메뉴 건너뛰기




Volumn 181, Issue 1, 2013, Pages 11-16

Characterization of β-domains in C-terminal fragments of TDP-43 by scanning tunneling microscopy

Author keywords

Domain; Amyloid; Fibril formation; STM; TAR DNA binding protein 43

Indexed keywords

MUTANT PROTEIN; TAR DNA BINDING PROTEIN;

EID: 84870916853     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.10.011     Document Type: Article
Times cited : (26)

References (27)
  • 2
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 Is toxic to neurons & enhanced by a mutation associated with familial ALS
    • Barmada S.J., Skibinski G., Korb E., Rao E.J., Wu J.Y., Finkbeiner S. Cytoplasmic mislocalization of TDP-43 Is toxic to neurons & enhanced by a mutation associated with familial ALS. J. Neurosci. 2010, 30:639-649.
    • (2010) J. Neurosci. , vol.30 , pp. 639-649
    • Barmada, S.J.1    Skibinski, G.2    Korb, E.3    Rao, E.J.4    Wu, J.Y.5    Finkbeiner, S.6
  • 4
    • 80755153025 scopus 로고    scopus 로고
    • TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
    • Cohen T.J., Lee V.M., Trojanowski J.Q. TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies. Trends Mol. Med. 2011, 17:659-667.
    • (2011) Trends Mol. Med. , vol.17 , pp. 659-667
    • Cohen, T.J.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 5
    • 79960040173 scopus 로고    scopus 로고
    • An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity
    • Guo W.R., Chen Y.B., Zhou X.H., Kar A., Ray P., Chen X.P., et al. An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity. Nat. Struct. Mol. Biol. 2011, 18:822-830.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 822-830
    • Guo, W.R.1    Chen, Y.B.2    Zhou, X.H.3    Kar, A.4    Ray, P.5    Chen, X.P.6
  • 6
    • 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., Hashizume Y., et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann. Neurol. 2008, 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    Hashizume, Y.6
  • 7
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson E.G., Thornton J.M. A revised set of potentials for beta-turn formation in proteins. Protein Sci. 1994, 3:2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 8
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • gaz L.M., Kwong L.K., Xu Y., Truax A.C., Uryu K., Neumann M., et al. Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am. J. Pathol. 2008, 173:182-194.
    • (2008) Am. J. Pathol. , vol.173 , pp. 182-194
    • gaz, L.M.1    Kwong, L.K.2    Xu, Y.3    Truax, A.C.4    Uryu, K.5    Neumann, M.6
  • 9
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies
    • Igaz L.M., Kwong L.K., Chen-Plotkin A., Winton M.J., Unger T.L., Xu Y., et al. Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J. Biol. Chem. 2009, 284:8516-8524.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8516-8524
    • Igaz, L.M.1    Kwong, L.K.2    Chen-Plotkin, A.3    Winton, M.J.4    Unger, T.L.5    Xu, Y.6
  • 10
    • 70349308579 scopus 로고    scopus 로고
    • Regional distribution of TDP-43 inclusions in Alzheimer's disease (AD) brains: their relation to AD common pathology
    • Kadokura A., Yamazaki T., Lemere C.A., Takatama M., Okamoto K. Regional distribution of TDP-43 inclusions in Alzheimer's disease (AD) brains: their relation to AD common pathology. Neuropathology 2009, 29:566-573.
    • (2009) Neuropathology , vol.29 , pp. 566-573
    • Kadokura, A.1    Yamazaki, T.2    Lemere, C.A.3    Takatama, M.4    Okamoto, K.5
  • 11
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo P.H., Doudeva L.G., Wang Y.T., Shen C.K.J., Yuan H.S. Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res. 2009, 37:1799-1808.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.J.4    Yuan, H.S.5
  • 12
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C., Polymenidou M., Cleveland D.W. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum. Mol. Genet. 2010, 19(R1):R46-R64.
    • (2010) Hum. Mol. Genet. , vol.19 , Issue.R1
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 13
    • 71949110860 scopus 로고    scopus 로고
    • Chaperon-mediated single molecular approach toward modulating Aβ peptide aggregation
    • Liu L., Zhang L., Mao X.B., Niu L., Yang Y.L., Wang C. Chaperon-mediated single molecular approach toward modulating Aβ peptide aggregation. Nano Lett. 2009, 9:4066-4072.
    • (2009) Nano Lett. , vol.9 , pp. 4066-4072
    • Liu, L.1    Zhang, L.2    Mao, X.B.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 14
    • 79961063205 scopus 로고    scopus 로고
    • Observation of reduced cytotoxicity of aggregated amyloidogenic peptides with chaperone-like molecules
    • Liu L., Zhang L., Niu L., Xu M., Mao X.B., Yang Y.L., et al. Observation of reduced cytotoxicity of aggregated amyloidogenic peptides with chaperone-like molecules. ACS Nano 2011, 5:6001-6007.
    • (2011) ACS Nano , vol.5 , pp. 6001-6007
    • Liu, L.1    Zhang, L.2    Niu, L.3    Xu, M.4    Mao, X.B.5    Yang, Y.L.6
  • 15
    • 67349128044 scopus 로고    scopus 로고
    • Amyloid-β (1-42) folding multiplicity and single molecule binding behavior studied by STM
    • Ma X.J., Liu L., Mao X.B., Niu L., Deng K., Wu W.H., et al. Amyloid-β (1-42) folding multiplicity and single molecule binding behavior studied by STM. J. Mol. Biol. 2009, 388:894-901.
    • (2009) J. Mol. Biol. , vol.388 , pp. 894-901
    • Ma, X.J.1    Liu, L.2    Mao, X.B.3    Niu, L.4    Deng, K.5    Wu, W.H.6
  • 16
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update
    • Mackenzie I.R.A., Neumann M., Bigio E.H., Cairns N.J., Alafuzoff I., Kril J., et al. Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update. Acta Neuropathol. 2010, 119:1-4.
    • (2010) Acta Neuropathol. , vol.119 , pp. 1-4
    • Mackenzie, I.R.A.1    Neumann, M.2    Bigio, E.H.3    Cairns, N.J.4    Alafuzoff, I.5    Kril, J.6
  • 17
    • 67650756419 scopus 로고    scopus 로고
    • Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy
    • Mao X.B., Ma X.J., Liu L., Niu L., Yang Y.L., Wang C. Structural characteristics of the beta-sheet-like human and rat islet amyloid polypeptides as determined by scanning tunneling microscopy. J. Struct. Biol. 2009, 167:209-215.
    • (2009) J. Struct. Biol. , vol.167 , pp. 209-215
    • Mao, X.B.1    Ma, X.J.2    Liu, L.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 18
    • 83755178092 scopus 로고    scopus 로고
    • Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies
    • Mao X.B., Wang C.X., Wu X.K., Ma X.J., Liu L., Zhang L., et al. Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies. Proc. Natl. Acad. Sci. USA 2011, 108:19605-19610.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 19605-19610
    • Mao, X.B.1    Wang, C.X.2    Wu, X.K.3    Ma, X.J.4    Liu, L.5    Zhang, L.6
  • 19
    • 79959249196 scopus 로고    scopus 로고
    • Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy
    • Mao X.B., Guo Y.Y., Wang C.X., Zhang M., Ma X.J., Liu L., et al. Binding modes of thioflavin t molecules to prion peptide assemblies identified by using scanning tunneling microscopy. ACS Chem. Neurosci. 2011, 2:281-287.
    • (2011) ACS Chem. Neurosci. , vol.2 , pp. 281-287
    • Mao, X.B.1    Guo, Y.Y.2    Wang, C.X.3    Zhang, M.4    Ma, X.J.5    Liu, L.6
  • 20
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M., Sampathu D.M., Kwong L.K., Truax A.C., Micsenyi M.C., Chou T.T., et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006, 314:130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 21
    • 0037251889 scopus 로고    scopus 로고
    • Neuropathology with clinical correlations of sporadic amyotrophic lateral sclerosis: 102 autopsy cases examined between 1962 and 2000
    • Piao Y.S., Wakabayashi K., Kakita A., Yamada M., Hayashi S., Morita T., et al. Neuropathology with clinical correlations of sporadic amyotrophic lateral sclerosis: 102 autopsy cases examined between 1962 and 2000. Brain Pathol. 2003, 13:10-22.
    • (2003) Brain Pathol. , vol.13 , pp. 10-22
    • Piao, Y.S.1    Wakabayashi, K.2    Kakita, A.3    Yamada, M.4    Hayashi, S.5    Morita, T.6
  • 23
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J., Blair I.P., Tripathi V.B., Hu X., Vance C., Rogelj B., et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008, 319:1668-1672.
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3    Hu, X.4    Vance, C.5    Rogelj, B.6
  • 24
    • 42449163952 scopus 로고    scopus 로고
    • TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor
    • Wang I.F., Wu L.S., Chang H.Y., Shen C.K.J. TDP-43, the signature protein of FTLD-U, is a neuronal activity-responsive factor. J. Neurochem. 2008, 105:797-806.
    • (2008) J. Neurochem. , vol.105 , pp. 797-806
    • Wang, I.F.1    Wu, L.S.2    Chang, H.Y.3    Shen, C.K.J.4
  • 25
    • 80052920642 scopus 로고    scopus 로고
    • Determination of relative binding affinities of labeling molecules with amino acids by using scanning tunneling microscopy
    • Wang C.X., Mao X.B., Yang A.H., Niu L., Wang S.N., Li D.H., et al. Determination of relative binding affinities of labeling molecules with amino acids by using scanning tunneling microscopy. Chem. Commun. 2011, 47:10638-10640.
    • (2011) Chem. Commun. , vol.47 , pp. 10638-10640
    • Wang, C.X.1    Mao, X.B.2    Yang, A.H.3    Niu, L.4    Wang, S.N.5    Li, D.H.6
  • 26
    • 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., Baloh R.H. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl. Acad. Sci. USA 2009, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.