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Volumn 43, Issue 32, 2004, Pages 10302-10307

Formation of amyloid fibers triggered by phosphatidylserine-containing membranes

Author keywords

[No Author keywords available]

Indexed keywords

BIREFRINGENCE; DISEASES; PHOSPHOLIPIDS; PHYSIOLOGY; PROTEINS; TISSUE; TOXICITY;

EID: 4043100348     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049002c     Document Type: Article
Times cited : (242)

References (49)
  • 1
    • 0242300624 scopus 로고    scopus 로고
    • Games played by rogue proteins in prion disorders and Alzheimer's disease
    • Aguzzi, A., and Haass, C. (2003) Games played by rogue proteins in prion disorders and Alzheimer's disease, Science 302, 814-818.
    • (2003) Science , vol.302 , pp. 814-818
    • Aguzzi, A.1    Haass, C.2
  • 2
    • 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., and 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
  • 4
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insight into protein folding, misfolding disease and biological evolution
    • Stefani, M., and Dobson, C. M. (2003) Protein aggregation and aggregate toxicity: new insight into protein folding, misfolding disease and biological evolution, J. Mol. Med. 81, 678-699.
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 6
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the Aplysia CPEB has prion-like properties
    • Si, K., Lindquist, S., and Kandel, E. R. (2003) A neuronal isoform of the Aplysia CPEB has prion-like properties, Cell 115, 879-891.
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 9
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist, M., Lindstrom, F., Watts, A., and Grobner, G. (2004) Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation, J. Mol. Biol. 335, 1039-1049.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindstrom, F.2    Watts, A.3    Grobner, G.4
  • 10
    • 0024434507 scopus 로고
    • Purification and analysis of H1 histones
    • Cole, R. D. (1989) Purification and analysis of H1 histones, Methods Enzymol. 170, 524-532.
    • (1989) Methods Enzymol. , vol.170 , pp. 524-532
    • Cole, R.D.1
  • 12
    • 0027452422 scopus 로고
    • Probing biomembrane interfacial and pH profiles with a new type of float-like fluorophores positioned at varying distance from the membrane surface
    • Kraayenhof, R., Sterk, G. J., and Wong Fong Sang, H. W. (1993) Probing biomembrane interfacial and pH profiles with a new type of float-like fluorophores positioned at varying distance from the membrane surface, Biochemistry 32, 10057-10066.
    • (1993) Biochemistry , vol.32 , pp. 10057-10066
    • Kraayenhof, R.1    Sterk, G.J.2    Wong Fong Sang, H.W.3
  • 13
    • 0029863068 scopus 로고    scopus 로고
    • Dissociation of cytochrome c from liposomes by histone H1. Comparison with basic peptides
    • Rytömaa, M., and Kinnunen, P. K. J. (1996) Dissociation of cytochrome c from liposomes by histone H1. Comparison with basic peptides, Biochemistry 35, 4529-4539.
    • (1996) Biochemistry , vol.35 , pp. 4529-4539
    • Rytömaa, M.1    Kinnunen, P.K.J.2
  • 15
    • 0032477811 scopus 로고    scopus 로고
    • Binding and dissociation of cytochrome c to and from membranes containing acidic phospholipids
    • Subramanian, M., Jutila, A., and Kinnunen, P. K. J. (1998) Binding and dissociation of cytochrome c to and from membranes containing acidic phospholipids, Biochemistry 37, 1394-1402.
    • (1998) Biochemistry , vol.37 , pp. 1394-1402
    • Subramanian, M.1    Jutila, A.2    Kinnunen, P.K.J.3
  • 16
    • 0028057721 scopus 로고
    • Evidence for two distinct acidic phospholipid-binding sites in cytochrome c
    • Rytömaa, M., and Kinnunen, P. K. J. (1994) Evidence for two distinct acidic phospholipid-binding sites in cytochrome c, J. Biol. Chem. 269, 1770-1774.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1770-1774
    • Rytömaa, M.1    Kinnunen, P.K.J.2
  • 17
    • 0029035902 scopus 로고
    • Evidence for ternary complex formation by histone H1, DNA, and liposomes
    • Koiv, A., Palvimo, J., and Kinnunen, P. K. J. (1995) Evidence for ternary complex formation by histone H1, DNA, and liposomes, Biochemistry 34, 8018-8027.
    • (1995) Biochemistry , vol.34 , pp. 8018-8027
    • Koiv, A.1    Palvimo, J.2    Kinnunen, P.K.J.3
  • 18
    • 0028179865 scopus 로고
    • Alzheimer β-amyloid peptide 25-35: Electrostatic interactions with phospholipid membranes
    • Terzi, E., Hoelzemann, G., and Seelig, J. (1994) Alzheimer β-amyloid peptide 25-35: electrostatic interactions with phospholipid membranes, Biochemistry 33, 7434-7441.
    • (1994) Biochemistry , vol.33 , pp. 7434-7441
    • Terzi, E.1    Hoelzemann, G.2    Seelig, J.3
  • 19
    • 0014088274 scopus 로고
    • Lipid content of amyloid fibrils purified by a variety of methods
    • Kirn, I.-C, Shirahama, T., and Cohen, A. S. (1967) Lipid content of amyloid fibrils purified by a variety of methods, Am. J. Pathol. 50, 869-886.
    • (1967) Am. J. Pathol. , vol.50 , pp. 869-886
    • Kirn, I.-C.1    Shirahama, T.2    Cohen, A.S.3
  • 20
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein, J. Biol. Chem. 274, 36859-36865.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 21
    • 0032562547 scopus 로고    scopus 로고
    • Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest
    • McLaurin, J., Franklin, T., Chakrabartty, A., and Fraser, P. E. (1998) Phosphatidylinositol and inositol involvement in Alzheimer amyloid-β fibril growth and arrest, J. Mol. Biol. 278, 183-194.
    • (1998) J. Mol. Biol. , vol.278 , pp. 183-194
    • McLaurin, J.1    Franklin, T.2    Chakrabartty, A.3    Fraser, P.E.4
  • 22
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization in α-synuclein: Implication for the pathogenesis and treatment of Parkinson's disease
    • Voiles, M. J., Lee, S.-J., Rochet, J.-C., Shtilerman, M. D., Ding, T. T., Kessler, J. C., and Lansbury, P. T., Jr. (2001) Vesicle permeabilization in α-synuclein: implication for the pathogenesis and treatment of Parkinson's disease, Biochemistry 40, 7812-7819.
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Voiles, M.J.1    Lee, S.-J.2    Rochet, J.-C.3    Shtilerman, M.D.4    Ding, T.T.5    Kessler, J.C.6    Lansbury Jr., P.T.7
  • 24
    • 0030007501 scopus 로고    scopus 로고
    • Characteristics of the binding of tacrine to acidic phospholipids
    • Lehtonen, J. Y. A., Rytömaa, M., and Kinnunen, P. K. J. (1996) Characteristics of the binding of tacrine to acidic phospholipids, Biophys. J. 70, 2185-2194.
    • (1996) Biophys. J. , vol.70 , pp. 2185-2194
    • Lehtonen, J.Y.A.1    Rytömaa, M.2    Kinnunen, P.K.J.3
  • 26
    • 0035949632 scopus 로고    scopus 로고
    • Anion shielding of electrostatic repulsion in transthyretin modulates stability and amyloidosis: Insight into the chaotrope unfolding dichotomy
    • Hammarström, P., Jiang, X., Deechongkit, S., and Kelly, J. W. (2001) Anion shielding of electrostatic repulsion in transthyretin modulates stability and amyloidosis: insight into the chaotrope unfolding dichotomy, Biochemistry 40, 11453-11459.
    • (2001) Biochemistry , vol.40 , pp. 11453-11459
    • Hammarström, P.1    Jiang, X.2    Deechongkit, S.3    Kelly, J.W.4
  • 27
    • 1642575162 scopus 로고    scopus 로고
    • Neurodegeneration in familial amyloid polyneuropathy: From pathology to molecular signaling
    • Sousa, M. M., and Saraiva, M. J. (2003) Neurodegeneration in familial amyloid polyneuropathy: from pathology to molecular signaling, Prog. Neurobiol. 71, 385-400.
    • (2003) Prog. Neurobiol. , vol.71 , pp. 385-400
    • Sousa, M.M.1    Saraiva, M.J.2
  • 28
    • 0035909893 scopus 로고    scopus 로고
    • Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis
    • Chakrabartty, A. (2001) Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis, Proc. Natl. Acad. Sci. U.S.A. 98, 14757-14759.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14757-14759
    • Chakrabartty, A.1
  • 29
    • 0029559770 scopus 로고
    • Neural membrane phospholipids in Alzheimer disease
    • Wells, K., Farooqui, A. A., Liss, L., and Horrocks, L. A. (1995) Neural membrane phospholipids in Alzheimer disease, Neurochem. Res. 20, 1329-1333.
    • (1995) Neurochem. Res. , vol.20 , pp. 1329-1333
    • Wells, K.1    Farooqui, A.A.2    Liss, L.3    Horrocks, L.A.4
  • 31
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn, J., Feil, S. C., McKinstry, W. J., Tweten, R. K., and Parker, M. W. (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form, Cell 89, 685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 32
    • 0037046163 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-synuclein is sensitive to Parkinson's disease-related mutations and occurs by a pore-like mechanism
    • Voiles, M. J., and Lansbury, P. T., Jr. (2002) Vesicle permeabilization by protofibrillar α-synuclein is sensitive to Parkinson's disease-related mutations and occurs by a pore-like mechanism, Biochemistry 41, 4595-4602.
    • (2002) Biochemistry , vol.41 , pp. 4595-4602
    • Voiles, M.J.1    Lansbury Jr., P.T.2
  • 33
    • 0025743796 scopus 로고
    • Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes
    • Utsugi, T., Schroit, A. J., Connor, J., Bucana, C. D., and Fidler, I. J. (1991) Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes, Cancer Res. 51, 3062-3066.
    • (1991) Cancer Res. , vol.51 , pp. 3062-3066
    • Utsugi, T.1    Schroit, A.J.2    Connor, J.3    Bucana, C.D.4    Fidler, I.J.5
  • 34
    • 0036891466 scopus 로고    scopus 로고
    • Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy
    • Ran, S., and Thorpe, P. E. (2002) Phosphatidylserine is a marker of tumor vasculature and a potential target for cancer imaging and therapy, Int. J. Radiat. Oncol. Biol. Phys. 54, 1479-1484.
    • (2002) Int. J. Radiat. Oncol. Biol. Phys. , vol.54 , pp. 1479-1484
    • Ran, S.1    Thorpe, P.E.2
  • 35
    • 0015494028 scopus 로고
    • Effect of phosphatidylserine decarboxylase on neural excitation
    • Cook, A. M., Low, E., and Ishijimi, M. (1972) Effect of phosphatidylserine decarboxylase on neural excitation, Nature 239, 150-151.
    • (1972) Nature , vol.239 , pp. 150-151
    • Cook, A.M.1    Low, E.2    Ishijimi, M.3
  • 38
    • 3543060532 scopus 로고    scopus 로고
    • Interaction of histone Hl with phospholipids and comparison of its binding to giant liposomes and human leukemic T cells
    • in press
    • Zhao, H., Bose, S., Tuominen, E. K. J., and Kinnunen, P. K. J. (2004) Interaction of histone Hl with phospholipids and comparison of its binding to giant liposomes and human leukemic T cells, Biochemistry (in press).
    • (2004) Biochemistry
    • Zhao, H.1    Bose, S.2    Tuominen, E.K.J.3    Kinnunen, P.K.J.4
  • 39
    • 0034233061 scopus 로고    scopus 로고
    • Oxidative refolding of lysozyme assisted by negatively charged liposomes: Relationship with lysozyme-mediated fusion of liposomes
    • Kuboi, R., Mawatari, T., and Yoshimoto, M. (2000) Oxidative refolding of lysozyme assisted by negatively charged liposomes: relationship with lysozyme-mediated fusion of liposomes, J. Biosci. Bioeng. 90, 14-19.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 14-19
    • Kuboi, R.1    Mawatari, T.2    Yoshimoto, M.3
  • 40
    • 0024347069 scopus 로고
    • Lysozyme and cancer: Role of exogenous lysozyme as anticancer agent
    • Sava, G., Ceschia, V., and Pacor, S. (1989) Lysozyme and cancer: role of exogenous lysozyme as anticancer agent, Anti-cancer Res. 9, 583-591.
    • (1989) Anti-cancer Res. , vol.9 , pp. 583-591
    • Sava, G.1    Ceschia, V.2    Pacor, S.3
  • 41
    • 0022976585 scopus 로고
    • Fusion of negatively charged phospholipid vesicles by insulin. Relationship with lipid fluidity
    • Farias, R. N., Vinals, A. L., and Morero, R. D. (1986) Fusion of negatively charged phospholipid vesicles by insulin. Relationship with lipid fluidity, J. Biol. Chem. 261, 15508-15512.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15508-15512
    • Farias, R.N.1    Vinals, A.L.2    Morero, R.D.3
  • 42
    • 0344394259 scopus 로고    scopus 로고
    • Long-term treatment with insulin induces apoptosis in brown adipocytes: Role of oxidative stress
    • Porras, A., Zuluaga, S., Valladares, A., Alvarez, A. M., Herrera, B., Fabregat, L, and Benito, M. (2003) Long-term treatment with insulin induces apoptosis in brown adipocytes: Role of oxidative stress, Endocrinology 144, 5390-5401.
    • (2003) Endocrinology , vol.144 , pp. 5390-5401
    • Porras, A.1    Zuluaga, S.2    Valladares, A.3    Alvarez, A.M.4    Herrera, B.5    Fabregat, L.6    Benito, M.7
  • 43
    • 0037136057 scopus 로고    scopus 로고
    • Interaction of nominally soluble proteins with phospholipid monolayers at the air-water interface
    • Pitcher, W. H., Keller, S. L., and Huestis, W. H. (2002) Interaction of nominally soluble proteins with phospholipid monolayers at the air-water interface, Biochim. Biophys. Acta 1564, 107-113.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 107-113
    • Pitcher, W.H.1    Keller, S.L.2    Huestis, W.H.3
  • 44
    • 0028947544 scopus 로고
    • Conformational changes of myoglobin upon interaction with negatively-charged phospholipid vesicles
    • Bergers, J. J., Van Bloois, L., Barenholz, Y., and Crommelin, D. J. A. (1995) Conformational changes of myoglobin upon interaction with negatively-charged phospholipid vesicles, J. Liposome Res. 5, 311-326.
    • (1995) J. Liposome Res. , vol.5 , pp. 311-326
    • Bergers, J.J.1    Van Bloois, L.2    Barenholz, Y.3    Crommelin, D.J.A.4
  • 45
    • 0037108018 scopus 로고    scopus 로고
    • A role for the myoglobin redox in the induction of endothelial cell apoptosis
    • D'Agnillo, F., and Alayash, A. I. (2002) A role for the myoglobin redox in the induction of endothelial cell apoptosis, Free Radical Biol. Med. 33, 1153-1164.
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 1153-1164
    • D'Agnillo, F.1    Alayash, A.I.2
  • 46
    • 0031036872 scopus 로고    scopus 로고
    • Prevention; of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J., and Liu, X. (1997) Prevention; of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked, Science 275, 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2
  • 47
    • 0029842987 scopus 로고    scopus 로고
    • Histone H1 suppresses tumor growth of leukemia cells in vitro, ex vivo and in an animal model suggesting extracellular functions of histones
    • Class, R., Lindman, S., Fassbender, C., Leinenbach, H. P., Rawer, S., Emrich, J. G., Brady, L. W., and Zeppezauer, M. (1996) Histone H1 suppresses tumor growth of leukemia cells in vitro, ex vivo and in an animal model suggesting extracellular functions of histones, Am. J. Clin. Oncol. 19, 522-531.
    • (1996) Am. J. Clin. Oncol. , vol.19 , pp. 522-531
    • Class, R.1    Lindman, S.2    Fassbender, C.3    Leinenbach, H.P.4    Rawer, S.5    Emrich, J.G.6    Brady, L.W.7    Zeppezauer, M.8
  • 48
    • 0037821763 scopus 로고    scopus 로고
    • The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions
    • Agasoster, A. V., Halskau, O., Fuglebakk, E., Froystein, N. A., Muga, A., Holmsen, H., and Martinez, A. (2003) The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions, J. Biol. Chem. 278, 21790-21797.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21790-21797
    • Agasoster, A.V.1    Halskau, O.2    Fuglebakk, E.3    Froystein, N.A.4    Muga, A.5    Holmsen, H.6    Martinez, A.7


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