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Volumn 11, Issue 10, 2015, Pages

ApoE4-specific Misfolded Intermediate Identified by Molecular Dynamics Simulations

Author keywords

[No Author keywords available]

Indexed keywords

MOLECULAR DYNAMICS; PHYSIOLOGY;

EID: 84946036229     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1004359     Document Type: Article
Times cited : (19)

References (68)
  • 1
    • 0024299370 scopus 로고
    • Apolipoprotein E: cholesterol transport protein with expanding role in cell biology
    • Mahley RW, Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science. 1988;240: 622–630. 3283935
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 2
    • 0028303072 scopus 로고
    • Apolipoprotein E: structure-function relationships
    • Weisgraber KH, Apolipoprotein E: structure-function relationships. Adv Protein Chem. 1994;45: 249–302. doi: 10.1016/S0065-3233(08)60642-7 8154371
    • (1994) Adv Protein Chem , vol.45 , pp. 249-302
    • Weisgraber, K.H.1
  • 3
    • 0034575124 scopus 로고    scopus 로고
    • Apolipoprotein E: far more than a lipid transport protein
    • Mahley RW, Rall SC, Apolipoprotein E: far more than a lipid transport protein. Annu Rev Genomics Hum Genet. 2000;1: 507–537. doi: 10.1146/annurev.genom.1.1.507 11701639
    • (2000) Annu Rev Genomics Hum Genet , vol.1 , pp. 507-537
    • Mahley, R.W.1    Rall, S.C.2
  • 4
    • 0023860891 scopus 로고
    • Apolipoprotein E polymorphism and atherosclerosis
    • Davignon J, Gregg RE, Sing CF, Apolipoprotein E polymorphism and atherosclerosis. Arteriosclerosis. 1988;8: 1–21. doi: 10.1161/01.ATV.8.1.1 3277611
    • (1988) Arteriosclerosis , vol.8 , pp. 1-21
    • Davignon, J.1    Gregg, R.E.2    Sing, C.F.3
  • 5
    • 0037184994 scopus 로고    scopus 로고
    • Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease
    • Morrow JA, Hatters DM, Lu B, Hochtl P, Oberg KA, Rupp B, et al. Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology; 2002;277: 50380–50385. doi: 10.1074/jbc.M204898200 12393895
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 50380-50385
    • Morrow, J.A.1    Hatters, D.M.2    Lu, B.3    Hochtl, P.4    Oberg, K.A.5    Rupp, B.6
  • 7
    • 65249182101 scopus 로고    scopus 로고
    • Molecular mechanism of apolipoprotein E binding to lipoprotein particles
    • Nguyen D, Dhanasekaran P, Phillips MC, Lund-Katz S, Molecular mechanism of apolipoprotein E binding to lipoprotein particles. Biochemistry. 2009;48: 3025–3032. doi: 10.1021/bi9000694 19209940
    • (2009) Biochemistry , vol.48 , pp. 3025-3032
    • Nguyen, D.1    Dhanasekaran, P.2    Phillips, M.C.3    Lund-Katz, S.4
  • 8
    • 0029844205 scopus 로고    scopus 로고
    • Human apolipoprotein E: the Alzheimer's disease connection
    • Weisgraber KH, Mahley RW, Human apolipoprotein E: the Alzheimer's disease connection. FASEB J. 1996;10: 1485–1494. 8940294
    • (1996) FASEB J , vol.10 , pp. 1485-1494
    • Weisgraber, K.H.1    Mahley, R.W.2
  • 9
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder EH, Saunders AM, Strittmatter WJ, Schmechel DE, Gaskell PC, Small GW, et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science. 1993;261: 921–923. 8346443
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1    Saunders, A.M.2    Strittmatter, W.J.3    Schmechel, D.E.4    Gaskell, P.C.5    Small, G.W.6
  • 11
    • 84885076245 scopus 로고    scopus 로고
    • Impact of apolipoprotein E on Alzheimer's disease
    • Hauser PS, Ryan RO, Impact of apolipoprotein E on Alzheimer's disease. Curr Alzheimer Res. 2013;10: 809–817. 23919769
    • (2013) Curr Alzheimer Res , vol.10 , pp. 809-817
    • Hauser, P.S.1    Ryan, R.O.2
  • 12
    • 33645808672 scopus 로고    scopus 로고
    • Apolipoprotein E4: a causative factor and therapeutic target in neuropathology, including Alzheimer's disease
    • Mahley RW, Weisgraber KH, Huang Y, Apolipoprotein E4: a causative factor and therapeutic target in neuropathology, including Alzheimer's disease. Proc Natl Acad Sci USA. National Acad Sciences; 2006;103: 5644–5651. doi: 10.1073/pnas.0600549103 16567625
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 5644-5651
    • Mahley, R.W.1    Weisgraber, K.H.2    Huang, Y.3
  • 13
    • 84909578703 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases
    • Huang Y, Mahley RW, Apolipoprotein E: Structure and function in lipid metabolism, neurobiology, and Alzheimer's diseases. Neurobiol Dis. 2014. doi: 10.1016/j.nbd.2014.08.025
    • (2014) Neurobiol Dis
    • Huang, Y.1    Mahley, R.W.2
  • 14
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson C, Wardell MR, Weisgraber KH, Mahley RW, Agard DA, Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science. 1991;252: 1817–1822. 2063194
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 15
    • 0029784503 scopus 로고    scopus 로고
    • Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia
    • Dong LM, Parkin S, Trakhanov SD, Rupp B, Simmons T, Arnold KS, et al. Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia. Nat Struct Biol. 1996;3: 718–722. 8756331
    • (1996) Nat Struct Biol , vol.3 , pp. 718-722
    • Dong, L.M.1    Parkin, S.2    Trakhanov, S.D.3    Rupp, B.4    Simmons, T.5    Arnold, K.S.6
  • 16
    • 80052604940 scopus 로고    scopus 로고
    • Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions
    • Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions. National Acad Sciences; 2011;108: 14813–14818. doi: 10.1073/pnas.1106420108
    • (2011) National Acad Sciences , vol.108 , pp. 14813-14818
  • 17
    • 0036795744 scopus 로고    scopus 로고
    • Influence of apoE domain structure and polymorphism on the kinetics of phospholipid vesicle solubilization
    • Segall ML, Dhanasekaran P, Baldwin F, Anantharamaiah GM, Weisgraber KH, Phillips MC, et al. Influence of apoE domain structure and polymorphism on the kinetics of phospholipid vesicle solubilization. The Journal of Lipid Research. American Society for Biochemistry and Molecular Biology; 2002;43: 1688–1700. doi: 10.1194/jlr.M200157-JLR200 12364553
    • (2002) The Journal of Lipid Research , vol.43 , pp. 1688-1700
    • Segall, M.L.1    Dhanasekaran, P.2    Baldwin, F.3    Anantharamaiah, G.M.4    Weisgraber, K.H.5    Phillips, M.C.6
  • 18
    • 33746311471 scopus 로고    scopus 로고
    • Apolipoprotein E structure: insights into function
    • Hatters DM, Peters-Libeu CA, Weisgraber KH, Apolipoprotein E structure: insights into function. Trends Biochem Sci. 2006;31: 445–454. doi: 10.1016/j.tibs.2006.06.008 16820298
    • (2006) Trends Biochem Sci , vol.31 , pp. 445-454
    • Hatters, D.M.1    Peters-Libeu, C.A.2    Weisgraber, K.H.3
  • 19
    • 29444460533 scopus 로고    scopus 로고
    • Apolipoprotein (apo) E4 enhances amyloid peptide production in cultured neuronal cells: ApoE structure as a potential therapeutic target
    • Ye S, Huang Y, Mullendorff K, Dong L, Giedt G, Meng EC, et al. Apolipoprotein (apo) E4 enhances amyloid peptide production in cultured neuronal cells: ApoE structure as a potential therapeutic target. Proceedings of the National Academy of Sciences. National Acad Sciences; 2005;102: 18700–18705.
    • (2005) Proceedings of the National Academy of Sciences , vol.102 , pp. 18700-18705
    • Ye, S.1    Huang, Y.2    Mullendorff, K.3    Dong, L.4    Giedt, G.5    Meng, E.C.6
  • 21
    • 84908032605 scopus 로고    scopus 로고
    • The Binding of Apolipoprotein E to Oligomers and Fibrils of Amyloid-β Alters the Kinetics of Amyloid Aggregation
    • Garai K, Verghese PB, Baban B, Holtzman DM, Frieden C, The Binding of Apolipoprotein E to Oligomers and Fibrils of Amyloid-β Alters the Kinetics of Amyloid Aggregation. Biochemistry. 2014.
    • (2014) Biochemistry
    • Garai, K.1    Verghese, P.B.2    Baban, B.3    Holtzman, D.M.4    Frieden, C.5
  • 22
    • 12144290271 scopus 로고    scopus 로고
    • Neuron-specific apolipoprotein e4 proteolysis is associated with increased tau phosphorylation in brains of transgenic mice
    • Brecht WJ, Harris FM, Chang S, Tesseur I, Yu G-Q, Xu Q, et al. Neuron-specific apolipoprotein e4 proteolysis is associated with increased tau phosphorylation in brains of transgenic mice. J Neurosci. 2004;24: 2527–2534. doi: 10.1523/JNEUROSCI.4315-03.2004 15014128
    • (2004) J Neurosci , vol.24 , pp. 2527-2534
    • Brecht, W.J.1    Harris, F.M.2    Chang, S.3    Tesseur, I.4    Yu, G.-Q.5    Xu, Q.6
  • 23
    • 0033889344 scopus 로고    scopus 로고
    • Expression of human apolipoprotein E4 in neurons causes hyperphosphorylation of protein tau in the brains of transgenic mice
    • Tesseur I, Van Dorpe J, Spittaels K, Van den Haute C, Moechars D, Van Leuven F, Expression of human apolipoprotein E4 in neurons causes hyperphosphorylation of protein tau in the brains of transgenic mice. Am J Pathol. 2000;156: 951–964. doi: 10.1016/S0002-9440(10)64963-2 10702411
    • (2000) Am J Pathol , vol.156 , pp. 951-964
    • Tesseur, I.1    Van Dorpe, J.2    Spittaels, K.3    Van den Haute, C.4    Moechars, D.5    Van Leuven, F.6
  • 24
    • 7244253060 scopus 로고    scopus 로고
    • Increased tau phosphorylation in apolipoprotein E4 transgenic mice is associated with activation of extracellular signal-regulated kinase: modulation by zinc
    • Harris FM, Brecht WJ, Xu Q, Mahley RW, Huang Y, Increased tau phosphorylation in apolipoprotein E4 transgenic mice is associated with activation of extracellular signal-regulated kinase: modulation by zinc. Journal of Biological Chemistry. 2004;279: 44795–44801. doi: 10.1074/jbc.M408127200 15322121
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 44795-44801
    • Harris, F.M.1    Brecht, W.J.2    Xu, Q.3    Mahley, R.W.4    Huang, Y.5
  • 26
    • 0022408782 scopus 로고
    • Behavior of human apolipoprotein E in aqueous solutions and at interfaces
    • Yokoyama S, Kawai Y, Tajima S, Yamamoto A, Behavior of human apolipoprotein E in aqueous solutions and at interfaces. Journal of Biological Chemistry. 1985;260: 16375–16382. 4066713
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 16375-16382
    • Yokoyama, S.1    Kawai, Y.2    Tajima, S.3    Yamamoto, A.4
  • 27
    • 34548701564 scopus 로고    scopus 로고
    • A monomeric, biologically active, full-length human apolipoprotein E
    • Zhang Y, Vasudevan S, Sojitrawala R, Zhao W, Cui C, Xu C, et al. A monomeric, biologically active, full-length human apolipoprotein E. Biochemistry. 2007;46: 10722–10732. doi: 10.1021/bi700672v 17715945
    • (2007) Biochemistry , vol.46 , pp. 10722-10732
    • Zhang, Y.1    Vasudevan, S.2    Sojitrawala, R.3    Zhao, W.4    Cui, C.5    Xu, C.6
  • 28
    • 0032443390 scopus 로고    scopus 로고
    • Discrete molecular dynamics studies of the folding of a protein-like model
    • Dokholyan NV, Buldyrev SV, Stanley HE, Shakhnovich EI, Discrete molecular dynamics studies of the folding of a protein-like model. Fold Des. 1998;3: 577–587. 9889167
    • (1998) Fold Des , vol.3 , pp. 577-587
    • Dokholyan, N.V.1    Buldyrev, S.V.2    Stanley, H.E.3    Shakhnovich, E.I.4
  • 29
    • 84864247114 scopus 로고    scopus 로고
    • Discrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization
    • Shirvanyants D, Ding F, Tsao D, Ramachandran S, Dokholyan NV, Discrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization. J Phys Chem B. 2012;116: 8375–8382. doi: 10.1021/jp2114576 22280505
    • (2012) J Phys Chem B , vol.116 , pp. 8375-8382
    • Shirvanyants, D.1    Ding, F.2    Tsao, D.3    Ramachandran, S.4    Dokholyan, N.V.5
  • 32
    • 0037026730 scopus 로고    scopus 로고
    • Comparison of the stabilities and unfolding pathways of human apolipoprotein E isoforms by differential scanning calorimetry and circular dichroism
    • Acharya P, Segall ML, Zaiou M, Morrow J, Weisgraber KH, Phillips MC, et al. Comparison of the stabilities and unfolding pathways of human apolipoprotein E isoforms by differential scanning calorimetry and circular dichroism. Biochim Biophys Acta. 2002;1584: 9–19. 12213488
    • (2002) Biochim Biophys Acta , vol.1584 , pp. 9-19
    • Acharya, P.1    Segall, M.L.2    Zaiou, M.3    Morrow, J.4    Weisgraber, K.H.5    Phillips, M.C.6
  • 33
    • 0034718456 scopus 로고    scopus 로고
    • Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain
    • Morrow JA, Segall ML, Lund-Katz S, Phillips MC, Knapp M, Rupp B, et al. Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain. Biochemistry. 2000;39: 11657–11666. doi: 10.1021/bi000099m 10995233
    • (2000) Biochemistry , vol.39 , pp. 11657-11666
    • Morrow, J.A.1    Segall, M.L.2    Lund-Katz, S.3    Phillips, M.C.4    Knapp, M.5    Rupp, B.6
  • 34
    • 34249777526 scopus 로고    scopus 로고
    • Eris: an automated estimator of protein stability
    • Yin S, Ding F, Dokholyan NV, Eris: an automated estimator of protein stability. Nat Methods. 2007;4: 466–467. doi: 10.1038/nmeth0607-466 17538626
    • (2007) Nat Methods , vol.4 , pp. 466-467
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3
  • 35
    • 36749018607 scopus 로고    scopus 로고
    • Modeling backbone flexibility improves protein stability estimation
    • Yin S, Ding F, Dokholyan NV, Modeling backbone flexibility improves protein stability estimation. Structure. 2007;15: 1567–1576. doi: 10.1016/j.str.2007.09.024 18073107
    • (2007) Structure , vol.15 , pp. 1567-1576
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3
  • 36
    • 0028092997 scopus 로고
    • Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms
    • Dong LM, Wilson C, Wardell MR, Simmons T, Mahley RW, Weisgraber KH, et al. Human apolipoprotein E. Role of arginine 61 in mediating the lipoprotein preferences of the E3 and E4 isoforms. Journal of Biological Chemistry. 1994;269: 22358–22365. 8071364
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 22358-22365
    • Dong, L.M.1    Wilson, C.2    Wardell, M.R.3    Simmons, T.4    Mahley, R.W.5    Weisgraber, K.H.6
  • 37
    • 0029766916 scopus 로고    scopus 로고
    • Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins
    • Dong LM, Weisgraber KH, Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins. Journal of Biological Chemistry. 1996;271: 19053–19057. doi: 10.1074/jbc.271.32.19053 8702576
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 19053-19057
    • Dong, L.M.1    Weisgraber, K.H.2
  • 38
    • 84892909138 scopus 로고    scopus 로고
    • Concerning the structure of apoE
    • Frieden C, Garai K, Concerning the structure of apoE. Protein Sci. 2013;22: 1820–1825. doi: 10.1002/pro.2379 24115173
    • (2013) Protein Sci , vol.22 , pp. 1820-1825
    • Frieden, C.1    Garai, K.2
  • 39
    • 0033564771 scopus 로고    scopus 로고
    • Expression of human apolipoprotein E3 or E4 in the brains of Apoe-/- mice: isoform-specific effects on neurodegeneration
    • Buttini M, Orth M, Bellosta S, Akeefe H, Pitas RE, Wyss-Coray T, et al. Expression of human apolipoprotein E3 or E4 in the brains of Apoe-/- mice: isoform-specific effects on neurodegeneration. J Neurosci. 1999;19: 4867–4880. 10366621
    • (1999) J Neurosci , vol.19 , pp. 4867-4880
    • Buttini, M.1    Orth, M.2    Bellosta, S.3    Akeefe, H.4    Pitas, R.E.5    Wyss-Coray, T.6
  • 40
    • 0034055035 scopus 로고    scopus 로고
    • Dominant negative effects of apolipoprotein E4 revealed in transgenic models of neurodegenerative disease
    • Buttini M, Akeefe H, Lin C, Mahley RW, Pitas RE, Wyss-Coray T, et al. Dominant negative effects of apolipoprotein E4 revealed in transgenic models of neurodegenerative disease. Neuroscience. 2000;97: 207–210. doi: 10.1016/S0306-4522(00)00069-5 10799751
    • (2000) Neuroscience , vol.97 , pp. 207-210
    • Buttini, M.1    Akeefe, H.2    Lin, C.3    Mahley, R.W.4    Pitas, R.E.5    Wyss-Coray, T.6
  • 41
    • 0032894924 scopus 로고    scopus 로고
    • Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
    • Fisher CA, Ryan RO, Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E. The Journal of Lipid Research. 1999;40: 93–99. 9869654
    • (1999) The Journal of Lipid Research , vol.40 , pp. 93-99
    • Fisher, C.A.1    Ryan, R.O.2
  • 42
    • 2942535903 scopus 로고    scopus 로고
    • Apolipoprotein E4 domain interaction occurs in living neuronal cells as determined by fluorescence resonance energy transfer
    • Xu Q, Brecht WJ, Weisgraber KH, Mahley RW, Huang Y, Apolipoprotein E4 domain interaction occurs in living neuronal cells as determined by fluorescence resonance energy transfer. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology; 2004;279: 25511–25516. doi: 10.1074/jbc.M311256200 15054100
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 25511-25516
    • Xu, Q.1    Brecht, W.J.2    Weisgraber, K.H.3    Mahley, R.W.4    Huang, Y.5
  • 43
    • 26644459735 scopus 로고    scopus 로고
    • Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms
    • Hatters DM, Budamagunta MS, Voss JC, Weisgraber KH, Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms. Journal of Biological Chemistry. American Society for Biochemistry and Molecular Biology; 2005;280: 34288–34295. doi: 10.1074/jbc.M506044200 16076841
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 34288-34295
    • Hatters, D.M.1    Budamagunta, M.S.2    Voss, J.C.3    Weisgraber, K.H.4
  • 44
    • 84863115245 scopus 로고    scopus 로고
    • Small molecule structure correctors abolish detrimental effects of apolipoprotein E4 in cultured neurons
    • Chen H-K, Liu Z, Meyer-Franke A, Brodbeck J, Miranda RD, McGuire JG, et al. Small molecule structure correctors abolish detrimental effects of apolipoprotein E4 in cultured neurons. J Biol Chem. American Society for Biochemistry and Molecular Biology; 2012;287: 5253–5266. doi: 10.1074/jbc.M111.276162 22158868
    • (2012) J Biol Chem , vol.287 , pp. 5253-5266
    • Chen, H.-K.1    Liu, Z.2    Meyer-Franke, A.3    Brodbeck, J.4    Miranda, R.D.5    McGuire, J.G.6
  • 45
    • 84868597475 scopus 로고    scopus 로고
    • Small-molecule structure correctors target abnormal protein structure and function: structure corrector rescue of apolipoprotein E4-associated neuropathology
    • Mahley RW, Huang Y, Small-molecule structure correctors target abnormal protein structure and function: structure corrector rescue of apolipoprotein E4-associated neuropathology. J Med Chem. 2012;55: 8997–9008. doi: 10.1021/jm3008618 23013167
    • (2012) J Med Chem , vol.55 , pp. 8997-9008
    • Mahley, R.W.1    Huang, Y.2
  • 46
    • 50849129147 scopus 로고    scopus 로고
    • Biophysical analysis of progressive C-terminal truncations of human apolipoprotein E4: insights into secondary structure and unfolding properties
    • Chroni A, Pyrpassopoulos S, Thanassoulas A, Nounesis G, Zannis VI, Stratikos E, Biophysical analysis of progressive C-terminal truncations of human apolipoprotein E4: insights into secondary structure and unfolding properties. Biochemistry. 2008;47: 9071–9080. doi: 10.1021/bi800469r 18690708
    • (2008) Biochemistry , vol.47 , pp. 9071-9080
    • Chroni, A.1    Pyrpassopoulos, S.2    Thanassoulas, A.3    Nounesis, G.4    Zannis, V.I.5    Stratikos, E.6
  • 47
    • 84861903643 scopus 로고    scopus 로고
    • Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease
    • Frieden C, Garai K, Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease. Proc Natl Acad Sci USA. National Acad Sciences; 2012;109: 8913–8918. doi: 10.1073/pnas.1207022109 22615372
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 8913-8918
    • Frieden, C.1    Garai, K.2
  • 48
    • 26044471824 scopus 로고    scopus 로고
    • Isoform-specific interactions of human apolipoprotein E to an intermediate conformation of human Alzheimer amyloid-beta peptide
    • Stratman NC, Castle CK, Taylor BM, Epps DE, Melchior GW, Carter DB, Isoform-specific interactions of human apolipoprotein E to an intermediate conformation of human Alzheimer amyloid-beta peptide. Chem Phys Lipids. 2005;137: 52–61. doi: 10.1016/j.chemphyslip.2005.06.005 16140289
    • (2005) Chem Phys Lipids , vol.137 , pp. 52-61
    • Stratman, N.C.1    Castle, C.K.2    Taylor, B.M.3    Epps, D.E.4    Melchior, G.W.5    Carter, D.B.6
  • 49
    • 84891502796 scopus 로고    scopus 로고
    • Soluble apoE/Aβ complex: mechanism and therapeutic target for APOE4-induced AD risk
    • Tai LM, Mehra S, Shete V, Estus S, Rebeck GW, Bu G, et al. Soluble apoE/Aβ complex: mechanism and therapeutic target for APOE4-induced AD risk. Mol Neurodegener. BioMed Central Ltd; 2014;9: 2. doi: 10.1186/1750-1326-9-2 24386905
    • (2014) Mol Neurodegener , vol.9 , pp. 2
    • Tai, L.M.1    Mehra, S.2    Shete, V.3    Estus, S.4    Rebeck, G.W.5    Bu, G.6
  • 50
    • 84873722367 scopus 로고    scopus 로고
    • Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy
    • Liu C-C, Liu C-C, Kanekiyo T, Xu H, Bu G, Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy. Nat Rev Neurol. 2013;9: 106–118. doi: 10.1038/nrneurol.2012.263 23296339
    • (2013) Nat Rev Neurol , vol.9 , pp. 106-118
    • Liu, C.-C.1    Liu, C.-C.2    Kanekiyo, T.3    Xu, H.4    Bu, G.5
  • 51
    • 65249158083 scopus 로고    scopus 로고
    • Understanding the association of apolipoprotein E4 with Alzheimer disease: clues from its structure
    • Zhong N, Weisgraber KH, Understanding the association of apolipoprotein E4 with Alzheimer disease: clues from its structure. Journal of Biological Chemistry. 2009;284: 6027–6031. doi: 10.1074/jbc.R800009200 18948255
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 6027-6031
    • Zhong, N.1    Weisgraber, K.H.2
  • 52
    • 78649817606 scopus 로고    scopus 로고
    • Isoform-specific proteolysis of apolipoprotein-E in the brain
    • Elliott DA, Tsoi K, Holinkova S, Chan SL, Kim WS, Halliday GM, et al. Isoform-specific proteolysis of apolipoprotein-E in the brain. Neurobiol Aging. 2011;32: 257–271. doi: 10.1016/j.neurobiolaging.2009.02.006 19278755
    • (2011) Neurobiol Aging , vol.32 , pp. 257-271
    • Elliott, D.A.1    Tsoi, K.2    Holinkova, S.3    Chan, S.L.4    Kim, W.S.5    Halliday, G.M.6
  • 53
    • 84899796613 scopus 로고    scopus 로고
    • Extracellular proteolysis of apolipoprotein E (apoE) by secreted serine neuronal protease
    • Tamboli IY, Heo D, Rebeck GW, Extracellular proteolysis of apolipoprotein E (apoE) by secreted serine neuronal protease. PLoS ONE. 2014;9: e93120. doi: 10.1371/journal.pone.0093120 24675880
    • (2014) PLoS ONE , vol.9 , pp. 93120
    • Tamboli, I.Y.1    Heo, D.2    Rebeck, G.W.3
  • 54
    • 84880759084 scopus 로고    scopus 로고
    • Proteolytic cleavage of apolipoprotein E4 as the keystone for the heightened risk associated with Alzheimer's disease
    • Rohn TT, Proteolytic cleavage of apolipoprotein E4 as the keystone for the heightened risk associated with Alzheimer's disease. Int J Mol Sci. 2013;14: 14908–14922. doi: 10.3390/ijms140714908 23867607
    • (2013) Int J Mol Sci , vol.14 , pp. 14908-14922
    • Rohn, T.T.1
  • 55
    • 0035902514 scopus 로고    scopus 로고
    • Apolipoprotein E fragments present in Alzheimer's disease brains induce neurofibrillary tangle-like intracellular inclusions in neurons
    • Huang Y, Liu XQ, Wyss-Coray T, Brecht WJ, Sanan DA, Mahley RW, Apolipoprotein E fragments present in Alzheimer's disease brains induce neurofibrillary tangle-like intracellular inclusions in neurons. Proceedings of the National Academy of Sciences. National Acad Sciences; 2001;98: 8838–8843. doi: 10.1073/pnas.151254698
    • (2001) Proceedings of the National Academy of Sciences , vol.98 , pp. 8838-8843
    • Huang, Y.1    Liu, X.Q.2    Wyss-Coray, T.3    Brecht, W.J.4    Sanan, D.A.5    Mahley, R.W.6
  • 56
    • 80054972554 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization
    • Huang RY-C, Garai K, Frieden C, Gross ML, Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization. Biochemistry. 2011;50: 9273–9282. doi: 10.1021/bi2010027 21899263
    • (2011) Biochemistry , vol.50 , pp. 9273-9282
    • Huang, R.Y.-C.1    Garai, K.2    Frieden, C.3    Gross, M.L.4
  • 57
    • 66349085616 scopus 로고    scopus 로고
    • Apolipoprotein E: structure determines function, from atherosclerosis to Alzheimer's disease to AIDS
    • Mahley RW, Weisgraber KH, Huang Y, Apolipoprotein E: structure determines function, from atherosclerosis to Alzheimer's disease to AIDS. The Journal of Lipid Research. 2009;50 Suppl: S183–8. doi: 10.1194/jlr.R800069-JLR200 19106071
    • (2009) The Journal of Lipid Research , vol.50 , pp. 183-188
    • Mahley, R.W.1    Weisgraber, K.H.2    Huang, Y.3
  • 58
    • 0034031680 scopus 로고    scopus 로고
    • Effective energy functions for protein structure prediction
    • Lazaridis T, Karplus M, Effective energy functions for protein structure prediction. Curr Opin Struct Biol. 2000;10: 139–145. doi: 10.1016/S0959-440X(00)00063-4 10753811
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 139-145
    • Lazaridis, T.1    Karplus, M.2
  • 59
    • 36749107785 scopus 로고
    • Molecular dynamics simulations at constant pressure and/or temperature
    • Andersen HC, Molecular dynamics simulations at constant pressure and/or temperature. J Chem Phys. 1980;72: 2384. doi: 10.1063/1.439486
    • (1980) J Chem Phys , vol.72 , pp. 2384
    • Andersen, H.C.1
  • 60
    • 78649763344 scopus 로고    scopus 로고
    • Automated minimization of steric clashes in protein structures
    • Ramachandran S, Kota P, Ding F, Dokholyan NV, Automated minimization of steric clashes in protein structures. Proteins. Wiley Subscription Services, Inc., A Wiley Company; 2010;79: 261–270. doi: 10.1002/prot.22879
    • (2010) Proteins , vol.79 , pp. 261-270
    • Ramachandran, S.1    Kota, P.2    Ding, F.3    Dokholyan, N.V.4
  • 61
    • 79961202365 scopus 로고    scopus 로고
    • Gaia: automated quality assessment of protein structure models
    • Kota P, Ding F, Ramachandran S, Dokholyan NV, Gaia: automated quality assessment of protein structure models. Bioinformatics. 2011;27: 2209–2215. doi: 10.1093/bioinformatics/btr374 21700672
    • (2011) Bioinformatics , vol.27 , pp. 2209-2215
    • Kota, P.1    Ding, F.2    Ramachandran, S.3    Dokholyan, N.V.4
  • 62
    • 1942455272 scopus 로고    scopus 로고
    • Generalized-ensemble algorithms: enhanced sampling techniques for Monte Carlo and molecular dynamics simulations
    • Okamoto Y, Generalized-ensemble algorithms: enhanced sampling techniques for Monte Carlo and molecular dynamics simulations. J Mol Graph Model. 2004;22: 425–439. doi: 10.1016/j.jmgm.2003.12.009 15099838
    • (2004) J Mol Graph Model , vol.22 , pp. 425-439
    • Okamoto, Y.1
  • 63
    • 0035909921 scopus 로고    scopus 로고
    • The free energy landscape for beta hairpin folding in explicit water
    • Zhou R, Berne BJ, Germain R, The free energy landscape for beta hairpin folding in explicit water. Proc Natl Acad Sci USA. National Acad Sciences; 2001;98: 14931–14936. doi: 10.1073/pnas.201543998 11752441
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14931-14936
    • Zhou, R.1    Berne, B.J.2    Germain, R.3
  • 64
    • 33947398571 scopus 로고    scopus 로고
    • Use of the weighted histogram analysis method for the analysis of simulated and parallel tempering simulations
    • Chodera JD, Swope WC, Pitera JW, Seok C, Dill KA, Use of the weighted histogram analysis method for the analysis of simulated and parallel tempering simulations. Journal of Chemical Theory and Computation. 2007;3: 26–41. doi: 10.1021/ct0502864
    • (2007) Journal of Chemical Theory and Computation , vol.3 , pp. 26-41
    • Chodera, J.D.1    Swope, W.C.2    Pitera, J.W.3    Seok, C.4    Dill, K.A.5
  • 65
    • 84946024314 scopus 로고    scopus 로고
    • Gyimesi G. PyWHAM [Internet]. Available: http://www.hegelab.org/databases.html
  • 66
    • 84875592758 scopus 로고    scopus 로고
    • GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit
    • Pronk S, Páll S, Schulz R, Larsson P, Bjelkmar P, Apostolov R, et al. GROMACS 4.5: a high-throughput and highly parallel open source molecular simulation toolkit. Bioinformatics. 2013;29: 845–854. doi: 10.1093/bioinformatics/btt055 23407358
    • (2013) Bioinformatics , vol.29 , pp. 845-854
    • Pronk, S.1    Páll, S.2    Schulz, R.3    Larsson, P.4    Bjelkmar, P.5    Apostolov, R.6
  • 67
    • 35748935079 scopus 로고    scopus 로고
    • Wordom: a program for efficient analysis of molecular dynamics simulations
    • Seeber M, Cecchini M, Rao F, Settanni G, Caflisch A, Wordom: a program for efficient analysis of molecular dynamics simulations. Bioinformatics. 2007;23: 2625–2627. doi: 10.1093/bioinformatics/btm378 17717034
    • (2007) Bioinformatics , vol.23 , pp. 2625-2627
    • Seeber, M.1    Cecchini, M.2    Rao, F.3    Settanni, G.4    Caflisch, A.5
  • 68
    • 79952498871 scopus 로고    scopus 로고
    • Wordom: a user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces
    • Seeber M, Felline A, Raimondi F, Muff S, Friedman R, Rao F, et al. Wordom: a user-friendly program for the analysis of molecular structures, trajectories, and free energy surfaces. J Comput Chem. 2011;32: 1183–1194. doi: 10.1002/jcc.21688 21387345
    • (2011) J Comput Chem , vol.32 , pp. 1183-1194
    • Seeber, M.1    Felline, A.2    Raimondi, F.3    Muff, S.4    Friedman, R.5    Rao, F.6


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