메뉴 건너뛰기




Volumn 9, Issue 3, 2007, Pages 270-275

Pore-forming proteins share structural and functional homology with amyloid oligomers

Author keywords

Hemolysin; Alzheimer's disease; Amyloid ; Hemolysis; Perforin; Pore forming protein; Toxicity

Indexed keywords

ALPHA HEMOLYSIN; AMYLOID PROTEIN; HEMOLYSIN; OLIGOMER; PERFORIN; UNCLASSIFIED DRUG;

EID: 36249023636     PISSN: 15351084     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12017-007-0003-6     Document Type: Article
Times cited : (62)

References (15)
  • 1
    • 77955095800 scopus 로고
    • Staphylococcal alpha-toxin: Oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles
    • Bhakdi, S., Fussle, R., & Tranum-Jensen J. (1981). Staphylococcal alpha-toxin: oligomerization of hydrophilic monomers to form amphiphilic hexamers induced through contact with deoxycholate detergent micelles. Proceedings of the National Academy of Sciences of the USA, 78, 5475-5479.
    • (1981) Proceedings of the National Academy of Sciences of the USA , vol.78 , pp. 5475-5479
    • Bhakdi, S.1    Fussle, R.2    Tranum-Jensen, J.3
  • 4
    • 0032548897 scopus 로고    scopus 로고
    • Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers
    • Czajkowsky, D. M., Sheng, S., & Shao, Z. (1998). Staphylococcal alpha-hemolysin can form hexamers in phospholipid bilayers. Journal of Molecular Biology, 276, 325-330.
    • (1998) Journal of Molecular Biology , vol.276 , pp. 325-330
    • Czajkowsky, D.M.1    Sheng, S.2    Shao, Z.3
  • 5
    • 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., & Glabe, C. G. (2005). Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. Journal of Biological Chemistry, 280, 17294-17300.
    • (2005) Journal of Biological Chemistry , 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
  • 7
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003). Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 8
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E., & Glabe, C. G. (2004). Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. Journal of Biological Chemistry, 279, 46363-46366.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 9
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., & Lansbury, P. T. Jr. (2002). Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature, 418, 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury Jr., P.T.5
  • 10
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H. III (1993). Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Science, 2, 404-410.
    • (1993) Protein Science , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 11
    • 0037427958 scopus 로고    scopus 로고
    • Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin
    • Montoya, M., & Gouaux, E. (2003). Beta-barrel membrane protein folding and structure viewed through the lens of alpha-hemolysin. Biochimica et Biophysica Acta, 1609, 19-27.
    • (2003) Biochimica et Biophysica Acta , vol.1609 , pp. 19-27
    • Montoya, M.1    Gouaux, E.2
  • 12
    • 0025864902 scopus 로고    scopus 로고
    • Ojcius, D. M., Persechini, P. M., Zheng, L. M., Notaroberto, P. C., Adeodato, S. C., &, Young, J. D. (1991). Cytolytic and ion channel-forming properties of the N terminus of lymphocyte perforin. Proceedings of the National Academy of Sciences of the USA, 88, 4621-4625.
    • Ojcius, D. M., Persechini, P. M., Zheng, L. M., Notaroberto, P. C., Adeodato, S. C., &, Young, J. D. (1991). Cytolytic and ion channel-forming properties of the N terminus of lymphocyte perforin. Proceedings of the National Academy of Sciences of the USA, 88, 4621-4625.
  • 14
    • 2542483823 scopus 로고    scopus 로고
    • ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures
    • Srinivasan, R., Marchant, R. E., & Zagorski, M. G. (2004). ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures. Amyloid, 11, 10-13.
    • (2004) Amyloid , vol.11 , pp. 10-13
    • Srinivasan, R.1    Marchant, R.E.2    Zagorski, M.G.3
  • 15
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M., & Dobson, C. M. (2003). Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. Journal of Molecular Medicine, 81, 678-699.
    • (2003) Journal of Molecular Medicine , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.