메뉴 건너뛰기




Volumn 75, Issue 5, 2004, Pages 347-357

SQSTM1 and Paget's disease of bone

Author keywords

p62; Paget's disease of bone; SQSTM1; UBA domain; Ubiquitin

Indexed keywords

PROTEIN; SEQUESTOSOME 1 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 11944268320     PISSN: 0171967X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00223-004-0041-0     Document Type: Article
Times cited : (59)

References (99)
  • 3
    • 0022634225 scopus 로고
    • Osteogenic sarcoma of bones and soft tissues in older persons. A clinicopathologic analysis of 117 patients older than 60 years
    • Huvos AG (1986) Osteogenic sarcoma of bones and soft tissues in older persons. A clinicopathologic analysis of 117 patients older than 60 years. Cancer 57:1442-1449
    • (1986) Cancer , vol.57 , pp. 1442-1449
    • Huvos, A.G.1
  • 4
    • 0013515410 scopus 로고
    • Paget's disease (osteitis deformans) and hereditary
    • Montagu MFA (1949) Paget's disease (osteitis deformans) and hereditary. Am J Hum Genet 1:94-95
    • (1949) Am J Hum Genet , vol.1 , pp. 94-95
    • Montagu, M.F.A.1
  • 5
    • 0028221605 scopus 로고
    • Epidemiological aspects of Paget's disease: Family history and relationship to other medical conditions
    • Siris ES (1994) Epidemiological aspects of Paget's disease: family history and relationship to other medical conditions. Semin Arth Rheum 23:222-225
    • (1994) Semin Arth Rheum , vol.23 , pp. 222-225
    • Siris, E.S.1
  • 8
    • 0034065196 scopus 로고    scopus 로고
    • Familial Paget's disease of bone: Patterns of inheritance and frequency of linkage to chromosome 18q
    • Hocking L, Slee F, Cundy T, Nicholson G, Van Hul W, Ralston SH (2000) Familial Paget's disease of bone: patterns of inheritance and frequency of linkage to chromosome 18q. Bone 26:577-580
    • (2000) Bone , vol.26 , pp. 577-580
    • Hocking, L.1    Slee, F.2    Cundy, T.3    Nicholson, G.4    Van Hul, W.5    Ralston, S.H.6
  • 10
    • 0019745914 scopus 로고
    • The epidemiology of Paget's disease
    • Barker DJ (1981) The epidemiology of Paget's disease. Metab Bone Dis Rel Res 3:231-233
    • (1981) Metab Bone Dis Rel Res , vol.3 , pp. 231-233
    • Barker, D.J.1
  • 11
    • 0030276966 scopus 로고    scopus 로고
    • Seeking the elusive aetiology of Paget's disease: A progress report
    • Siris ES (1996) Seeking the elusive aetiology of Paget's disease: a progress report. J Bone Miner Res 11:1599-1601
    • (1996) J Bone Miner Res , vol.11 , pp. 1599-1601
    • Siris, E.S.1
  • 14
    • 0033827275 scopus 로고    scopus 로고
    • Long-term trends in the incidence of Paget's disease of bone
    • Tiegs RD, Lohse CM, Wollan PC, Melton LJ (2000) Long-term trends in the incidence of Paget's disease of bone. [abstract]. Bone 27:423-427
    • (2000) Bone , vol.27 , pp. 423-427
    • Tiegs, R.D.1    Lohse, C.M.2    Wollan, P.C.3    Melton, L.J.4
  • 15
    • 0035999447 scopus 로고    scopus 로고
    • Paget's disease in an archeological population
    • Rogers J, Jeffrey DR, Watt I (2002) Paget's disease in an archeological population. J Bone Miner Res 17:1127-1134
    • (2002) J Bone Miner Res , vol.17 , pp. 1127-1134
    • Rogers, J.1    Jeffrey, D.R.2    Watt, I.3
  • 19
    • 0038643034 scopus 로고    scopus 로고
    • Phenotypic Characterisation of Early Onset Paget's Disease of Bone Caused by a 27 bp Duplication in the TNFRSF11A Gene
    • Nakatsuka K, Nishizawa K, Ralston SH (2003) Phenotypic Characterisation of Early Onset Paget's Disease of Bone Caused by a 27 bp Duplication in the TNFRSF11A Gene. J Bone Miner Res 18:1381-1385
    • (2003) J Bone Miner Res , vol.18 , pp. 1381-1385
    • Nakatsuka, K.1    Nishizawa, K.2    Ralston, S.H.3
  • 20
    • 0036133351 scopus 로고    scopus 로고
    • Expansile skeletal hyperphosphatasia is caused by a 15-base pair tandem duplication in TNFRSF11A encoding RANK and is allelic to familial expansile osteolysis
    • Whyte MP, Hughes AE (2002) Expansile skeletal hyperphosphatasia is caused by a 15-base pair tandem duplication in TNFRSF11A encoding RANK and is allelic to familial expansile osteolysis. J Bone Miner Res 17:26-29
    • (2002) J Bone Miner Res , vol.17 , pp. 26-29
    • Whyte, M.P.1    Hughes, A.E.2
  • 21
    • 0035171445 scopus 로고    scopus 로고
    • Familial Paget's disease of bone: Nonlinkage to the PDB1 and PDB2 loci on chromosomes 6p and 18q in a large pedigree
    • Good D, Busfield F, Duffy D, Lovelock PK, Resting JB, Cameron DP, Shaw JT (2001) Familial Paget's disease of bone: nonlinkage to the PDB1 and PDB2 loci on chromosomes 6p and 18q in a large pedigree. J Bone Miner Res 16:33-38
    • (2001) J Bone Miner Res , vol.16 , pp. 33-38
    • Good, D.1    Busfield, F.2    Duffy, D.3    Lovelock, P.K.4    Resting, J.B.5    Cameron, D.P.6    Shaw, J.T.7
  • 30
    • 0036094026 scopus 로고    scopus 로고
    • Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone
    • Laurin N, Brown JP, Morissette J, Raymond V (2002) Recurrent mutation of the gene encoding sequestosome 1 (SQSTM1/p62) in Paget disease of bone. Am J Hum Genet 70:1582-1588
    • (2002) Am J Hum Genet , vol.70 , pp. 1582-1588
    • Laurin, N.1    Brown, J.P.2    Morissette, J.3    Raymond, V.4
  • 32
    • 11944265773 scopus 로고    scopus 로고
    • Single base-pair deletion of gene encoding Sequestosome 1 (SQSTM1/p62) in Paget's disease of bone
    • abstract 04:13. Adelaide, Australia
    • Good DA, Busfield F, Duffy D, Kestin J, Shaw TE (2002) Single base-pair deletion of gene encoding Sequestosome 1 (SQSTM1/p62) in Paget's disease of bone. [abstract 04:13]. ANZBMS 12th Annual Scientific Meeting. Adelaide, Australia
    • (2002) ANZBMS 12th Annual Scientific Meeting
    • Good, D.A.1    Busfield, F.2    Duffy, D.3    Kestin, J.4    Shaw, T.E.5
  • 35
    • 0037070216 scopus 로고    scopus 로고
    • Structure and functional properties of the ubiquitin binding protein p62
    • Geetha T, Wooten MW (2002) Structure and functional properties of the ubiquitin binding protein p62. FEBS Lett 512:19-24
    • (2002) FEBS Lett , vol.512 , pp. 19-24
    • Geetha, T.1    Wooten, M.W.2
  • 37
    • 0034599476 scopus 로고    scopus 로고
    • The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway
    • Sanz L, Diaz-Meco MT, Nakano H, Moscat J (2000) The atypical PKC-interacting protein p62 channels NF-kappaB activation by the IL-1-TRAF6 pathway. EMBO J 19:1576-1586
    • (2000) EMBO J , vol.19 , pp. 1576-1586
    • Sanz, L.1    Diaz-Meco, M.T.2    Nakano, H.3    Moscat, J.4
  • 38
    • 0035896518 scopus 로고    scopus 로고
    • The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor
    • Wooten MW, Seibenhener ML, Mamidipudi V, Diaz-Meco MT, Barker PA, Moscat J (2001) The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor. J Biol Chem 276:7709-7712
    • (2001) J Biol Chem , vol.276 , pp. 7709-7712
    • Wooten, M.W.1    Seibenhener, M.L.2    Mamidipudi, V.3    Diaz-Meco, M.T.4    Barker, P.A.5    Moscat, J.6
  • 39
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation
    • Sanz L, Sanchez P, Lallena MJ, Diaz-Meco MT, Moscat J (1999) The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. EMBO J 18:3044-3053
    • (1999) EMBO J , vol.18 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.J.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 40
    • 0043267732 scopus 로고    scopus 로고
    • Genetic regulation of osteoclast development and function
    • Teitelbaum SL, Ross FP (2003) Genetic regulation of osteoclast development and function. Nat Rev Genet 4:638-649
    • (2003) Nat Rev Genet , vol.4 , pp. 638-649
    • Teitelbaum, S.L.1    Ross, F.P.2
  • 42
    • 0033582819 scopus 로고    scopus 로고
    • Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAP) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif
    • Darnay BG, Ni J, Moore PA, Aggarwal BB (1999) Activation of NF-kappaB by RANK requires tumor necrosis factor receptor-associated factor (TRAP) 6 and NF-kappaB-inducing kinase. Identification of a novel TRAF6 interaction motif. J Biol Chem 274:7724-7731
    • (1999) J Biol Chem , vol.274 , pp. 7724-7731
    • Darnay, B.G.1    Ni, J.2    Moore, P.A.3    Aggarwal, B.B.4
  • 45
    • 0035478997 scopus 로고    scopus 로고
    • Mouse models of abnormal skeletal development and homeostasis
    • McLean W, Olsen BR (2001) Mouse models of abnormal skeletal development and homeostasis. Trends Genet 17:S38-43
    • (2001) Trends Genet , vol.17
    • McLean, W.1    Olsen, B.R.2
  • 47
    • 0030911597 scopus 로고    scopus 로고
    • Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein
    • Puls A, Schmidt S, Grawe F, Stabel S (1997) Interaction of protein kinase C zeta with ZIP, a novel protein kinase C-binding protein. Proc Natl Acad Sci USA 94:6191-6196
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6191-6196
    • Puls, A.1    Schmidt, S.2    Grawe, F.3    Stabel, S.4
  • 48
    • 0041625934 scopus 로고    scopus 로고
    • PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62
    • Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL (2003) PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mo1 Cell 12:39-50
    • (2003) Mo1 Cell , vol.12 , pp. 39-50
    • Wilson, M.I.1    Gill, D.J.2    Perisic, O.3    Quinn, M.T.4    Williams, R.L.5
  • 51
    • 0032253214 scopus 로고    scopus 로고
    • p62 and the sequestosome, a novel mechanism for protein metabolism
    • Shin J (1998) p62 and the sequestosome, a novel mechanism for protein metabolism. Arch Pharm Res 21:629-633
    • (1998) Arch Pharm Res , vol.21 , pp. 629-633
    • Shin, J.1
  • 52
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: Possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I (2002) Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation. Neuropathol Appl Neurobiol 28:228-237
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 54
    • 0029894586 scopus 로고    scopus 로고
    • Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain
    • Joung I, Strominger JL, Shin J (1996) Molecular cloning of a phosphotyrosine-independent ligand of the p56lck SH2 domain. Proc Natl Acad Sci USA 93:5991-5995
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5991-5995
    • Joung, I.1    Strominger, J.L.2    Shin, J.3
  • 56
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M, Rogers SW (1996) PEST sequences and regulation by proteolysis. Trends Biochem Sci 21:267-271
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 58
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain; a sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K, Bucher P (1996) The UBA domain; a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21:172-173
    • (1996) Trends Biochem Sci , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 61
    • 0034514655 scopus 로고    scopus 로고
    • Ubiquitination and deubiquitination: Targeting of proteins for degradation by the proteasome
    • Wilkinson KD (2000) Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin Cell Dev Biol 11:141-148
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 141-148
    • Wilkinson, K.D.1
  • 63
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson ES, Ma PC, Ota IM, Varshavsky A (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem 270:17442-17456
    • (1995) J Biol Chem , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 65
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan JM, Haguenauer-Tsapis R (1997) Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J 16:5847-5854
    • (1997) EMBO J , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 66
    • 0028847989 scopus 로고
    • A ubiquitin mutant with specific defects in DNA repair and multi-ubiquitination
    • Spence J, Sadis S, Haas AL, Finley D (1995) A ubiquitin mutant with specific defects in DNA repair and multi-ubiquitination. Mol Cell Biol 15:1265-1273
    • (1995) Mol Cell Biol , vol.15 , pp. 1265-1273
    • Spence, J.1    Sadis, S.2    Haas, A.L.3    Finley, D.4
  • 67
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103:351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 69
    • 0036150184 scopus 로고    scopus 로고
    • Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6
    • Mizukami J, Takaesu G, Akatsuka H, Sakurai H, Ninomiya-Tsuji J, Matsumoto K, Sakurai N (2002) Receptor activator of NF-kappaB ligand (RANKL) activates TAK1 mitogen-activated protein kinase kinase kinase through a signaling complex containing RANK, TAB2, and TRAF6. Mol Cell Biol 22:992-1000
    • (2002) Mol Cell Biol , vol.22 , pp. 992-1000
    • Mizukami, J.1    Takaesu, G.2    Akatsuka, H.3    Sakurai, H.4    Ninomiya-Tsuji, J.5    Matsumoto, K.6    Sakurai, N.7
  • 70
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki E, Hatzivassiliou E, Tsichritzis T, Fanner H, Ashworth A, Mosialos G (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424:793-796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Fanner, H.4    Ashworth, A.5    Mosialos, G.6
  • 74
    • 0034762028 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
    • Chen L, Shinde U, Ortolan TG, Madura K (2001) Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly. EMBO Rep 2:933-938
    • (2001) EMBO Rep , vol.2 , pp. 933-938
    • Chen, L.1    Shinde, U.2    Ortolan, T.G.3    Madura, K.4
  • 75
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi M, Sasaki T, Nishimoto T, Kobayashi H (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc Natl Acad Sci USA 99:745-750
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 76
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K, Bucher P (1996) The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem Sci 21:172-173
    • (1996) Trends Biochem Sci , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 77
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci USA 95:5857-5864
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 78
    • 0141844580 scopus 로고    scopus 로고
    • Structure of the UBA domain of p62 (SQSTM1) and implications for mutations which cause Paget's disease of bone
    • Ciani B, Layfield R, Cavey JR, Sheppard PW, Searle MS (2003) Structure of the UBA domain of p62 (SQSTM1) and implications for mutations which cause Paget's disease of bone. J Biol Chem 278:37409-37412
    • (2003) J Biol Chem , vol.278 , pp. 37409-37412
    • Ciani, B.1    Layfield, R.2    Cavey, J.R.3    Sheppard, P.W.4    Searle, M.S.5
  • 79
    • 0029809134 scopus 로고    scopus 로고
    • p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins
    • Vadlamudi RK, Joung I, Strominger JL, Shin J (1996) p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J Biol Chem 271:20235-20237
    • (1996) J Biol Chem , vol.271 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 80
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen L, Madura K (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol Cell Biol 22:4902-4913
    • (2002) Mol Cell Biol , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 81
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 UBA domains inhibit 26S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • Raasi S, Pickart CM (2003) Rad23 UBA domains inhibit 26S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J Biol Chem 278:8951-8959
    • (2003) J Biol Chem , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 82
    • 0037472654 scopus 로고    scopus 로고
    • Ubiquitin-binding proteins protect ubiquitin conjugates from disassembly
    • Hartmann-Petersen R, Hendil KB, Gordon C (2003) Ubiquitin-binding proteins protect ubiquitin conjugates from disassembly. FEBS Lett 535:77-81
    • (2003) FEBS Lett , vol.535 , pp. 77-81
    • Hartmann-Petersen, R.1    Hendil, K.B.2    Gordon, C.3
  • 85
    • 0033634977 scopus 로고    scopus 로고
    • TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway
    • Takaesu G, Kishida S, Hiyama A, Yamaguchi K, Shibuya H, Irie K, Ninomiya-Tsuji J, Matsumoto K (2000) TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Mol Cell 5:649-658
    • (2000) Mol Cell , vol.5 , pp. 649-658
    • Takaesu, G.1    Kishida, S.2    Hiyama, A.3    Yamaguchi, K.4    Shibuya, H.5    Irie, K.6    Ninomiya-Tsuji, J.7    Matsumoto, K.8
  • 86
    • 0019996989 scopus 로고
    • Ultrastructural features of the osteoclasts from Paget's disease of bone in relation to a viral aetiology
    • Harvey L, Gray T, Beneton MNC, Douglas DL, Kanis JA, Russell RGG (1982) Ultrastructural features of the osteoclasts from Paget's disease of bone in relation to a viral aetiology. J Clin Path 35:771-779
    • (1982) J Clin Path , vol.35 , pp. 771-779
    • Harvey, L.1    Gray, T.2    Beneton, M.N.C.3    Douglas, D.L.4    Kanis, J.A.5    Russell, R.G.G.6
  • 87
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, Clark HB, Zoghbi HY, Orr HT (1998) Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 95:41-53
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 88
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95:55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 93
    • 0034645063 scopus 로고    scopus 로고
    • Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation
    • Mah AL, Perry G, Smith MA, Monteiro MJ (2000) Identification of ubiquilin, a novel presenilin interactor that increases presenilin protein accumulation. J Cell Biol 151:847-862
    • (2000) J Cell Biol , vol.151 , pp. 847-862
    • Mah, A.L.1    Perry, G.2    Smith, M.A.3    Monteiro, M.J.4
  • 94
    • 0141632772 scopus 로고    scopus 로고
    • The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome
    • Kleijnen MF, Alarcon RM, Howley PM (2003) The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Mol Biol Cell 14:3868-3875
    • (2003) Mol Biol Cell , vol.14 , pp. 3868-3875
    • Kleijnen, M.F.1    Alarcon, R.M.2    Howley, P.M.3
  • 97
    • 0141428795 scopus 로고    scopus 로고
    • Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders
    • Layfield R, Cavey JR, Lowe J (2003) Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders. Ageing Res Rev 2:343-356
    • (2003) Ageing Res Rev , vol.2 , pp. 343-356
    • Layfield, R.1    Cavey, J.R.2    Lowe, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.