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Volumn 1597, Issue , 2015, Pages 37-46

Signature changes in ubiquilin expression in the R6/2 mouse model of Huntington's disease

Author keywords

Brain; Huntington's disease; Inclusions; Ubiquilin; Ubiquitin

Indexed keywords

PROTEIN; UBIQUILIN 1 PROTEIN; UBIQUILIN 2 PROTEIN; UBIQUILIN 3 PROTEIN; UBIQUILIN 4 PROTEIN; UBIQUILIN PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; SMALL INTERFERING RNA; UBQLN1 PROTEIN, MOUSE; UBQLN2 PROTEIN, MOUSE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 84923233814     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2014.12.008     Document Type: Article
Times cited : (14)

References (45)
  • 2
    • 0034673973 scopus 로고    scopus 로고
    • Molecular cloning, chromosome mapping and characterization of UBQLN3 a testis-specific gene that contains an ubiquitin-like domain
    • D. Conklin, S. Holderman, T.E. Whitmore, M. Maurer, and A.L. Feldhaus Molecular cloning, chromosome mapping and characterization of UBQLN3 a testis-specific gene that contains an ubiquitin-like domain Gene 249 2000 91 98
    • (2000) Gene , vol.249 , pp. 91-98
    • Conklin, D.1    Holderman, S.2    Whitmore, T.E.3    Maurer, M.4    Feldhaus, A.L.5
  • 3
    • 0034703397 scopus 로고    scopus 로고
    • Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein
    • J.D. Davidson, B. Riley, E.N. Burright, L.A. Duvick, H.Y. Zoghbi, and H.T. Orr Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein Hum. Mol. Genet 9 2000 2305 2312
    • (2000) Hum. Mol. Genet , vol.9 , pp. 2305-2312
    • Davidson, J.D.1    Riley, B.2    Burright, E.N.3    Duvick, L.A.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 6
    • 3342879140 scopus 로고    scopus 로고
    • Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates
    • H. Doi, K. Mitsui, M. Kurosawa, Y. Machida, Y. Kuroiwa, and N. Nukina Identification of ubiquitin-interacting proteins in purified polyglutamine aggregates FEBS Lett. 571 2004 171 176
    • (2004) FEBS Lett. , vol.571 , pp. 171-176
    • Doi, H.1    Mitsui, K.2    Kurosawa, M.3    Machida, Y.4    Kuroiwa, Y.5    Nukina, N.6
  • 7
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • S. Elsasser, and D. Finley Delivery of ubiquitinated substrates to protein-unfolding machines Nat. Cell Biol. 7 2005 742 749
    • (2005) Nat. Cell Biol. , vol.7 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 10
    • 33750568162 scopus 로고    scopus 로고
    • Dimerization of ubiquilin is dependent upon the central region of the protein: Evidence that the monomer, but not the dimer, is involved in binding presenilins
    • D.L. Ford, and M.J. Monteiro Dimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilins Biochem. J. 399 2006 397 404
    • (2006) Biochem. J. , vol.399 , pp. 397-404
    • Ford, D.L.1    Monteiro, M.J.2
  • 11
    • 34547640864 scopus 로고    scopus 로고
    • Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2
    • D.L. Ford, and M.J. Monteiro Studies of the role of ubiquitination in the interaction of ubiquilin with the loop and carboxyl terminal regions of presenilin-2 Biochemistry 46 2007 8827 8837
    • (2007) Biochemistry , vol.46 , pp. 8827-8837
    • Ford, D.L.1    Monteiro, M.J.2
  • 12
    • 37849018692 scopus 로고    scopus 로고
    • Ubiquilin antagonizes presenilin and promotes neurodegeneration in Drosophila
    • A. Ganguly, R.M. Feldman, and M. Guo ubiquilin antagonizes presenilin and promotes neurodegeneration in Drosophila Hum. Mol. Genet 17 2008 293 302
    • (2008) Hum. Mol. Genet , vol.17 , pp. 293-302
    • Ganguly, A.1    Feldman, R.M.2    Guo, M.3
  • 14
    • 3242695184 scopus 로고    scopus 로고
    • Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach
    • D.G. Hay, K. Sathasivam, S. Tobaben, B. Stahl, M. Marber, R. Mestril, A. Mahal, D.L. Smith, B. Woodman, and G.P. Bates Progressive decrease in chaperone protein levels in a mouse model of Huntington's disease and induction of stress proteins as a therapeutic approach Hum. Mol. Genet 13 2004 1389 1405
    • (2004) Hum. Mol. Genet , vol.13 , pp. 1389-1405
    • Hay, D.G.1    Sathasivam, K.2    Tobaben, S.3    Stahl, B.4    Marber, M.5    Mestril, R.6    Mahal, A.7    Smith, D.L.8    Woodman, B.9    Bates, G.P.10
  • 15
    • 0141678246 scopus 로고    scopus 로고
    • Standardization and statistical approaches to therapeutic trials in the R6/2 mouse
    • E. Hockly, B. Woodman, A. Mahal, C.M. Lewis, and G. Bates Standardization and statistical approaches to therapeutic trials in the R6/2 mouse Brain Res. Bull. 61 2003 469 479
    • (2003) Brain Res. Bull. , vol.61 , pp. 469-479
    • Hockly, E.1    Woodman, B.2    Mahal, A.3    Lewis, C.M.4    Bates, G.5
  • 17
    • 0141632772 scopus 로고    scopus 로고
    • The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome
    • M.F. Kleijnen, R.M. Alarcon, and P.M. Howley The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome Mol. Biol. Cell. 14 2003 3868 3875
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3868-3875
    • Kleijnen, M.F.1    Alarcon, R.M.2    Howley, P.M.3
  • 19
    • 2442520399 scopus 로고    scopus 로고
    • Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains
    • H.S. Ko, T. Uehara, K. Tsuruma, and Y. Nomura Ubiquilin interacts with ubiquitylated proteins and proteasome through its ubiquitin-associated and ubiquitin-like domains FEBS Lett. 566 2004 110 114
    • (2004) FEBS Lett. , vol.566 , pp. 110-114
    • Ko, H.S.1    Uehara, T.2    Tsuruma, K.3    Nomura, Y.4
  • 20
    • 41949131052 scopus 로고    scopus 로고
    • A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43
    • X. Li, V. Su, W.E. Kurata, C. Jin, and A.F. Lau A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43 J. Biol. Chem. 283 2008 5748 5759
    • (2008) J. Biol. Chem. , vol.283 , pp. 5748-5759
    • Li, X.1    Su, V.2    Kurata, W.E.3    Jin, C.4    Lau, A.F.5
  • 22
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • A.L. Mah, G. Perry, M.A. Smith, and M.J. Monteiro Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation J. Cell Biol. 151 2000 847 862
    • (2000) J. Cell Biol. , vol.151 , pp. 847-862
    • Mah, A.L.1    Perry, G.2    Smith, M.A.3    Monteiro, M.J.4
  • 25
    • 27744468749 scopus 로고    scopus 로고
    • Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin
    • L.K. Massey, A.L. Mah, and M.J. Monteiro Ubiquilin regulates presenilin endoproteolysis and modulates gamma-secretase components, Pen-2 and nicastrin Biochem. J. 391 2005 513 525
    • (2005) Biochem. J. , vol.391 , pp. 513-525
    • Massey, L.K.1    Mah, A.L.2    Monteiro, M.J.3
  • 27
    • 59649110865 scopus 로고    scopus 로고
    • PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation
    • E.N. N'Diaye, K.K. Kajihara, I. Hsieh, H. Morisaki, J. Debnath, and E.J. Brown PLIC proteins or ubiquilins regulate autophagy-dependent cell survival during nutrient starvation EMBO Rep. 10 2009 173 179
    • (2009) EMBO Rep. , vol.10 , pp. 173-179
    • N'Diaye, E.N.1    Kajihara, K.K.2    Hsieh, I.3    Morisaki, H.4    Debnath, J.5    Brown, E.J.6
  • 29
    • 26944465404 scopus 로고    scopus 로고
    • Diverse polyubiquitin interaction properties of ubiquitin-associated domains
    • S. Raasi, R. Varadan, D. Fushman, and C.M. Pickart Diverse polyubiquitin interaction properties of ubiquitin-associated domains Nat. Struct. Mol. Biol. 12 2005 708 714
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 708-714
    • Raasi, S.1    Varadan, R.2    Fushman, D.3    Pickart, C.M.4
  • 30
    • 77957674939 scopus 로고    scopus 로고
    • Ubiquilin at a crossroads in protein degradation pathways
    • C. Rothenberg, and M.J. Monteiro Ubiquilin at a crossroads in protein degradation pathways Autophagy 6 2010 979 980
    • (2010) Autophagy , vol.6 , pp. 979-980
    • Rothenberg, C.1    Monteiro, M.J.2
  • 33
    • 84898728074 scopus 로고    scopus 로고
    • Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease
    • N. Safren, A. El Ayadi, L. Chang, C.E. Terrillion, T.D. Gould, D.F. Boehning, and M.J. Monteiro Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease PLoS One 9 2014 e87513
    • (2014) PLoS One , vol.9 , pp. e87513
    • Safren, N.1    El Ayadi, A.2    Chang, L.3    Terrillion, C.E.4    Gould, T.D.5    Boehning, D.F.6    Monteiro, M.J.7
  • 34
    • 0037059042 scopus 로고    scopus 로고
    • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity
    • H. Sakahira, P. Breuer, M.K. Hayer-Hartl, and F.U. Hartl Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity Proc. Natl. Acad. Sci. U.S.A. 99 Suppl. 4 2002 16412 16418
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16412-16418
    • Sakahira, H.1    Breuer, P.2    Hayer-Hartl, M.K.3    Hartl, F.U.4
  • 37
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • F.O. Walker Huntington's disease Lancet 369 2007 218 228
    • (2007) Lancet , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 38
    • 33644771265 scopus 로고    scopus 로고
    • Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin
    • H. Wang, P.J. Lim, C. Yin, M. Rieckher, B.E. Vogel, and M.J. Monteiro Suppression of polyglutamine-induced toxicity in cell and animal models of Huntington's disease by ubiquilin Hum. Mol. Genet 15 2006 1025 1041
    • (2006) Hum. Mol. Genet , vol.15 , pp. 1025-1041
    • Wang, H.1    Lim, P.J.2    Yin, C.3    Rieckher, M.4    Vogel, B.E.5    Monteiro, M.J.6
  • 39
    • 34447095637 scopus 로고    scopus 로고
    • Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins
    • H. Wang, and M.J. Monteiro Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins Biochem. Biophys. Res. Commun. 360 2007 423 427
    • (2007) Biochem. Biophys. Res. Commun. , vol.360 , pp. 423-427
    • Wang, H.1    Monteiro, M.J.2
  • 41
    • 0033213325 scopus 로고    scopus 로고
    • Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane
    • A.L. Wu, J. Wang, A. Zheleznyak, and E.J. Brown Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane Mol. Cell 4 1999 619 625
    • (1999) Mol. Cell , vol.4 , pp. 619-625
    • Wu, A.L.1    Wang, J.2    Zheleznyak, A.3    Brown, E.J.4
  • 43
    • 0028208253 scopus 로고
    • Identification and characterization of a novel (115 kDa) neurofilament-associated kinase
    • J. Xiao, and M.J. Monteiro Identification and characterization of a novel (115 kDa) neurofilament-associated kinase J. Neurosci. 14 1994 1820 1833
    • (1994) J. Neurosci. , vol.14 , pp. 1820-1833
    • Xiao, J.1    Monteiro, M.J.2
  • 44
    • 84900307676 scopus 로고    scopus 로고
    • A new mutation in ubiquilin gene family and its effect on protein degradation
    • J. Yan, K. Ajroud, F. Fecto, Y. Shi, N. Siddique, H.-X. Deng, and T. Siddique A new mutation in ubiquilin gene family and its effect on protein degradation Neurology 80 P02 2013 168
    • (2013) Neurology , vol.80 , Issue.P02 , pp. 168
    • Yan, J.1    Ajroud, K.2    Fecto, F.3    Shi, Y.4    Siddique, N.5    Deng, H.-X.6    Siddique, T.7
  • 45
    • 0029175420 scopus 로고
    • Spinocerebellar ataxia type 1
    • H.Y. Zoghbi Spinocerebellar ataxia type 1 Clin. Neurosci. 3 1995 5 11
    • (1995) Clin. Neurosci. , vol.3 , pp. 5-11
    • Zoghbi, H.Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.