메뉴 건너뛰기




Volumn 9, Issue 3, 2014, Pages

Correction: Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins (PLoS ONE (2014) 9, 3, (e90452) DOI: 10.1371/journal.pone.0090452);Casein kinase II induced polymerization of soluble TDP-43 into filaments is inhibited by heat shock proteins

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; HEAT SHOCK PROTEIN; TAR DNA BINDING PROTEIN; UBIQUITIN; DNA BINDING PROTEIN; HEAT SHOCK PROTEIN 90; PROTEIN TDP-43;

EID: 84897052708     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0100026     Document Type: Erratum
Times cited : (43)

References (57)
  • 3
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Epub 2008 Feb 1628
    • Sreedharan J, Blair IP, Tripathi VB, Hu X, Vance C, et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319: 1668-1672. Epub 2008 Feb 1628.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5
  • 5
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford NJ, Zhang YJ, Baker M, Gass JM, Finch NA, et al. (2008) Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis. PLoS Genet 4: e1000193.
    • (2008) PLoS Genet , vol.4
    • Rutherford, N.J.1    Zhang, Y.J.2    Baker, M.3    Gass, J.M.4    Finch, N.A.5
  • 6
    • 84881337350 scopus 로고    scopus 로고
    • TARDBP Mutation Analysis in TDP-43 Proteinopathies and Deciphering the Toxicity of Mutant TDP-43
    • Gendron TF, Rademakers R, Petrucelli L (2012) TARDBP Mutation Analysis in TDP-43 Proteinopathies and Deciphering the Toxicity of Mutant TDP-43. J Alzheimers Dis 29: 29.
    • (2012) J Alzheimers Dis , vol.29 , pp. 29
    • Gendron, T.F.1    Rademakers, R.2    Petrucelli, L.3
  • 7
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Epub 32005 Sep 37512
    • Buratti E, Brindisi A, Giombi M, Tisminetzky S, Ayala YM, et al. (2005) TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 280: 37572-37584. Epub 32005 Sep 37512.
    • (2005) J Biol Chem , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3    Tisminetzky, S.4    Ayala, Y.M.5
  • 8
    • 77956155794 scopus 로고    scopus 로고
    • Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43
    • Epub 22010 Jun 26316
    • Fuentealba RA, Udan M, Bell S, Wegorzewska I, Shao J, et al. (2010) Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43. J Biol Chem 285: 26304-26314. Epub 22010 Jun 26316.
    • (2010) J Biol Chem , vol.285 , pp. 26304-26314
    • Fuentealba, R.A.1    Udan, M.2    Bell, S.3    Wegorzewska, I.4    Shao, J.5
  • 9
    • 78149461229 scopus 로고    scopus 로고
    • Tar DNA binding protein-43 (TDP-43) associates with stress granules: Analysis of cultured cells and pathological brain tissue
    • Liu-Yesucevitz L, Bilgutay A, Zhang YJ, Vanderweyde T, Citro A, et al. (2010) Tar DNA binding protein-43 (TDP-43) associates with stress granules: analysis of cultured cells and pathological brain tissue. PLoS One 5: e13250.
    • (2010) PLoS One , vol.5
    • Liu-Yesucevitz, L.1    Bilgutay, A.2    Zhang, Y.J.3    Vanderweyde, T.4    Citro, A.5
  • 10
    • 79960040173 scopus 로고    scopus 로고
    • An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
    • doi: 810.1038/nsmb.2053
    • Guo W, Chen Y, Zhou X, Kar A, Ray P, et al. (2011) An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat Struct Mol Biol 18: 822-830. doi: 810.1038/nsmb.2053.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 822-830
    • Guo, W.1    Chen, Y.2    Zhou, X.3    Kar, A.4    Ray, P.5
  • 12
    • 0037108967 scopus 로고    scopus 로고
    • Higher order arrangement of the eukaryotic nuclear bodies
    • Epub 12002 Oct 13582
    • Wang IF, Reddy NM, Shen CK (2002) Higher order arrangement of the eukaryotic nuclear bodies. Proc Natl Acad Sci U S A 99: 13583-13588. Epub 12002 Oct 13582.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 13583-13588
    • Wang, I.F.1    Reddy, N.M.2    Shen, C.K.3
  • 14
    • 77950360176 scopus 로고    scopus 로고
    • Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo
    • Epub 2009 Dec 2003
    • Kabashi E, Lin L, Tradewell ML, Dion PA, Bercier V, et al. (2010) Gain and loss of function of ALS-related mutations of TARDBP (TDP-43) cause motor deficits in vivo. Hum Mol Genet 19: 671-683. Epub 2009 Dec 2003.
    • (2010) Hum Mol Genet , vol.19 , pp. 671-683
    • Kabashi, E.1    Lin, L.2    Tradewell, M.L.3    Dion, P.A.4    Bercier, V.5
  • 15
    • 84865028374 scopus 로고    scopus 로고
    • Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice
    • doi:27310.21074/jbc.M27112.359000. Epub 352012 Jun 359020
    • Wu LS, Cheng WC, Shen CK (2012) Targeted depletion of TDP-43 expression in the spinal cord motor neurons leads to the development of amyotrophic lateral sclerosis-like phenotypes in mice. J Biol Chem 287: 27335-27344. doi:27310.21074/jbc.M27112.359000. Epub 352012 Jun 359020.
    • (2012) J Biol Chem , vol.287 , pp. 27335-27344
    • Wu, L.S.1    Cheng, W.C.2    Shen, C.K.3
  • 16
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T, Kametani F, Yoshida M, et al. (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64: 60-70.
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3    Kametani, F.4    Yoshida, M.5
  • 17
    • 84870188303 scopus 로고    scopus 로고
    • Molecular analysis and biochemical classification of TDP-43 proteinopathy
    • doi: 3310.1093/brain/aws3230. Epub 2012 Oct 3383
    • Tsuji H, Arai T, Kametani F, Nonaka T, Yamashita M, et al. (2012) Molecular analysis and biochemical classification of TDP-43 proteinopathy. Brain 135: 3380-3391. doi: 3310.1093/brain/aws3230. Epub 2012 Oct 3383.
    • (2012) Brain , vol.135 , pp. 3380-3391
    • Tsuji, H.1    Arai, T.2    Kametani, F.3    Nonaka, T.4    Yamashita, M.5
  • 18
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Epub 2006 Oct 2030
    • Arai T, Hasegawa M, Akiyama H, Ikeda K, Nonaka T, et al. (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351: 602-611. Epub 2006 Oct 2030.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3    Ikeda, K.4    Nonaka, T.5
  • 19
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • Epub 2009 Mar 1207
    • Geser F, Martinez-Lage M, Kwong LK, Lee VM, Trojanowski JQ (2009) Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases. J Neurol 256: 1205-1214. Epub 2009 Mar 1207.
    • (2009) J Neurol , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 21
    • 57049178339 scopus 로고    scopus 로고
    • Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy
    • Epub 2008 Oct 1631
    • Thorpe JR, Tang H, Atherton J, Cairns NJ (2008) Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy. J Neural Transm 115: 1661-1671. Epub 2008 Oct 1631.
    • (2008) J Neural Transm , vol.115 , pp. 1661-1671
    • Thorpe, J.R.1    Tang, H.2    Atherton, J.3    Cairns, N.J.4
  • 22
    • 47949093588 scopus 로고    scopus 로고
    • Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases
    • Epub 2008 Jul 2008
    • Lin WL, Dickson DW (2008) Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases. Acta Neuropathol 116: 205-213. Epub 2008 Jul 2008.
    • (2008) Acta Neuropathol , vol.116 , pp. 205-213
    • Lin, W.L.1    Dickson, D.W.2
  • 23
    • 84857918252 scopus 로고    scopus 로고
    • Microglial activation and TDP-43 pathology correlate with executive dysfunction in amyotrophic lateral sclerosis
    • Epub 2012 Jan 2011
    • Brettschneider J, Libon DJ, Toledo JB, Xie SX, McCluskey L, et al. (2012) Microglial activation and TDP-43 pathology correlate with executive dysfunction in amyotrophic lateral sclerosis. Acta Neuropathol 123: 395-407. Epub 2012 Jan 2011.
    • (2012) Acta Neuropathol , vol.123 , pp. 395-407
    • Brettschneider, J.1    Libon, D.J.2    Toledo, J.B.3    Xie, S.X.4    McCluskey, L.5
  • 24
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, et al. (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. The Journal of biological chemistry 284: 20329-20339.
    • (2009) The Journal of Biological Chemistry , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5
  • 25
    • 79956311051 scopus 로고    scopus 로고
    • A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions
    • Epub 12011 Mar 18624
    • Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N (2011) A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. J Biol Chem 286: 18664-18672.Epub 12011 Mar 18624.
    • (2011) J Biol Chem , vol.286 , pp. 18664-18672
    • Furukawa, Y.1    Kaneko, K.2    Watanabe, S.3    Yamanaka, K.4    Nukina, N.5
  • 26
    • 79956304001 scopus 로고    scopus 로고
    • A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport
    • Pesiridis GS, Tripathy K, Tanik S, Trojanowski JQ, Lee VM (2011) A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport. The Journal of biological chemistry 286: 18845-18855.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 18845-18855
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 27
    • 84885484356 scopus 로고    scopus 로고
    • Prion-like properties of pathological TDP-43 aggregates from diseased brains
    • Nonaka T, Masuda-Suzukake M, Arai T, Hasegawa Y, Akatsu H, et al. (2013) Prion-like properties of pathological TDP-43 aggregates from diseased brains. Cell reports 4: 124-134.
    • (2013) Cell Reports , vol.4 , pp. 124-134
    • Nonaka, T.1    Masuda-Suzukake, M.2    Arai, T.3    Hasegawa, Y.4    Akatsu, H.5
  • 28
    • 84897070051 scopus 로고    scopus 로고
    • TDP-43 Phosphorylation by casein kinase I{varepsilon} promotes oligomerization and enhances toxicity in vivo
    • Choksi DK, Roy B, Chatterjee S, Yusuff T, Bakhoum MF, et al. (2013) TDP-43 Phosphorylation by casein kinase I{varepsilon} promotes oligomerization and enhances toxicity in vivo. Human molecular genetics.
    • (2013) Human Molecular Genetics
    • Choksi, D.K.1    Roy, B.2    Chatterjee, S.3    Yusuff, T.4    Bakhoum, M.F.5
  • 29
    • 58149498300 scopus 로고    scopus 로고
    • Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells
    • Epub 2008 Dec 2025
    • Nonaka T, Arai T, Buratti E, Baralle FE, Akiyama H, et al. (2009) Phosphorylated and ubiquitinated TDP-43 pathological inclusions in ALS and FTLD-U are recapitulated in SH-SY5Y cells. FEBS Lett 583: 394-400. Epub 2008 Dec 2025.
    • (2009) FEBS Lett , vol.583 , pp. 394-400
    • Nonaka, T.1    Arai, T.2    Buratti, E.3    Baralle, F.E.4    Akiyama, H.5
  • 30
    • 78649750391 scopus 로고    scopus 로고
    • Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy
    • Liachko NF, Guthrie CR, Kraemer BC (2010) Phosphorylation promotes neurotoxicity in a Caenorhabditis elegans model of TDP-43 proteinopathy. J Neurosci 30: 16208-16219.
    • (2010) J Neurosci , vol.30 , pp. 16208-16219
    • Liachko, N.F.1    Guthrie, C.R.2    Kraemer, B.C.3
  • 31
    • 85040709233 scopus 로고    scopus 로고
    • Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments
    • Zhang YJ, Gendron TF, Xu YF, Ko LW, Yen SH, et al. (2010) Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments. Mol Neurodegener 5: 33.
    • (2010) Mol Neurodegener , vol.5 , pp. 33
    • Zhang, Y.J.1    Gendron, T.F.2    Xu, Y.F.3    Ko, L.W.4    Yen, S.H.5
  • 32
    • 57049139853 scopus 로고    scopus 로고
    • Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone
    • Sarkar M, Kuret J, Lee G (2008) Two motifs within the tau microtubule-binding domain mediate its association with the hsc70 molecular chaperone. J Neurosci Res 86: 2763-2773.
    • (2008) J Neurosci Res , vol.86 , pp. 2763-2773
    • Sarkar, M.1    Kuret, J.2    Lee, G.3
  • 33
    • 77952779305 scopus 로고    scopus 로고
    • Hsc70 rapidly engages tau after microtubule destabilization
    • Epub 12010 Mar 16722
    • Jinwal UK, O'Leary JC 3rd, Borysov SI, Jones JR, Li Q, et al. (2010) Hsc70 rapidly engages tau after microtubule destabilization. J Biol Chem 285: 16798-16805. Epub 12010 Mar 16722.
    • (2010) J Biol Chem , vol.285 , pp. 16798-16805
    • Jinwal, U.K.1    O'Leary III, J.C.2    Borysov, S.I.3    Jones, J.R.4    Li, Q.5
  • 34
    • 33847369469 scopus 로고    scopus 로고
    • The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins
    • PMCID: PMC1794119
    • Dickey CA, Kamal A, Lundgren K, Klosak N, Bailey RM, et al. (2007) The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. J Clin Invest 117: 648-658. PMCID: PMC1794119.
    • (2007) J Clin Invest , vol.117 , pp. 648-658
    • Dickey, C.A.1    Kamal, A.2    Lundgren, K.3    Klosak, N.4    Bailey, R.M.5
  • 35
    • 58249116541 scopus 로고    scopus 로고
    • Aging analysis reveals slowed tau turnover and enhanced stress response in a mouse model of tauopathy
    • Epub 2008 Dec 2012
    • Dickey C, Kraft C, Jinwal U, Koren J, Johnson A, et al. (2009) Aging analysis reveals slowed tau turnover and enhanced stress response in a mouse model of tauopathy. Am J Pathol 174: 228-238.Epub 2008 Dec 2012.
    • (2009) Am J Pathol , vol.174 , pp. 228-238
    • Dickey, C.1    Kraft, C.2    Jinwal, U.3    Koren, J.4    Johnson, A.5
  • 36
    • 84863792269 scopus 로고    scopus 로고
    • Cdc37/Hsp90 protein complex disruption triggers an autophagic clearance cascade for TDP-43 protein
    • Epub 22012 Jun 24816
    • Jinwal UK, Abisambra JF, Zhang J, Dharia S, O'Leary JC, et al. (2012) Cdc37/Hsp90 protein complex disruption triggers an autophagic clearance cascade for TDP-43 protein. J Biol Chem 287: 24814-24820. Epub 22012 Jun 24816.
    • (2012) J Biol Chem , vol.287 , pp. 24814-24820
    • Jinwal, U.K.1    Abisambra, J.F.2    Zhang, J.3    Dharia, S.4    O'Leary, J.C.5
  • 37
    • 76149120427 scopus 로고    scopus 로고
    • Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery
    • Freibaum BD, Chitta RK, High AA, Taylor JP (2010) Global analysis of TDP-43 interacting proteins reveals strong association with RNA splicing and translation machinery. Journal of proteome research 9: 1104-1120.
    • (2010) Journal of Proteome Research , vol.9 , pp. 1104-1120
    • Freibaum, B.D.1    Chitta, R.K.2    High, A.A.3    Taylor, J.P.4
  • 38
    • 33846212717 scopus 로고    scopus 로고
    • Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration
    • DOI 10.1111/j.1460-9568.2006.05226.x
    • Wang JZ, Grundke-Iqbal I, Iqbal K (2007) Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration. Eur J Neurosci 25: 59-68. (Pubitemid 46098893)
    • (2007) European Journal of Neuroscience , vol.25 , Issue.1 , pp. 59-68
    • Wang, J.-Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 40
    • 81855190900 scopus 로고    scopus 로고
    • Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport
    • Epub 12011 Nov 10308
    • Patterson KR, Ward SM, Combs B, Voss K, Kanaan NM, et al. (2011) Heat shock protein 70 prevents both tau aggregation and the inhibitory effects of preexisting tau aggregates on fast axonal transport. Biochemistry 50: 10300-10310. Epub 12011 Nov 10308.
    • (2011) Biochemistry , vol.50 , pp. 10300-10310
    • Patterson, K.R.1    Ward, S.M.2    Combs, B.3    Voss, K.4    Kanaan, N.M.5
  • 41
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT Jr (2002) Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 418: 291. (Pubitemid 34790672)
    • (2002) Nature , vol.418 , Issue.6895 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 42
    • 77957006608 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone and ALS-linked mutations accelerate aggregation and increase toxicity
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, et al. (2009) TDP-43 is intrinsically aggregation-prone and ALS-linked mutations accelerate aggregation and increase toxicity. The Journal of biological chemistry 22: 22.
    • (2009) The Journal of Biological Chemistry , vol.22 , pp. 22
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5
  • 43
    • 80155166000 scopus 로고    scopus 로고
    • Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms
    • doi: 9410.1021/bi2010569. Epub 2012011 Oct 2010517
    • Combs B, Voss K, Gamblin TC (2011) Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms. Biochemistry 50: 9446-9456. doi: 9410.1021/bi2010569. Epub 2012011 Oct 2010517.
    • (2011) Biochemistry , vol.50 , pp. 9446-9456
    • Combs, B.1    Voss, K.2    Gamblin, T.C.3
  • 44
    • 0037457966 scopus 로고    scopus 로고
    • Chaperones increase association of tau protein with microtubules
    • Epub 2003 Jan 2009
    • Dou F, Netzer WJ, Tanemura K, Li F, Hartl FU, et al. (2003) Chaperones increase association of tau protein with microtubules. Proc Natl Acad Sci U S A 100: 721-726. Epub 2003 Jan 2009.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 721-726
    • Dou, F.1    Netzer, W.J.2    Tanemura, K.3    Li, F.4    Hartl, F.U.5
  • 46
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
    • Miyata Y, Yahara I (1992) The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. The Journal of biological chemistry 267: 7042-7047.
    • (1992) The Journal of Biological Chemistry , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 48
    • 0025044588 scopus 로고
    • Aberrant casein kinase II in Alzheimer's disease
    • DOI 10.1016/0006-8993(90)90282-G
    • Iimoto DS, Masliah E, DeTeresa R, Terry RD, Saitoh T (1990) Aberrant casein kinase II in Alzheimer's disease. Brain research 507: 273-280. (Pubitemid 20054109)
    • (1990) Brain Research , vol.507 , Issue.2 , pp. 273-280
    • Iimoto, D.S.1    Masliah, E.2    DeTeresa, R.3    Terry, R.D.4    Saitoh, T.5
  • 50
    • 79961148135 scopus 로고    scopus 로고
    • Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation
    • Li HY, Yeh PA, Chiu HC, Tang CY, Tu BP (2011) Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation. PloS one 6: e23075.
    • (2011) PloS One , vol.6
    • Li, H.Y.1    Yeh, P.A.2    Chiu, H.C.3    Tang, C.Y.4    Tu, B.P.5
  • 51
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady OA, Meng P, Zheng Y, Mao Y, Hu F (2011) Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. Journal of neurochemistry 116: 248-259.
    • (2011) Journal of Neurochemistry , vol.116 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 52
    • 80052023055 scopus 로고    scopus 로고
    • Apigenin inhibits proliferation and induces apoptosis in human multiple myeloma cells through targeting the trinity of CK2, Cdc37 and Hsp90
    • Zhao M, Ma J, Zhu HY, Zhang XH, Du ZY, et al. (2011) Apigenin inhibits proliferation and induces apoptosis in human multiple myeloma cells through targeting the trinity of CK2, Cdc37 and Hsp90. Molecular cancer 10: 104.
    • (2011) Molecular Cancer , vol.10 , pp. 104
    • Zhao, M.1    Ma, J.2    Zhu, H.Y.3    Zhang, X.H.4    Du, Z.Y.5
  • 54
    • 67749133873 scopus 로고    scopus 로고
    • TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity
    • Epub 22009 May 20322
    • Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, et al. (2009) TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity. J Biol Chem 284: 20329-20339. Epub 22009 May 20322.
    • (2009) J Biol Chem , vol.284 , pp. 20329-20339
    • Johnson, B.S.1    Snead, D.2    Lee, J.J.3    McCaffery, J.M.4    Shorter, J.5
  • 55
    • 0037064023 scopus 로고    scopus 로고
    • The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
    • Epub 32002 Aug 38292
    • Hernandez MP, Sullivan WP, Toft DO (2002) The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex. J Biol Chem 277: 38294-38304. Epub 32002 Aug 38292.
    • (2002) J Biol Chem , vol.277 , pp. 38294-38304
    • Hernandez, M.P.1    Sullivan, W.P.2    Toft, D.O.3
  • 56
    • 47949093588 scopus 로고    scopus 로고
    • Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases
    • Lin WL, Dickson DW (2008) Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases. Acta neuropathologica 116: 205-213.
    • (2008) Acta Neuropathologica , vol.116 , pp. 205-213
    • Lin, W.L.1    Dickson, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.