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Volumn 116, Issue 2, 2011, Pages 248-259

Regulation of TDP-43 aggregation by phosphorylation andp62/SQSTM1

Author keywords

aggregation; autophagy; p62 SQSTM1; phosphorylation; proteasome; TDP 43

Indexed keywords

ASPARTIC ACID; PROTEASOME; PROTEIN P62; SERINE; TAR DNA BINDING PROTEIN;

EID: 78650680776     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.07098.x     Document Type: Article
Times cited : (170)

References (57)
  • 3
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T., Hasegawa M., Akiyama H., 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.
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 4
    • 21344463770 scopus 로고    scopus 로고
    • Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation
    • Babu J. R., Geetha T., and, Wooten M. W., (2005) Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J. Neurochem. 94, 192-203.
    • (2005) J. Neurochem. , vol.94 , pp. 192-203
    • Babu, J.R.1    Geetha, T.2    Wooten, M.W.3
  • 5
    • 77952766891 scopus 로고    scopus 로고
    • Autophagy: Assays and artifacts
    • Barth S., Glick D., and, Macleod K. F., (2010) Autophagy: assays and artifacts. J. Pathol. 221, 117-124.
    • (2010) J. Pathol. , vol.221 , pp. 117-124
    • Barth, S.1    Glick, D.2    MacLeod, K.F.3
  • 6
    • 77955897545 scopus 로고    scopus 로고
    • Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations
    • Baumer D., Hilton D., Paine S. M., Turner M. R., Lowe J., Talbot K., and, Ansorge O., (2010) Juvenile ALS with basophilic inclusions is a FUS proteinopathy with FUS mutations. Neurology 75, 611-618.
    • (2010) Neurology , vol.75 , pp. 611-618
    • Baumer, D.1    Hilton, D.2    Paine, S.M.3    Turner, M.R.4    Lowe, J.5    Talbot, K.6    Ansorge, O.7
  • 7
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti E., and, Baralle F. E., (2008) Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci. 13, 867-878.
    • (2008) Front Biosci. , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 8
    • 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
    • Buratti E., Brindisi A., Giombi M., Tisminetzky S., Ayala Y. M., and, Baralle F. E., (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.
    • (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    Baralle, F.E.6
  • 9
    • 79954427132 scopus 로고    scopus 로고
    • New neuropathological findings in Unverricht-Lundborg disease: Neuronal intranuclear and cytoplasmic inclusions
    • in press.
    • Cohen N. R., Hammans S. R., Macpherson J., and, Nicoll J. A., (2010) New neuropathological findings in Unverricht-Lundborg disease: neuronal intranuclear and cytoplasmic inclusions. Acta Neuropathol. in press.
    • (2010) Acta Neuropathol.
    • Cohen, N.R.1    Hammans, S.R.2    MacPherson, J.3    Nicoll, J.A.4
  • 10
    • 77952932485 scopus 로고    scopus 로고
    • FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis
    • Deng H. X., Zhai H., Bigio E. H., et al. (2010) FUS-immunoreactive inclusions are a common feature in sporadic and non-SOD1 familial amyotrophic lateral sclerosis. Ann. Neurol. 67, 739-748.
    • (2010) Ann. Neurol. , vol.67 , pp. 739-748
    • Deng, H.X.1    Zhai, H.2    Bigio, E.H.3
  • 11
    • 67650432367 scopus 로고    scopus 로고
    • Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin
    • Dormann D., Capell A., Carlson A. M., et al. (2009) Proteolytic processing of TAR DNA binding protein-43 by caspases produces C-terminal fragments with disease defining properties independent of progranulin. J. Neurochem. 110, 1082-1094.
    • (2009) J. Neurochem. , vol.110 , pp. 1082-1094
    • Dormann, D.1    Capell, A.2    Carlson, A.M.3
  • 12
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi Z., Csizmok V., Tompa P., and, Simon I., (2005) The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J. Mol. Biol. 347, 827-839.
    • (2005) J. Mol. Biol. , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 15
    • 78650707221 scopus 로고    scopus 로고
    • Numerous FUS-positive inclusions in an elderly woman with motor neuron disease
    • [Epub ahead of print].
    • Fujita Y., Fujita S., Takatama M., Ikeda M., and, Okamoto K., (2010) Numerous FUS-positive inclusions in an elderly woman with motor neuron disease. Neuropathology [Epub ahead of print].
    • (2010) Neuropathology
    • Fujita, Y.1    Fujita, S.2    Takatama, M.3    Ikeda, M.4    Okamoto, K.5
  • 16
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal J., Strom A. L., Kwinter D. M., Kilty R., Zhang J., Shi P., Fu W., Wooten M. W., and, Zhu H., (2009) Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J. Neurochem. 111, 1062-1073.
    • (2009) J. Neurochem. , vol.111 , pp. 1062-1073
    • Gal, J.1    Strom, A.L.2    Kwinter, D.M.3    Kilty, R.4    Zhang, J.5    Shi, P.6    Fu, W.7    Wooten, M.W.8    Zhu, H.9
  • 18
    • 51049118332 scopus 로고    scopus 로고
    • The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: Beyond the usual suspects' review series
    • Geng J., and, Klionsky D. J., (2008) The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep. 9, 859-864.
    • (2008) EMBO Rep. , vol.9 , pp. 859-864
    • Geng, J.1    Klionsky, D.J.2
  • 19
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T., Nakamura K., Matsui M., et al. (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441, 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 20
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M., Arai T., Nonaka T., 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
  • 21
    • 36348972414 scopus 로고    scopus 로고
    • Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
    • Higashi S., Iseki E., Yamamoto R., et al. (2007) Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies. Brain Res. 1184, 284-294.
    • (2007) Brain Res. , vol.1184 , pp. 284-294
    • Higashi, S.1    Iseki, E.2    Yamamoto, R.3
  • 23
    • 48749088629 scopus 로고    scopus 로고
    • Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
    • Inukai Y., Nonaka T., Arai T., et al. (2008) Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett. 582, 2899-2904.
    • (2008) FEBS Lett. , vol.582 , pp. 2899-2904
    • Inukai, Y.1    Nonaka, T.2    Arai, T.3
  • 24
    • 40449127705 scopus 로고    scopus 로고
    • Neuropathological aspects of Alzheimer disease, Parkinson disease and frontotemporal dementia
    • Jellinger K. A., (2008) Neuropathological aspects of Alzheimer disease, Parkinson disease and frontotemporal dementia. Neurodegener. Dis. 5, 118-121.
    • (2008) Neurodegener. Dis. , vol.5 , pp. 118-121
    • Jellinger, K.A.1
  • 26
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E., Valdmanis P. N., Dion P., et al. (2008) TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat. Genet. 40, 572-574.
    • (2008) Nat. Genet. , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3
  • 27
    • 68149159190 scopus 로고    scopus 로고
    • Phosphorylation-dependent TDP-43 antibody detects intraneuronal dot-like structures showing morphological characters of granulovacuolar degeneration
    • Kadokura A., Yamazaki T., Kakuda S., Makioka K., Lemere C. A., Fujita Y., Takatama M., and, Okamoto K., (2009) Phosphorylation-dependent TDP-43 antibody detects intraneuronal dot-like structures showing morphological characters of granulovacuolar degeneration. Neurosci. Lett. 463, 87-92.
    • (2009) Neurosci. Lett. , vol.463 , pp. 87-92
    • Kadokura, A.1    Yamazaki, T.2    Kakuda, S.3    Makioka, K.4    Lemere, C.A.5    Fujita, Y.6    Takatama, M.7    Okamoto, K.8
  • 29
    • 77958604956 scopus 로고    scopus 로고
    • ALS-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to coregulate HDAC6 mRNA
    • Kim S. H., Shanware N., Bowler M. J., and, Tibbetts R. S., (2010) ALS-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to coregulate HDAC6 mRNA. J. Biol. Chem. 285, 34097-34105.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 30
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski T. J., Jr, Bosco D. A., Leclerc A. L., et al. (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323, 1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski, Jr.T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 32
    • 34547733547 scopus 로고    scopus 로고
    • Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases
    • Nakashima-Yasuda H., Uryu K., Robinson J., et al. (2007) Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases. Acta Neuropathol. 114, 221-229.
    • (2007) Acta Neuropathol. , vol.114 , pp. 221-229
    • Nakashima-Yasuda, H.1    Uryu, K.2    Robinson, J.3
  • 33
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M., Sampathu D. M., Kwong L. K., et al. (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314, 130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 34
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann M., Kwong L. K., Lee E. B., et al. (2009) Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol. 117, 137-149.
    • (2009) Acta Neuropathol. , vol.117 , pp. 137-149
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3
  • 35
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • Nonaka T., Kametani F., Arai T., Akiyama H., and, Hasegawa M., (2009) Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum. Mol. Genet. 18, 3353-3364.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 37
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C. A., and, Poirier M. A., (2004) Protein aggregation and neurodegenerative disease. Nat. Med. 10 (Suppl.), S10-S17.
    • (2004) Nat. Med. , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 38
    • 52949094629 scopus 로고    scopus 로고
    • Novel mutations in TARDBP (TDP-43) in patients with familial amyotrophic lateral sclerosis
    • Rutherford N. J., Zhang Y. J., Baker M., 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
  • 39
    • 58149398638 scopus 로고    scopus 로고
    • Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of huntington disease
    • Schwab C., Arai T., Hasegawa M., Yu S., and, McGeer P. L., (2008) Colocalization of transactivation-responsive DNA-binding protein 43 and huntingtin in inclusions of huntington disease. J. Neuropathol. Exp. Neurol. 67, 1159-1165.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 1159-1165
    • Schwab, C.1    Arai, T.2    Hasegawa, M.3    Yu, S.4    McGeer, P.L.5
  • 40
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener M. L., Babu J. R., Geetha T., Wong H. C., Krishna N. R., and, Wooten M. W., (2004) Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol. Cell. Biol. 24, 8055-8068.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 41
    • 33846240526 scopus 로고    scopus 로고
    • Sequestosome 1/p62 - More than just a scaffold
    • Seibenhener M. L., Geetha T., and, Wooten M. W., (2007) Sequestosome 1/p62-more than just a scaffold. FEBS Lett. 581, 175-179.
    • (2007) FEBS Lett. , vol.581 , pp. 175-179
    • Seibenhener, M.L.1    Geetha, T.2    Wooten, M.W.3
  • 42
    • 77958022745 scopus 로고    scopus 로고
    • Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice
    • Shan X., Chiang P. M., Price D. L., and, Wong P. C., (2010) Altered distributions of Gemini of coiled bodies and mitochondria in motor neurons of TDP-43 transgenic mice. Proc. Natl Acad. Sci. USA 107, 16325-16330.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16325-16330
    • Shan, X.1    Chiang, P.M.2    Price, D.L.3    Wong, P.C.4
  • 43
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J., Blair I. P., Tripathi V. B., et al. (2008) TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 319, 1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3
  • 44
    • 68949221689 scopus 로고    scopus 로고
    • Ubiquitin-like and ubiquitin-associated domain proteins: Significance in proteasomal degradation
    • Su V., and, Lau A. F., (2009) Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation. Cell. Mol. Life Sci. 66, 2819-2833.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2819-2833
    • Su, V.1    Lau, A.F.2
  • 45
    • 44649137415 scopus 로고    scopus 로고
    • Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies
    • Uryu K., Nakashima-Yasuda H., Forman M. S., et al. (2008) Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies. J. Neuropathol. Exp. Neurol. 67, 555-564.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 555-564
    • Uryu, K.1    Nakashima-Yasuda, H.2    Forman, M.S.3
  • 46
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C., Rogelj B., Hortobagyi T., et al. (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323, 1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3
  • 48
    • 54249100481 scopus 로고    scopus 로고
    • TDP-43: An emerging new player in neurodegenerative diseases
    • Wang I. F., Wu L. S., and, Shen C. K., (2008) TDP-43: an emerging new player in neurodegenerative diseases. Trends Mol. Med. 14, 479-485.
    • (2008) Trends Mol. Med. , vol.14 , pp. 479-485
    • Wang, I.F.1    Wu, L.S.2    Shen, C.K.3
  • 49
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska I., Bell S., Cairns N. J., Miller T. M., and, Baloh R. H., (2009) TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 106, 18809-18814.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 51
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton M. J., Igaz L. M., Wong M. M., Kwong L. K., Trojanowski J. Q., and, Lee V. M., (2008) Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J. Biol. Chem. 283, 13302-13309.
    • (2008) J. Biol. Chem. , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3    Kwong, L.K.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 52
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang Z., and, Klionsky D. J., (2009) Mammalian autophagy: core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22, 124-131.
    • (2009) Curr. Opin. Cell Biol. , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 53
    • 55849133733 scopus 로고    scopus 로고
    • Identification of SCF ubiquitin ligase substrates by global protein stability profiling
    • Yen H. C., and, Elledge S. J., (2008) Identification of SCF ubiquitin ligase substrates by global protein stability profiling. Science 322, 923-929.
    • (2008) Science , vol.322 , pp. 923-929
    • Yen, H.C.1    Elledge, S.J.2
  • 54
    • 42949094584 scopus 로고    scopus 로고
    • TDP-43 mutation in familial amyotrophic lateral sclerosis
    • Yokoseki A., Shiga A., Tan C. F., et al. (2008) TDP-43 mutation in familial amyotrophic lateral sclerosis. Ann. Neurol. 63, 538-542.
    • (2008) Ann. Neurol. , vol.63 , pp. 538-542
    • Yokoseki, A.1    Shiga, A.2    Tan, C.F.3
  • 56
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • Zhang Y. J., Xu Y. F., Cook C., et al. (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc. Natl Acad. Sci. USA 106, 7607-7612.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 7607-7612
    • Zhang, Y.J.1    Xu, Y.F.2    Cook, C.3
  • 57
    • 85040709233 scopus 로고    scopus 로고
    • Phosphorylation regulates proteasomal-mediated degradation and solubility of TAR DNA binding protein-43 C-terminal fragments
    • Zhang Y. J., Gendron T. F., Xu Y. F., Ko L. W., Yen S. H., and, Petrucelli L., (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    Petrucelli, L.6


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