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Volumn 670, Issue , 2011, Pages 109-123

Split GFP complementation assay for quantitative measurement of tau aggregation in situ

Author keywords

Aggregation; GSK3 ; Split GFP complementation; Tau

Indexed keywords

GREEN FLUORESCENT PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; TAU PROTEIN;

EID: 84934435700     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-60761-744-0_9     Document Type: Article
Times cited : (15)

References (13)
  • 2
    • 10944227282 scopus 로고    scopus 로고
    • Tau phosphorylation: Physiological and pathological consequences
    • Stoothoff, W. H., and Johnson, G. V. (2005) Tau phosphorylation: physiological and pathological consequences. Biochim Biophys Acta 1739, 280-97.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 280-297
    • Stoothoff, W.H.1    Johnson, G.V.2
  • 3
    • 49149126973 scopus 로고    scopus 로고
    • The last tangle of tau
    • Ding, H., and Johnson, G. V. (2008) The last tangle of tau. J Alzheimers Dis 14, 441-7.
    • (2008) J Alzheimers Dis , vol.14 , pp. 441-447
    • Ding, H.1    Johnson, G.V.2
  • 4
    • 0023009658 scopus 로고
    • Microtubule-associated protein tau. A component of Alzheimer paired helical filaments
    • Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., and Wisniewski, H. M. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261, 6084-9.
    • (1986) J Biol Chem , vol.261 , pp. 6084-6089
    • Grundke-Iqbal, I.1    Iqbal, K.2    Quinlan, M.3    Tung, Y.C.4    Zaidi, M.S.5    Wisniewski, H.M.6
  • 5
    • 0009364134 scopus 로고
    • Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease
    • Kosik, K. S., Joachim, C. L., and Selkoe, D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci U S A 83, 4044-8.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4044-4048
    • Kosik, K.S.1    Joachim, C.L.2    Selkoe, D.J.3
  • 6
    • 34248181511 scopus 로고    scopus 로고
    • Reducing endogenous tau ameliorates amyloid betainduced deficits in an Alzheimer's disease mouse model
    • Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G. Q., and Mucke, L. (2007) Reducing endogenous tau ameliorates amyloid betainduced deficits in an Alzheimer's disease mouse model. Science 316, 750-4.
    • (2007) Science , vol.316 , pp. 750-754
    • Roberson, E.D.1    Scearce-Levie, K.2    Palop, J.J.3    Yan, F.4    Cheng, I.H.5    Wu, T.6    Gerstein, H.7    Yu, G.Q.8    Mucke, L.9
  • 8
    • 36448995426 scopus 로고    scopus 로고
    • Split GFP complementation assay: A novel approach to quantitatively measure aggregation of tau in situ: Effects of GSK3beta activation and caspase 3 cleavage
    • Chun, W., Waldo, G. S., and Johnson, G. V. (2007) Split GFP complementation assay: a novel approach to quantitatively measure aggregation of tau in situ: effects of GSK3beta activation and caspase 3 cleavage. J Neurochem 103, 2529-39.
    • (2007) J Neurochem , vol.103 , pp. 2529-2539
    • Chun, W.1    Waldo, G.S.2    Johnson, G.V.3
  • 9
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • Cabantous, S., Terwilliger, T. C., and Waldo, G. S. (2005) Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol 23, 102-7.
    • (2005) Nat Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 10
    • 33644851265 scopus 로고    scopus 로고
    • Inducible expression of Tau repeat domain in cell models of tauopathy: Aggregation is toxic to cells but can be reversed by inhibitor drugs
    • Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen, M., Gazova, Z., Mandelkow, E., and Mandelkow, E. M. (2006) Inducible expression of Tau repeat domain in cell models of tauopathy: aggregation is toxic to cells but can be reversed by inhibitor drugs. J Biol Chem 281, 1205-14.
    • (2006) J Biol Chem , vol.281 , pp. 1205-1214
    • Khlistunova, I.1    Biernat, J.2    Wang, Y.3    Pickhardt, M.4    Von Bergen, M.5    Gazova, Z.6    Mandelkow, E.7    Mandelkow, E.M.8
  • 11
    • 0037414833 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding
    • Cho, J. H., and Johnson, G. V. (2003) Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding. J Biol Chem 278, 187-93.
    • (2003) J Biol Chem , vol.278 , pp. 187-193
    • Cho, J.H.1    Johnson, G.V.2
  • 12
    • 34447119530 scopus 로고    scopus 로고
    • Resolution of the nuclear localization mechanism of glycogen synthase kinase-3: Functional effects in apoptosis
    • Meares, G. P., and Jope, R. S. (2007) Resolution of the nuclear localization mechanism of glycogen synthase kinase-3: functional effects in apoptosis. J Biol Chem 282, 16989-7001.
    • (2007) J Biol Chem , vol.282 , pp. 16989-17001
    • Meares, G.P.1    Jope, R.S.2
  • 13
    • 11144228296 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 beta induces caspase- cleaved tau aggregation in situ
    • Cho, J. H., and Johnson, G. V. (2004) Glycogen synthase kinase 3 beta induces caspase- cleaved tau aggregation in situ. J Biol Chem 279, 54716-23.
    • (2004) J Biol Chem , vol.279 , pp. 54716-54723
    • Cho, J.H.1    Johnson, G.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.