E., Teichmann, S. A., and Babu, M. M. (2008) Tight regulation of unstructured proteins: from transcript synthesis to protein degradation Science (Washington, DC, U. S.) 322, 1365-1368 10.1126/science.1163581
    • (2008) Science (Washington, DC, U. S.) , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 26
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome inhibitors: An expanding army attacking a unique target
    • Kisselev, A. F., van der Linden, W. A., and Overkleeft, H. S. (2012) Proteasome inhibitors: an expanding army attacking a unique target Chem. Biol. 19, 99-115 10.1016/j.chembiol.2012.01.003
    • (2012) Chem. Biol. , vol.19 , pp. 99-115
    • Kisselev, A.F.1    Van Der Linden, W.A.2    Overkleeft, H.S.3
  • 27
    • 79952399087 scopus 로고    scopus 로고
    • Beyond natural antibodies: The power of in vitro display technologies
    • Bradbury, A. R., Sidhu, S., Dubel, S., and McCafferty, J. (2011) Beyond natural antibodies: the power of in vitro display technologies Nat. Biotechnol. 29, 245-254 10.1038/nbt.1791
    • (2011) Nat. Biotechnol. , vol.29 , pp. 245-254
    • Bradbury, A.R.1    Sidhu, S.2    Dubel, S.3    McCafferty, J.4
  • 28
    • 84907931054 scopus 로고    scopus 로고
    • Recent progress in generating intracellular functional antibody fragments to target and trace cellular components in living cells
    • Kaiser, P. D., Maier, J., Traenkle, B., Emele, F., and Rothbauer, U. (2014) Recent progress in generating intracellular functional antibody fragments to target and trace cellular components in living cells Biochim. Biophys. Acta, Proteins Proteomics 1844, 1933-1942 10.1016/j.bbapap.2014.04.019
    • (2014) Biochim. Biophys. Acta, Proteins Proteomics , vol.1844 , pp. 1933-1942
    • Kaiser, P.D.1    Maier, J.2    Traenkle, B.3    Emele, F.4    Rothbauer, U.5
  • 29
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide, A., Bailey, C. W., Huang, X., and Koide, S. (1998) The fibronectin type III domain as a scaffold for novel binding proteins J. Mol. Biol. 284, 1141-1151 10.1006/jmbi.1998.2238
    • (1998) J. Mol. Biol. , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 30
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond, J. B. and Cohen, G. M. (2002) The proteasome: a novel target for cancer chemotherapy Leukemia 16, 433-443 10.1038/sj.leu.2402417
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 31
    • 0033596124 scopus 로고    scopus 로고
    • Aberrant rel/nfkb genes and activity in human cancer
    • Rayet, B. and Gelinas, C. (1999) Aberrant rel/nfkb genes and activity in human cancer Oncogene 18, 6938-6947 10.1038/sj.onc.1203221
    • (1999) Oncogene , vol.18 , pp. 6938-6947
    • Rayet, B.1    Gelinas, C.2


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