메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Facilitated tau degradation by USP14 aptamers via enhanced proteasome activity

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; PROTEASOME; PROTEIN BINDING; RECOMBINANT PROTEIN; TAU PROTEIN; UBIQUITIN THIOLESTERASE; USP14 PROTEIN, HUMAN;

EID: 84930651495     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep10757     Document Type: Article
Times cited : (51)

References (38)
  • 1
    • 59649115172 scopus 로고    scopus 로고
    • Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination
    • Baugh, J. M., Viktorova, E. G. & Pilipenko, E. V. Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination. J Mol Biol 386, 814-827 (2009
    • (2009) J Mol Biol , vol.386 , pp. 814-827
    • Baugh, J.M.1    Viktorova, E.G.2    Pilipenko, E.V.3
  • 2
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley, D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78, 477-513 (2009
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 3
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-Associated deubiquitinating enzymes
    • R110.003871
    • Lee, M. J., Lee, B. H., Hanna, J., King, R. W. & Finley, D. Trimming of ubiquitin chains by proteasome-Associated deubiquitinating enzymes. Mol Cell Proteomics 10, R110.003871 (2011
    • (2011) Mol Cell Proteomics , vol.10
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 4
    • 0036753063 scopus 로고    scopus 로고
    • Multiple associated proteins regulate proteasome structure and function
    • Leggett, D. S., et al. Multiple associated proteins regulate proteasome structure and function. Mol Cell 10, 495-507 (2002
    • (2002) Mol Cell , vol.10 , pp. 495-507
    • Leggett, D.S.1
  • 5
    • 33748188085 scopus 로고    scopus 로고
    • Proteasome recruitment and activation of the uch37 deubiquitinating enzyme by adrm1
    • Yao, T., et al Proteasome Recruitment and Activation of the Uch37 Deubiquitinating Enzyme by Adrm1. Nat Cell Biol 8, 994-1002 (2006
    • (2006) Nat cell biol , vol.8 , pp. 994-1002
    • Yao, T.1
  • 6
    • 33749049581 scopus 로고    scopus 로고
    • Deubiquitinating enzyme ubp6 functions noncatalytically to delay proteasomal degradation
    • Hanna, J., et al. Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation. Cell 127, 99-111 (2006
    • (2006) Cell , vol.127 , pp. 99-111
    • Hanna, J.1
  • 7
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of usp14
    • Lee, B H., et Al. Enhancement of Proteasome Activity by A Small-molecule Inhibitor of Usp14. Nature 467, 179-184 (2010
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1
  • 8
    • 84872773589 scopus 로고    scopus 로고
    • Functions of the 19s complex in proteasomal degradation
    • Liu, C.-W. & Jacobson, D. Functions of the 19S complex in proteasomal degradation. Trends Biochem Sci 38, 103-110 (2013Z
    • (2013) Trends Biochem Sci , vol.38 , pp. 103-110
    • Liu, C.-W.1    Jacobson, D.2
  • 9
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: Rna ligands to bacteriophage t4 dna polymerase
    • Tuerk, C. & Gold, L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science 249, 505-510 (1990
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 10
    • 0025074907 scopus 로고
    • In vitro selection of rna molecules that bind specific ligands
    • Ellington, A. D. & Szostak, J. W. In vitro selection of RNA molecules that bind specific ligands. Nature 346, 818-822 (1990
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 11
    • 0034051357 scopus 로고    scopus 로고
    • A novel rna motif that binds efficiently and specifically to the ttat protein of hiv and inhibits the transactivation by tat of transcription in vitro and in vivo
    • Yamamoto, R., et al. A novel RNA motif that binds efficiently and specifically to the Ttat protein of HIV and inhibits the transactivation by Tat of transcription in vitro and in vivo. Genes Cells 5, 371-388 (2000
    • (2000) Genes Cells , vol.5 , pp. 371-388
    • Yamamoto, R.1
  • 12
    • 0026651981 scopus 로고
    • Rna pseudoknots that inhibit human immunodeficiency virus type 1 reverse transcriptase
    • Tuerk, C., MacDougal, S. & Gold, L. RNA pseudoknots that inhibit human immunodeficiency virus type 1 reverse transcriptase. Proc Natl Acad Sci USA 89, 6988-6992 (1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6988-6992
    • Tuerk, C.1    MacDougal, S.2    Gold, L.3
  • 13
    • 0033938340 scopus 로고    scopus 로고
    • Isolation and characterization of rna aptamers specific for the hepatitis c virus nonstructural protein 3 protease
    • Fukuda, K., et al. Isolation and characterization of RNA aptamers specific for the hepatitis C virus nonstructural protein 3 protease. Eur J Biochem 267, 3685-3694 (2000
    • (2000) Eur J Biochem , vol.267 , pp. 3685-3694
    • Fukuda, K.1
  • 14
    • 3342877385 scopus 로고    scopus 로고
    • Isolation of specific and high-Affinity rna aptamers against ns3 helicase domain of hepatitis c virus
    • Hwang, B., et al. Isolation of specific and high-Affinity RNA aptamers against NS3 helicase domain of hepatitis C virus. RNA 10, 1277-1290 (2004
    • (2004) RNA , vol.10 , pp. 1277-1290
    • Hwang, B.1
  • 15
    • 0036200412 scopus 로고    scopus 로고
    • Selection of rna aptamers that are specific and high-Affinity ligands of the hepatitis c virus rna-dependent rna polymerase
    • Biroccio, A., Hamm, J., Incitti, I., De Francesco, R. & Tomei, L. Selection of RNA aptamers that are specific and high-Affinity ligands of the hepatitis C virus RNA-dependent RNA polymerase. J Virol 76, 3688-3696 (2002
    • (2002) J Virol , vol.76 , pp. 3688-3696
    • Biroccio, A.1    Hamm, J.2    Incitti, I.3    De Francesco, R.4    Tomei, L.5
  • 16
    • 37549040255 scopus 로고    scopus 로고
    • Isolation of inhibitory rna aptamers against severe acute respiratory syndrome (sars) coronavirus ntpase/helicase
    • Jang, K. J., Lee, N. R., Yeo, W. S., Jeong, Y. J. & Kim, D. E. Isolation of inhibitory RNA aptamers against severe acute respiratory syndrome (SARS) coronavirus NTPase/Helicase. Biochem Biophys Res Commun 366, 738-744 (2008
    • (2008) Biochem Biophys Res Commun , vol.366 , pp. 738-744
    • Jang, K.J.1    Lee, N.R.2    Yeo, W.S.3    Jeong, Y.J.4    Kim, D.E.5
  • 17
    • 0037099536 scopus 로고    scopus 로고
    • Identification and characterization of nuclease-stabilized rna molecules that bind human prostate cancer cells via the prostate-specific membrane antigen
    • Lupold, S. E., Hicke, B. J., Lin, Y. & Coffey, D. S. Identification and characterization of nuclease-stabilized RNA molecules that bind human prostate cancer cells via the prostate-specific membrane antigen. Cancer Res 62, 4029-4033 (2002
    • (2002) Cancer Res , vol.62 , pp. 4029-4033
    • Lupold, S.E.1    Hicke, B.J.2    Lin, Y.3    Coffey, D.S.4
  • 21
    • 84883185607 scopus 로고    scopus 로고
    • Deubiquitination of dishevelled by usp14 is required for wnt signaling
    • Jung, H., et al. Deubiquitination of Dishevelled by Usp14 is required for Wnt signaling. Oncogenesis 2, e64 (2013
    • (2013) Oncogenesis , vol.2 , pp. e64
    • Jung, H.1
  • 22
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of usp14
    • Borodovsky, A., et al A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14. EMBO J 20, 5187-5196 (2001
    • (2001) EMBO J , vol.20 , pp. 5187-5196
    • Borodovsky, A.1
  • 23
    • 28844484999 scopus 로고    scopus 로고
    • Preparation of ubiquitinated substrates by the py motif-insertion method for monitoring 26s proteasome activity
    • Saeki, Y., Isono, E. & Toh, E. A. Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity. Methods Enzymol 399, 215-227 (2005
    • (2005) Methods Enzymol , vol.399 , pp. 215-227
    • Saeki, Y.1    Isono, E.2    Toh, E.A.3
  • 24
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65, 55-63 (1983
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 25
    • 34447498400 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in a cell culture model of tauopathy
    • Bandyopadhyay, B., Li, G., Yin, H. & Kuret, J. Tau aggregation and toxicity in a cell culture model of tauopathy. J Biol Chem 282, 16454-16464 (2007
    • (2007) J Biol Chem , vol.282 , pp. 16454-16464
    • Bandyopadhyay, B.1    Li, G.2    Yin, H.3    Kuret, J.4
  • 26
    • 33644670152 scopus 로고    scopus 로고
    • An integrated mass spectrometry-based proteomic approach: Quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (qtax) to decipher the 26 s proteasome-interacting network
    • Guerrero, C., Tagwerker, C., Kaiser, P. & Huang, L. An integrated mass spectrometry-based proteomic approach: quantitative analysis of tandem affinity-purified in vivo cross-linked protein complexes (QTAX) to decipher the 26 S proteasome-interacting network. Mol Cell Proteomics 5, 366-378 (2006
    • (2006) Mol Cell Proteomics , vol.5 , pp. 366-378
    • Guerrero, C.1    Tagwerker, C.2    Kaiser, P.3    Huang, L.4
  • 27
    • 0031745782 scopus 로고    scopus 로고
    • Using reliability information to annotate rna secondary structures
    • Zuker, M. & Jacobson, A. B. Using reliability information to annotate RNA secondary structures. RNA 4, 669-679 (1998
    • (1998) RNA , vol.4 , pp. 669-679
    • Zuker, M.1    Jacobson, A.B.2
  • 28
    • 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 426, 895-899 (2003
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 29
    • 84878114130 scopus 로고    scopus 로고
    • Tau degradation: The ubiquitin-proteasome system versus the autophagy-lysosome system
    • Lee, M. J., Lee, J. H. & Rubinsztein, D. C. Tau degradation: the ubiquitin-proteasome system versus the autophagy-lysosome system. Prog Neurobiol 105, 49-59 (2013
    • (2013) Prog Neurobiol , vol.105 , pp. 49-59
    • Lee, M.J.1    Lee, J.H.2    Rubinsztein, D.C.3
  • 30
    • 0036789647 scopus 로고    scopus 로고
    • Proteasomal degradation of tau protein
    • David, D. C., et al. Proteasomal degradation of tau protein. J Neurochem 83, 176-185 (2002
    • (2002) J Neurochem , vol.83 , pp. 176-185
    • David, D.C.1
  • 32
    • 34249864120 scopus 로고    scopus 로고
    • A proteasome for all occasions
    • Hanna, J. & Finley, D. A proteasome for all occasions. FEBS Lett 581, 2854-2861 (2007
    • (2007) FEBS Lett , vol.581 , pp. 2854-2861
    • Hanna, J.1    Finley, D.2
  • 33
    • 0347364648 scopus 로고    scopus 로고
    • A tenascin-c aptamer identified by tumor cell selex: Systematic evolution of ligands by exponential enrichment
    • Daniels, D. A., Chen, H., Hicke, B. J., Swiderek, K. M. & Gold, L. A tenascin-C aptamer identified by tumor cell SELEX: systematic evolution of ligands by exponential enrichment. Proc Natl Acad Sci USA 100, 15416-15421 (2003
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15416-15421
    • Daniels, D.A.1    Chen, H.2    Hicke, B.J.3    Swiderek, K.M.4    Gold, L.5
  • 34
    • 16644376270 scopus 로고    scopus 로고
    • Targeting ku protein for sensitizing of breast cancer cells to dnadamage
    • Zhang, L., Yoo, S., Dritschilo, A., Belyaev, I. & Soldatenkov, V. Targeting Ku protein for sensitizing of breast cancer cells to DNAdamage. Int J Mol Med 14, 153-159 (2004
    • (2004) Int J Mol Med , vol.14 , pp. 153-159
    • Zhang, L.1    Yoo, S.2    Dritschilo, A.3    Belyaev, I.4    Soldatenkov, V.5
  • 35
    • 34447519933 scopus 로고    scopus 로고
    • Clinical update: New treatments for age-related macular degeneration
    • Wong, T. Y., Liew, G. & Mitchell, P. Clinical update: new treatments for age-related macular degeneration. Lancet 370, 204-206 (2007
    • (2007) Lancet , vol.370 , pp. 204-206
    • Wong, T.Y.1    Liew, G.2    Mitchell, P.3
  • 36
    • 79954590790 scopus 로고    scopus 로고
    • Enhancement of proteasome function by pa28 & alpha; Overexpression protects against oxidative stress
    • Li, J., Powell, S. R. & Wang, X. Enhancement of proteasome function by PA28 & alpha; overexpression protects against oxidative stress. FASEB J 25, 883-893 (2011
    • (2011) FASEB J , vol.25 , pp. 883-893
    • Li, J.1    Powell, S.R.2    Wang, X.3
  • 37
    • 80052386730 scopus 로고    scopus 로고
    • Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice
    • Li, J., et al. Enhancement of proteasomal function protects against cardiac proteinopathy and ischemia/reperfusion injury in mice. J Clin Invest 121, 3689-3700 (2011
    • (2011) J Clin Invest , vol.121 , pp. 3689-3700
    • Li, J.1
  • 38
    • 34249007126 scopus 로고    scopus 로고
    • A ubiquitin stress response induces altered proteasome composition
    • Hanna, J., Meides, A., Zhang, D. P. & Finley, D. A ubiquitin stress response induces altered proteasome composition. Cell 129, 747-759 (2007
    • (2007) Cell , vol.129 , pp. 747-759
    • Hanna, J.1    Meides, A.2    Zhang, D.P.3    Finley, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.