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Volumn 51, Issue 3, 2012, Pages 776-785

Probing structural features of Alzheimers amyloid-β pores in bilayers using site-specific amino acid substitutions

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMERS DISEASE; AMINO ACID SUBSTITUTION; ATOMIC RESOLUTION; BI-LAYER; CELLULAR MEMBRANES; CHANNEL ACTIVITY; CHANNEL CONDUCTANCE; CHANNEL FORMATION; CHANNEL STRUCTURES; COMPUTATIONAL MODEL; DRUG DESIGN; EXPERIMENTAL EVIDENCE; ION FLUXES; MD SIMULATION; MOLECULAR DYNAMICS SIMULATIONS; MUTATION SITES; MUTATIONAL ANALYSIS; POINT MUTATIONS; POLYMORPHIC STATE; SITE-SPECIFIC; STRUCTURAL FEATURE; STRUCTURAL MODELS; WILD TYPES;

EID: 84856262919     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2017427     Document Type: Article
Times cited : (49)

References (71)
  • 1
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimers disease
    • Selkoe, D. J. (1991) The molecular pathology of Alzheimers disease Neuron 6, 487-498
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 2
    • 0024314702 scopus 로고
    • Amyloid β protein precursor and the pathogenesis of Alzheimer's disease
    • DOI 10.1016/0092-8674(89)90093-7
    • Selkoe, D. J. (1989) Amyloid β protein precursor and the pathogenesis of Alzheimers disease Cell 58, 611-612 (Pubitemid 19210954)
    • (1989) Cell , vol.58 , Issue.4 , pp. 611-612
    • Selkoe, D.J.1
  • 3
    • 0024309958 scopus 로고
    • Aging, amyloid, and Alzheimers disease
    • Selkoe, D. J. (1989) Aging, amyloid, and Alzheimers disease N. Engl. J. Med. 320, 1484-1487
    • (1989) N. Engl. J. Med. , vol.320 , pp. 1484-1487
    • Selkoe, D.J.1
  • 4
    • 84861183285 scopus 로고    scopus 로고
    • Intracellular Aβ-oligomers and early inflammation in a model of Alzheimers disease
    • Ferretti, M. T., Bruno, M. A., Ducatenzeiler, A., Klein, W. L., and Cuello, A. C. (2011) Intracellular Aβ-oligomers and early inflammation in a model of Alzheimers disease Neurobiol. Aging DOI: 10.1016/j.neurobiolaging. 2011.01.007
    • (2011) Neurobiol. Aging
    • Ferretti, M.T.1    Bruno, M.A.2    Ducatenzeiler, A.3    Klein, W.L.4    Cuello, A.C.5
  • 5
    • 0035993237 scopus 로고    scopus 로고
    • Aβ toxicity in Alzheimers disease: Globular oligomers (ADDLs) as new vaccine and drug targets
    • Klein, W. L. (2002) Aβ toxicity in Alzheimers disease: Globular oligomers (ADDLs) as new vaccine and drug targets Neurochem. Int. 41, 345-352
    • (2002) Neurochem. Int. , vol.41 , pp. 345-352
    • Klein, W.L.1
  • 6
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., and Mori, H. (2011) Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo J. Neurosci. Res. 89, 1031-1042
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5    Klein, W.L.6    Mori, H.7
  • 7
    • 33646485088 scopus 로고    scopus 로고
    • Early and late cytotoxic effects of external application of the Alzheimers Aβ result from the initial formation and function of Aβ ion channels
    • Simakova, O. and Arispe, N. J. (2006) Early and late cytotoxic effects of external application of the Alzheimers Aβ result from the initial formation and function of Aβ ion channels Biochemistry 45, 5907-5915
    • (2006) Biochemistry , vol.45 , pp. 5907-5915
    • Simakova, O.1    Arispe, N.J.2
  • 8
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: Evidence for AβP channel-mediated cellular toxicity
    • Bhatia, R., Lin, H., and Lal, R. (2000) Fresh and globular amyloid β protein (1-42) induces rapid cellular degeneration: Evidence for AβP channel-mediated cellular toxicity FASEB J. 14, 1233-1243 (Pubitemid 30350405)
    • (2000) FASEB Journal , vol.14 , Issue.9 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 9
    • 0034089960 scopus 로고    scopus 로고
    • Fresh and nonfibrillar amyloid β protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AβP-channel-mediated cellular toxicity
    • Zhu, Y. J., Lin, H., and Lal, R. (2000) Fresh and nonfibrillar amyloid β protein(1-40) induces rapid cellular degeneration in aged human fibroblasts: Evidence for AβP-channel-mediated cellular toxicity FASEB J. 14, 1244-1254 (Pubitemid 30350406)
    • (2000) FASEB Journal , vol.14 , Issue.9 , pp. 1244-1254
    • Zhu, Y.J.1    Lin, H.2    Lal, R.3
  • 13
    • 34548788549 scopus 로고    scopus 로고
    • Models of β-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • DOI 10.1529/biophysj.107.110148
    • Jang, H., Zheng, J., and Nussinov, R. (2007) Models of β-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process Biophys. J. 93, 1938-1949 (Pubitemid 47437578)
    • (2007) Biophysical Journal , vol.93 , Issue.6 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 14
    • 72549099399 scopus 로고    scopus 로고
    • Misfolded Amyloid Ion Channels Present Mobile β-Sheet Subunits in Contrast to Conventional Ion Channels
    • Jang, H., Arce, F. T., Capone, R., Ramachandran, S., Lal, R., and Nussinov, R. (2009) Misfolded Amyloid Ion Channels Present Mobile β-Sheet Subunits in Contrast to Conventional Ion Channels Biophys. J. 97, 3029-3037
    • (2009) Biophys. J. , vol.97 , pp. 3029-3037
    • Jang, H.1    Arce, F.T.2    Capone, R.3    Ramachandran, S.4    Lal, R.5    Nussinov, R.6
  • 15
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • DOI 10.1016/S0196-9781(02)00067-0, PII S0196978102000670
    • Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., and Lin, M. C. (2002) The channel hypothesis of Alzheimers disease: Current status Peptides 23, 1311-1315 (Pubitemid 34786709)
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.-C.5
  • 16
    • 37249067994 scopus 로고    scopus 로고
    • The cell-selective neurotoxicity of the Alzheimer's Aβ peptide is determined by surface phosphatidylserine and cytosolic ATP levels. Membrane binding is required for Aβ toxicity
    • DOI 10.1523/JNEUROSCI.3006-07.2007
    • Simakova, O. and Arispe, N. J. (2007) The Cell-Selective Neurotoxicity of the Alzheimers Aβ Peptide Is Determined by Surface Phosphatidylserine and Cytosolic ATP Levels. Membrane Binding Is Required for Aβ Toxicity J. Neurosci. 27, 13719-13729 (Pubitemid 350278273)
    • (2007) Journal of Neuroscience , vol.27 , Issue.50 , pp. 13719-13729
    • Simakova, O.1    Arispe, N.J.2
  • 17
    • 0026423215 scopus 로고
    • Alzheimers disease. in the beginning
    • Selkoe, D. J. (1991) Alzheimers disease. In the beginning Nature 354, 432-433
    • (1991) Nature , vol.354 , pp. 432-433
    • Selkoe, D.J.1
  • 18
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • DOI 10.1126/science.1072994
    • Hardy, J. (2002) The Amyloid Hypothesis of Alzheimers Disease: Progress and Problems on the Road to Therapeutics Science 297, 353-356 (Pubitemid 34790756)
    • (2002) Science , vol.297 , Issue.5580 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 19
    • 0026597063 scopus 로고
    • Alzheimers disease: The amyloid cascade hypothesis
    • Hardy, J. A. and Higgins, G. A. (1992) Alzheimers disease: The amyloid cascade hypothesis Science 256, 184-185
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 21
    • 84855750207 scopus 로고    scopus 로고
    • 2+ imaging implicates Aβ1-42 amyloid pores in Alzheimers disease pathology
    • 2+ imaging implicates Aβ1-42 amyloid pores in Alzheimers disease pathology J. Cell Biol. 195, 515-524
    • (2011) J. Cell Biol. , vol.195 , pp. 515-524
    • Demuro, A.1    Smith, M.2    Parker, I.3
  • 22
    • 0034856924 scopus 로고    scopus 로고
    • Diversity of amyloid β protein fragment [1-40]-formed channels
    • DOI 10.1023/A:1010995121153
    • Kourie, J. I., Henry, C. L., and Farrelly, P. (2001) Diversity of amyloid β protein fragment [1-40]-formed channels Cell. Mol. Neurobiol. 21, 255-284 (Pubitemid 32852779)
    • (2001) Cellular and Molecular Neurobiology , vol.21 , Issue.3 , pp. 255-284
    • Kourie, J.I.1    Henry, C.L.2    Farrelly, P.3
  • 24
    • 0028649480 scopus 로고
    • 2+ channels provides a mechanism for neuronal death in Alzheimers disease
    • 2+ channels provides a mechanism for neuronal death in Alzheimers disease Ann. N.Y. Acad. Sci. 747, 256-266
    • (1994) Ann. N.Y. Acad. Sci. , vol.747 , pp. 256-266
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 27
    • 0033566369 scopus 로고    scopus 로고
    • Alzheimer amyloid Aβ1-42 channels: Effects of solvent, pH, and Congo Red
    • DOI 10.1002/(SICI)1097-4547(19990815)57:4<458::AID-JNR5>3.0.CO;2-4
    • Hirakura, Y., Lin, M. C., and Kagan, B. L. (1999) Alzheimer amyloid Aβ1-42 channels: Effects of solvent, pH, and Congo Red J. Neurosci. Res. 57, 458-466 (Pubitemid 29372920)
    • (1999) Journal of Neuroscience Research , vol.57 , Issue.4 , pp. 458-466
    • Hirakura, Y.1    Lin, M.-C.2    Kagan, B.L.3
  • 30
    • 0035997224 scopus 로고    scopus 로고
    • Electrophysiologic properties of channels induced by Aβ25-35 in planar lipid bilayers
    • DOI 10.1016/S0196-9781(02)00057-8, PII S0196978102000578
    • Lin, M. C. and Kagan, B. L. (2002) Electrophysiologic properties of channels induced by Aβ25-35 in planar lipid bilayers Peptides 23, 1215-1228 (Pubitemid 34786701)
    • (2002) Peptides , vol.23 , Issue.7 , pp. 1215-1228
    • Lin, M.-C.A.1    Kagan, B.L.2
  • 36
    • 0034282630 scopus 로고    scopus 로고
    • Substitutions at codon 22 of Alzheimers Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells
    • Miravalle, L., Tokuda, T., Chiarle, R., Giaccone, G., Bugiani, O., Tagliavini, F., Frangione, B., and Ghiso, J. (2000) Substitutions at codon 22 of Alzheimers Aβ peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells J. Biol. Chem. 275, 27110-27116
    • (2000) J. Biol. Chem. , vol.275 , pp. 27110-27116
    • Miravalle, L.1    Tokuda, T.2    Chiarle, R.3    Giaccone, G.4    Bugiani, O.5    Tagliavini, F.6    Frangione, B.7    Ghiso, J.8
  • 37
    • 0034982951 scopus 로고    scopus 로고
    • Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy
    • DOI 10.1002/ana.1009
    • Grabowski, T. J., Cho, H. S., Vonsattel, J. P. G., Rebeck, G. W., and Greenberg, S. M. (2001) Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy Ann. Neurol. 49, 697-705 (Pubitemid 32530235)
    • (2001) Annals of Neurology , vol.49 , Issue.6 , pp. 697-705
    • Grabowski, T.J.1    Cho, H.S.2    Vonsattel, J.P.G.3    William Rebeck, G.4    Greenberg, S.M.5
  • 38
    • 79251539305 scopus 로고    scopus 로고
    • Point Mutations in Aβ Result in the Formation of Distinct Polymorphic Aggregates in the Presence of Lipid Bilayers
    • e16248
    • Pifer, P. M., Yates, E. A., and Legleiter, J. (2011) Point Mutations in Aβ Result in the Formation of Distinct Polymorphic Aggregates in the Presence of Lipid Bilayers PLoS One 6 e16248
    • (2011) PLoS One , vol.6
    • Pifer, P.M.1    Yates, E.A.2    Legleiter, J.3
  • 39
    • 0036288788 scopus 로고    scopus 로고
    • Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-42 mutants of familial Alzheimer's disease at positions 21-23
    • DOI 10.1016/S0006-291X(02)00430-8, PII S0006291X02004308
    • Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. (2002) Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-42 mutants of familial Alzheimers disease at positions 21-23 Biochem. Biophys. Res. Commun. 294, 5-10 (Pubitemid 34687206)
    • (2002) Biochemical and Biophysical Research Communications , vol.294 , Issue.1 , pp. 5-10
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 40
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • DOI 10.1074/jbc.M301874200
    • Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. (2003) Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: Implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimers disease J. Biol. Chem. 278, 46179-46187 (Pubitemid 37432769)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 43
    • 84856298593 scopus 로고    scopus 로고
    • Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All- d -Enantiomer of Alzheimers β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology
    • in press, DOI: 10.1021/jp2108126.
    • Connelly, L., Teran, A. F., Jang, H., Capone, R., Kotler, S. A., Ramachandran, S., Kagan, B. L., Nussinov, R., and Lal, R. (2011) Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All- d -Enantiomer of Alzheimers β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology. J. Phys. Chem. B, in press, DOI: 10.1021/jp2108126.
    • (2011) J. Phys. Chem. B
    • Connelly, L.1    Teran, A.F.2    Jang, H.3    Capone, R.4    Kotler, S.A.5    Ramachandran, S.6    Kagan, B.L.7    Nussinov, R.8    Lal, R.9
  • 45
    • 77956419916 scopus 로고    scopus 로고
    • Models of membrane-bound Alzheimers Aβ peptide assemblies
    • Shafrir, Y., Durell, S., Arispe, N., and Guy, H. R. (2010) Models of membrane-bound Alzheimers Aβ peptide assemblies Proteins 78, 3473-3487
    • (2010) Proteins , vol.78 , pp. 3473-3487
    • Shafrir, Y.1    Durell, S.2    Arispe, N.3    Guy, H.R.4
  • 46
    • 77957105623 scopus 로고    scopus 로고
    • Transmembrane Structures for Alzheimers Aβ(1-42) Oligomers
    • Strodel, B., Lee, J. W. L., Whittleston, C. S., and Wales, D. J. (2010) Transmembrane Structures for Alzheimers Aβ(1-42) Oligomers J. Am. Chem. Soc. 132, 13300-13312
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13300-13312
    • Strodel, B.1    Lee, J.W.L.2    Whittleston, C.S.3    Wales, D.J.4
  • 47
    • 0141819130 scopus 로고    scopus 로고
    • Microfabricated Teflon membranes for low-noise recordings of ion channels in planar lipid bilayers
    • Mayer, M., Kriebel, J. K., Tosteson, M. T., and Whitesides, G. M. (2003) Microfabricated Teflon membranes for low-noise recordings of ion channels in planar lipid bilayers Biophys. J. 85, 2684-2695 (Pubitemid 37210814)
    • (2003) Biophysical Journal , vol.85 , Issue.4 , pp. 2684-2695
    • Mayer, M.1    Kriebel, J.K.2    Tosteson, M.T.3    Whitesides, G.M.4
  • 48
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M. and Mueller, P. (1972) Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties Proc. Natl. Acad. Sci. U.S.A. 69, 3561-3566
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 50
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • DOI 10.1021/bi051952q
    • Petkova, A. T., Yau, W. M., and Tycko, R. (2006) Experimental constraints on quaternary structure in Alzheimers β-amyloid fibrils Biochemistry 45, 498-512 (Pubitemid 43100415)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 498-512
    • Petkova, A.T.1    Yau, W.-M.2    Tycko, R.3
  • 51
  • 52
    • 38949167084 scopus 로고    scopus 로고
    • New structures help the modeling of toxic amyloid β ion channels
    • Jang, H., Zheng, J., Lal, R., and Nussinov, R. (2008) New structures help the modeling of toxic amyloid β ion channels Trends Biochem. Sci. 33, 91-100
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 91-100
    • Jang, H.1    Zheng, J.2    Lal, R.3    Nussinov, R.4
  • 56
    • 34547214510 scopus 로고    scopus 로고
    • Aβ ion channels. Prospects for treating Alzheimer's disease with Aβ channel blockers
    • DOI 10.1016/j.bbamem.2007.03.014, PII S0005273607001034
    • Arispe, N., Diaz, J. C., and Simakova, O. (2007) Aβ ion channels. Prospects for treating Alzheimers disease with Aβ channel blockers Biochim. Biophys. Acta 1768, 1952-1965 (Pubitemid 47125852)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.8 , pp. 1952-1965
    • Arispe, N.1    Diaz, J.C.2    Simakova, O.3
  • 57
    • 0027374494 scopus 로고
    • A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid β protein (AβP) in phospholipid bilayer membranes
    • DOI 10.1111/j.1749-6632.1993.tb23046.x
    • Pollard, H. B., Rojas, E., and Arispe, N. (1993) A new hypothesis for the mechanism of amyloid toxicity, based on the calcium channel activity of amyloid β protein (AβP) in phospholipid bilayer membranes Ann. N.Y. Acad. Sci. 695, 165-168 (Pubitemid 23348255)
    • (1993) Annals of the New York Academy of Sciences , vol.695 , pp. 165-168
    • Pollard, H.B.1    Rojas, E.2    Arispe, N.3
  • 58
    • 85043367528 scopus 로고    scopus 로고
    • Amyloidosis and Protein Folding
    • Kagan, L. B. and Dobson, C. M. (2005) Amyloidosis and Protein Folding Science 307, 42-43
    • (2005) Science , vol.307 , pp. 42-43
    • Kagan, L.B.1    Dobson, C.M.2
  • 59
    • 0030966536 scopus 로고    scopus 로고
    • 2+- sensitive, cation- selective channels across excised membrane patches from hypothalamic neurons
    • 2+-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons Biophys. J. 73, 67-75 (Pubitemid 27274105)
    • (1997) Biophysical Journal , vol.73 , Issue.1 , pp. 67-75
    • Kawahara, M.1    Arispe, N.2    Kuroda, Y.3    Rojas, E.4
  • 60
    • 0035159553 scopus 로고    scopus 로고
    • Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology
    • DOI 10.1096/fj.01-0377com
    • Lin, H., Bhatia, R., and Lal, R. (2001) Amyloid β protein forms ion channels: Implications for Alzheimers disease pathophysiology FASEB J. 15, 2433-2444 (Pubitemid 33063171)
    • (2001) FASEB Journal , vol.15 , Issue.13 , pp. 2433-2444
    • Lin, H.1    Bhatia, R.2    Lal, R.3
  • 61
    • 62649172167 scopus 로고    scopus 로고
    • Small molecule blockers of the Alzheimer Aβ calcium channel potently protect neurons from Aβ cytotoxicity
    • Diaz, J. C., Simakova, O., Jacobson, K. A., Arispe, N., and Pollard, H. B. (2009) Small molecule blockers of the Alzheimer Aβ calcium channel potently protect neurons from Aβ cytotoxicity Proc. Natl. Acad. Sci. U.S.A. 106, 3348-3353
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 3348-3353
    • Diaz, J.C.1    Simakova, O.2    Jacobson, K.A.3    Arispe, N.4    Pollard, H.B.5
  • 62
    • 0033485580 scopus 로고    scopus 로고
    • Erratum: Hirakura, Y., Lin, M.-C., Kagan, B. L. 1999. Alzheimer amyloid Aβ1-42 channels: Effects of solvent, pH, and Congo red. J. Neurosci. Res. 57:458-466
    • Hirakura, Y., Lin, M. C., and Kagan, B. (1999) Erratum: Hirakura, Y., Lin, M.-C., Kagan, B. L. 1999. Alzheimer amyloid Aβ1-42 channels: Effects of solvent, pH, and Congo red. J. Neurosci. Res. 57:458-466 J. Neurosci. Res 58, 726
    • (1999) J. Neurosci. Res , vol.58 , pp. 726
    • Hirakura, Y.1    Lin, M.C.2    Kagan, B.3
  • 63
    • 1542600164 scopus 로고    scopus 로고
    • Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis
    • DOI 10.1016/j.jmb.2003.11.008, PII S0022283603013925
    • Williams, A. D., Portelius, E., Kheterpal, I., Guo, J. T., Cook, K. D., Xu, Y., and Wetzel, R. (2004) Mapping Aβ amyloid fibril secondary structure using scanning proline mutagenesis J. Mol. Biol. 335, 833-842 (Pubitemid 38352823)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.3 , pp. 833-842
    • Williams, A.D.1    Portelius, E.2    Kheterpal, I.3    Guo, J.-T.4    Cook, K.D.5    Xu, Y.6    Wetzel, R.7
  • 64
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • Cannon, M. J., Williams, A. D., Wetzel, R., and Myszka, D. G. (2004) Kinetic analysis of β-amyloid fibril elongation Anal. Biochem. 328, 67-75 (Pubitemid 38479619)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 67-75
    • Cannon, M.J.1    Williams, A.D.2    Wetzel, R.3    Myszka, D.G.4
  • 65
    • 0028920098 scopus 로고
    • Prolines and amyloidogenicity in fragments of the Alzheimers peptide β/A4
    • Wood, S. J., Wetzel, R., Martin, J. D., and Hurle, M. R. (1995) Prolines and amyloidogenicity in fragments of the Alzheimers peptide β/A4 Biochemistry 34, 724-730
    • (1995) Biochemistry , vol.34 , pp. 724-730
    • Wood, S.J.1    Wetzel, R.2    Martin, J.D.3    Hurle, M.R.4
  • 66
    • 33644817349 scopus 로고    scopus 로고
    • Scanning cysteine mutagenesis analysis of Aβ(1-40) amyloid fibrils
    • Shivaprasad, S. and Wetzel, R. (2006) Scanning cysteine mutagenesis analysis of Aβ(1-40) amyloid fibrils J. Biol. Chem. 281, 993-1000
    • (2006) J. Biol. Chem. , vol.281 , pp. 993-1000
    • Shivaprasad, S.1    Wetzel, R.2
  • 69
    • 0033779406 scopus 로고    scopus 로고
    • Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers
    • Krasilnikov, O. V., Merzlyak, P. G., Yuldasheva, L. N., Rodrigues, C. G., Bhakdi, S., and Valeva, A. (2000) Electrophysiological evidence for heptameric stoichiometry of ion channels formed by Staphylococcus aureus α-toxin in planar lipid bilayers Mol. Microbiol. 37, 1372-1378
    • (2000) Mol. Microbiol. , vol.37 , pp. 1372-1378
    • Krasilnikov, O.V.1    Merzlyak, P.G.2    Yuldasheva, L.N.3    Rodrigues, C.G.4    Bhakdi, S.5    Valeva, A.6
  • 71
    • 0030886648 scopus 로고    scopus 로고
    • Probing the structure of the diphtheria toxin channel: Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives
    • DOI 10.1085/jgp.110.3.229
    • Huynh, P. D., Cui, C., Zhan, H. J., Oh, K. J., Collier, R. J., and Finkelstein, A. (1997) Probing the structure of the diphtheria toxin channel: Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives J. Gen. Physiol. 110, 229-242 (Pubitemid 27388116)
    • (1997) Journal of General Physiology , vol.110 , Issue.3 , pp. 229-242
    • Huynh, P.D.1    Cui, C.2    Zhan, H.3    Oh, K.J.4    Collier, R.J.5    Finkelstein, A.6


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