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Volumn 413, Issue , 2006, Pages 313-325

Screening for Modulators of Aggregation with a Microplate Elongation Assay

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; ETHINYLESTRADIOL; GOSSYPOL ACETIC ACID; GUAIAZULENE; LATAMOXEF; MERBROMIN; METACYCLINE; MONOMER; PROTOPORPHYRIN;

EID: 33749521675     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(06)13016-5     Document Type: Review
Times cited : (13)

References (30)
  • 2
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M., Mitra S., Schweitzer E.S., Segal M.R., and Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431 (2004) 805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 3
    • 0035203662 scopus 로고    scopus 로고
    • Key factors in Alzheimer's disease: Beta-amyloid precursor protein processing, metabolism and intraneuronal transport
    • Bayer T.A., Wirths O., Majtenyi K., Hartmann T., Multhaup G., Beyreuther K., and Czech C. Key factors in Alzheimer's disease: Beta-amyloid precursor protein processing, metabolism and intraneuronal transport. Brain Pathol. 11 (2001) 1-11
    • (2001) Brain Pathol. , vol.11 , pp. 1-11
    • Bayer, T.A.1    Wirths, O.2    Majtenyi, K.3    Hartmann, T.4    Multhaup, G.5    Beyreuther, K.6    Czech, C.7
  • 4
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 (2001) 1552-1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 5
    • 0035881211 scopus 로고    scopus 로고
    • A microtiter plate assay for polyglutamine aggregate extension
    • Berthelier V., Hamilton J.B., Chen S., and Wetzel R. A microtiter plate assay for polyglutamine aggregate extension. Anal. Biochem. 295 (2001) 227-236
    • (2001) Anal. Biochem. , vol.295 , pp. 227-236
    • Berthelier, V.1    Hamilton, J.B.2    Chen, S.3    Wetzel, R.4
  • 6
    • 0037209202 scopus 로고    scopus 로고
    • An assay for characterizing in vitro the kinetics of polyglutamine aggregation
    • Berthelier V., and Wetzel R. An assay for characterizing in vitro the kinetics of polyglutamine aggregation. Methods Mol. Biol. 217 (2003) 295-303
    • (2003) Methods Mol. Biol. , vol.217 , pp. 295-303
    • Berthelier, V.1    Wetzel, R.2
  • 8
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B., and Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26 (2003) 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 9
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A., Mina E., Kayed R., Milton S.C., Parker I., and Glabe C.G. Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J. Biol. Chem. 280 (2005) 17294-17300
    • (2005) J. Biol. Chem. , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 17
  • 18
    • 0037044835 scopus 로고    scopus 로고
    • New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease
    • Lashuel H.A., Hartley D.M., Balakhaneh D., Aggarwal A., Teichberg S., and Callaway D.J. New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. J. Biol. Chem. 277 (2002) 42881-42890
    • (2002) J. Biol. Chem. , vol.277 , pp. 42881-42890
    • Lashuel, H.A.1    Hartley, D.M.2    Balakhaneh, D.3    Aggarwal, A.4    Teichberg, S.5    Callaway, D.J.6
  • 21
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • Poirier M.A., Li H., Macosko J., Cai S., Amzel M., and Ross C.A. Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277 (2002) 41032-41037
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 22
    • 0031873102 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto C., Sigurdsson E.M., Morelli L., Kumar R.A., Castano E.M., and Frangione B. Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat. Med. 4 (1998) 822-826
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 23
    • 0037079065 scopus 로고    scopus 로고
    • Chemical genetic screening approaches to neurobiology
    • Stockwell B.R. Chemical genetic screening approaches to neurobiology. Neuron 36 (2002) 559-562
    • (2002) Neuron , vol.36 , pp. 559-562
    • Stockwell, B.R.1
  • 24
    • 0037415751 scopus 로고    scopus 로고
    • From Alzheimer to Huntington: Why is a structural understanding so difficult?
    • Temussi P.A., Masino L., and Pastore A. From Alzheimer to Huntington: Why is a structural understanding so difficult?. EMBO J. 22 (2003) 355-361
    • (2003) EMBO J. , vol.22 , pp. 355-361
    • Temussi, P.A.1    Masino, L.2    Pastore, A.3
  • 25
    • 2542427690 scopus 로고    scopus 로고
    • Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration
    • Walsh D.M., and Selkoe D.J. Oligomers on the brain: The emerging role of soluble protein aggregates in neurodegeneration. Protein Pept. Lett. 11 (2004) 213-228
    • (2004) Protein Pept. Lett. , vol.11 , pp. 213-228
    • Walsh, D.M.1    Selkoe, D.J.2
  • 26
    • 27344445112 scopus 로고    scopus 로고
    • Protein folding and aggregation in the expanded polyglutamine repeat diseases
    • Buchner J., and Kiefhaber T. (Eds), Wiley Wiley press, N.Y
    • Wetzel R. Protein folding and aggregation in the expanded polyglutamine repeat diseases. In: Buchner J., and Kiefhaber T. (Eds). "The Protein Folding Handbook" (2005), Wiley Wiley press, N.Y
    • (2005) "The Protein Folding Handbook"
    • Wetzel, R.1
  • 27
    • 33749251393 scopus 로고    scopus 로고
    • Chemical and physical properties of polyglutamine repeat sequences
    • Wells R., and Ashizawa T. (Eds), Elsevier, San Diego Elsevier-Academic press, San Diego
    • Wetzel R. Chemical and physical properties of polyglutamine repeat sequences. In: Wells R., and Ashizawa T. (Eds). "Genetic Instabilities and Neurological Diseases" (2006), Elsevier, San Diego Elsevier-Academic press, San Diego
    • (2006) "Genetic Instabilities and Neurological Diseases"
    • Wetzel, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.