메뉴 건너뛰기




Volumn 105, Issue 10, 2013, Pages 2323-2332

Membrane permeation induced by aggregates of human islet amyloid polypeptides

Author keywords

[No Author keywords available]

Indexed keywords

1,2 DIPALMITOYLPHOSPHATIDYLGLYCEROL; 1,2-DIPALMITOYLPHOSPHATIDYLGLYCEROL; AMYLIN; PHOSPHATIDYLGLYCEROL;

EID: 84887879948     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.09.045     Document Type: Article
Times cited : (37)

References (80)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • D.M. Walsh, and I. Klyubin D.J. Selkoe Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo Nature 416 2002 535 539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Selkoe, D.J.3
  • 3
    • 0036708168 scopus 로고    scopus 로고
    • Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies
    • M.D. Kirkitadze, G. Bitan, and D.B. Teplow Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies J. Neurosci. Res. 69 2002 567 577
    • (2002) J. Neurosci. Res. , vol.69 , pp. 567-577
    • Kirkitadze, M.D.1    Bitan, G.2    Teplow, D.B.3
  • 4
    • 0037041420 scopus 로고    scopus 로고
    • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
    • M. Bucciantini, and E. Giannoni M. Stefani Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases Nature 416 2002 507 511
    • (2002) Nature , vol.416 , pp. 507-511
    • Bucciantini, M.1    Giannoni, E.2    Stefani, M.3
  • 5
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease
    • W.L. Klein, W.B. Stine Jr., and D.B. Teplow Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease Neurobiol. Aging 25 2004 569 580
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine, Jr.W.B.2    Teplow, D.B.3
  • 6
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic protein-membrane interactions: Mechanistic insight from model systems
    • S.M. Butterfield, and H.A. Lashuel Amyloidogenic protein-membrane interactions: mechanistic insight from model systems Angew. Chem. Int. Ed. Engl. 49 2010 5628 5654
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 7
    • 78049290389 scopus 로고    scopus 로고
    • Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity
    • M. Stefani Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity FEBS J. 277 2010 4602 4613
    • (2010) FEBS J. , vol.277 , pp. 4602-4613
    • Stefani, M.1
  • 8
    • 80053589341 scopus 로고    scopus 로고
    • Membrane and surface interactions of Alzheimer's Aβ peptide - Insights into the mechanism of cytotoxicity
    • T.L. Williams, and L.C. Serpell Membrane and surface interactions of Alzheimer's Aβ peptide - insights into the mechanism of cytotoxicity FEBS J. 278 2011 3905 3917
    • (2011) FEBS J. , vol.278 , pp. 3905-3917
    • Williams, T.L.1    Serpell, L.C.2
  • 9
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • J. Janson, and R.H. Ashley P.C. Butler The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles Diabetes 48 1999 491 498
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Butler, P.C.3
  • 10
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • M. Anguiano, R.J. Nowak, and P.T. Lansbury Jr. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes Biochemistry 41 2002 11338 11343
    • (2002) Biochemistry , vol.41 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury, Jr.P.T.3
  • 11
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
    • Y. Porat, and S. Kolusheva E. Gazit The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies Biochemistry 42 2003 10971 10977
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Gazit, E.3
  • 12
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • R. Kayed, and Y. Sokolov C.G. Glabe Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases J. Biol. Chem. 279 2004 46363 46366
    • (2004) J. Biol. Chem. , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Glabe, C.G.3
  • 13
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • A. Demuro, and E. Mina C.G. Glabe 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    Glabe, C.G.3
  • 14
    • 33847012626 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets
    • R.A. Ritzel, and J.J. Meier P.C. Butler Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets Diabetes 56 2007 65 71
    • (2007) Diabetes , vol.56 , pp. 65-71
    • Ritzel, R.A.1    Meier, J.J.2    Butler, P.C.3
  • 15
    • 0024213009 scopus 로고
    • Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: Quantitative changes in the pancreas in type 2 diabetes
    • A. Clark, and C.A. Wells R.C. Turner Islet amyloid, increased A-cells, reduced B-cells and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes Diabetes Res. 9 1988 151 159
    • (1988) Diabetes Res. , vol.9 , pp. 151-159
    • Clark, A.1    Wells, C.A.2    Turner, R.C.3
  • 16
    • 4043171124 scopus 로고    scopus 로고
    • Islet amyloid: A critical entity in the pathogenesis of type 2 diabetes
    • R.L. Hull, and G.T. Westermark S.E. Kahn Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes J. Clin. Endocrinol. Metab. 89 2004 3629 3643
    • (2004) J. Clin. Endocrinol. Metab. , vol.89 , pp. 3629-3643
    • Hull, R.L.1    Westermark, G.T.2    Kahn, S.E.3
  • 17
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • S.E. Kahn, S. Andrikopoulos, and C.B. Verchere Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes Diabetes 48 1999 241 253
    • (1999) Diabetes , vol.48 , pp. 241-253
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 18
    • 0028307637 scopus 로고
    • Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice
    • J.W. Höppener, and C. Oosterwijk C.J. Lips Molecular physiology of the islet amyloid polypeptide (IAPP)/amylin gene in man, rat, and transgenic mice J. Cell. Biochem. 55 Suppl 1994 39 53
    • (1994) J. Cell. Biochem. , vol.55 , Issue.SUPPL. , pp. 39-53
    • Höppener, J.W.1    Oosterwijk, C.2    Lips, C.J.3
  • 19
    • 0025302287 scopus 로고
    • Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells
    • S.E. Kahn, and D.A. D'Alessio D. Porte Jr. Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells Diabetes 39 1990 634 638
    • (1990) Diabetes , vol.39 , pp. 634-638
    • Kahn, S.E.1    D'Alessio, D.A.2    Porte, Jr.D.3
  • 20
    • 36749033116 scopus 로고    scopus 로고
    • Peptide conformation and supramolecular organization in amylin fibrils: Constraints from solid-state NMR
    • S. Luca, and W.M. Yau R. Tycko Peptide conformation and supramolecular organization in amylin fibrils: constraints from solid-state NMR Biochemistry 46 2007 13505 13522
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Tycko, R.3
  • 21
    • 9144267018 scopus 로고    scopus 로고
    • Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling
    • S.A. Jayasinghe, and R. Langen Identifying structural features of fibrillar islet amyloid polypeptide using site-directed spin labeling J. Biol. Chem. 279 2004 48420 48425
    • (2004) J. Biol. Chem. , vol.279 , pp. 48420-48425
    • Jayasinghe, S.A.1    Langen, R.2
  • 22
    • 36049013172 scopus 로고    scopus 로고
    • Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy
    • D.H.J. Lopes, and A. Meister R. Winter Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy Biophys. J. 93 2007 3132 3141
    • (2007) Biophys. J. , vol.93 , pp. 3132-3141
    • Lopes, D.H.J.1    Meister, A.2    Winter, R.3
  • 23
    • 0025366838 scopus 로고
    • Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation
    • P. Westermark, and U. Engström C. Betsholtz Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation Proc. Natl. Acad. Sci. USA 87 1990 5036 5040
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5036-5040
    • Westermark, P.1    Engström, U.2    Betsholtz, C.3
  • 24
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • E.T. Jaikaran, and C.E. Higham P.E. Fraser Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis J. Mol. Biol. 308 2001 515 525
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Fraser, P.E.3
  • 25
    • 24644502612 scopus 로고    scopus 로고
    • Lipid membranes modulate the structure of islet amyloid polypeptide
    • S.A. Jayasinghe, and R. Langen Lipid membranes modulate the structure of islet amyloid polypeptide Biochemistry 44 2005 12113 12119
    • (2005) Biochemistry , vol.44 , pp. 12113-12119
    • Jayasinghe, S.A.1    Langen, R.2
  • 26
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • J.D. Knight, and A.D. Miranker Phospholipid catalysis of diabetic amyloid assembly J. Mol. Biol. 341 2004 1175 1187
    • (2004) J. Mol. Biol. , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 27
    • 33747119677 scopus 로고    scopus 로고
    • Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide
    • J.D. Knight, J.A. Hebda, and A.D. Miranker Conserved and cooperative assembly of membrane-bound alpha-helical states of islet amyloid polypeptide Biochemistry 45 2006 9496 9508
    • (2006) Biochemistry , vol.45 , pp. 9496-9508
    • Knight, J.D.1    Hebda, J.A.2    Miranker, A.D.3
  • 28
    • 7544245555 scopus 로고    scopus 로고
    • Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers
    • E. Sparr, and M.F.M. Engel J.A. Killian Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers FEBS Lett. 577 2004 117 120
    • (2004) FEBS Lett. , vol.577 , pp. 117-120
    • Sparr, E.1    Engel, M.F.M.2    Killian, J.A.3
  • 29
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • A. Quist, and I. Doudevski R. Lal Amyloid ion channels: a common structural link for protein-misfolding disease Proc. Natl. Acad. Sci. USA 102 2005 10427 10432
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lal, R.3
  • 30
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • T.A. Mirzabekov, M.C. Lin, and B.L. Kagan Pore formation by the cytotoxic islet amyloid peptide amylin J. Biol. Chem. 271 1996 1988 1992
    • (1996) J. Biol. Chem. , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 31
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • A. Lorenzo, and B. Razzaboni B.A. Yankner Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus Nature 368 1994 756 760
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Yankner, B.A.3
  • 32
    • 0029126786 scopus 로고
    • Human islet amyloid polypeptide expression in COS-1 cells. A model of intracellular amyloidogenesis
    • T.D. O'Brien, and P.C. Butler N.L. Eberhardt Human islet amyloid polypeptide expression in COS-1 cells. A model of intracellular amyloidogenesis Am. J. Pathol. 147 1995 609 616
    • (1995) Am. J. Pathol. , vol.147 , pp. 609-616
    • O'Brien, T.D.1    Butler, P.C.2    Eberhardt, N.L.3
  • 33
    • 0032932422 scopus 로고    scopus 로고
    • Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cells
    • H.J. Hiddinga, and N.L. Eberhardt Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cells Am. J. Pathol. 154 1999 1077 1088
    • (1999) Am. J. Pathol. , vol.154 , pp. 1077-1088
    • Hiddinga, H.J.1    Eberhardt, N.L.2
  • 34
    • 84887954328 scopus 로고    scopus 로고
    • Reference deleted in proof.
    • Reference deleted in proof.
  • 35
    • 31344478495 scopus 로고    scopus 로고
    • Islet amyloid polypeptide inserts into phospholipid monolayers as monomer
    • M.F.M. Engel, and H. Yigittop J. Antoinette Killian Islet amyloid polypeptide inserts into phospholipid monolayers as monomer J. Mol. Biol. 356 2006 783 789
    • (2006) J. Mol. Biol. , vol.356 , pp. 783-789
    • Engel, M.F.M.1    Yigittop, H.2    Antoinette Killian, J.3
  • 36
    • 57049086457 scopus 로고    scopus 로고
    • A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity
    • J.R. Brender, and K. Hartman A. Ramamoorthy A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity Biochemistry 47 2008 12680 12688
    • (2008) Biochemistry , vol.47 , pp. 12680-12688
    • Brender, J.R.1    Hartman, K.2    Ramamoorthy, A.3
  • 37
    • 84887959484 scopus 로고    scopus 로고
    • Reference deleted in proof.
    • Reference deleted in proof.
  • 38
    • 84861707850 scopus 로고    scopus 로고
    • Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations
    • Y. Zhang, and Y. Luo G. Wei Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations PLoS ONE 7 2012 e38191
    • (2012) PLoS ONE , vol.7 , pp. 38191
    • Zhang, Y.1    Luo, Y.2    Wei, G.3
  • 39
    • 84868316813 scopus 로고    scopus 로고
    • Conformations of islet amyloid polypeptide monomers in a membrane environment: Implications for fibril formation
    • M. Duan, J. Fan, and S. Huo Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation PLoS ONE 7 2012 e47150
    • (2012) PLoS ONE , vol.7 , pp. 47150
    • Duan, M.1    Fan, J.2    Huo, S.3
  • 40
    • 84865652060 scopus 로고    scopus 로고
    • Probing ion channel activity of human islet amyloid polypeptide (amylin)
    • J. Zhao, and Y. Luo J. Zheng Probing ion channel activity of human islet amyloid polypeptide (amylin) Biochim. Biophys. Acta 1818 2012 3121 3130
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 3121-3130
    • Zhao, J.1    Luo, Y.2    Zheng, J.3
  • 41
    • 84864287221 scopus 로고    scopus 로고
    • Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces
    • D. Xiao, and L. Fu E.C. Yan Amphiphilic adsorption of human islet amyloid polypeptide aggregates to lipid/aqueous interfaces J. Mol. Biol. 421 2012 537 547
    • (2012) J. Mol. Biol. , vol.421 , pp. 537-547
    • Xiao, D.1    Fu, L.2    Yan, E.C.3
  • 42
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: The GROMOS force-field parameter sets 53A5 and 53A6
    • C. Oostenbrink, and A. Villa W.F. van Gunsteren A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6 J. Comput. Chem. 25 2004 1656 1676
    • (2004) J. Comput. Chem. , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Van Gunsteren, W.F.3
  • 43
    • 28444442999 scopus 로고    scopus 로고
    • 3D structure of Alzheimer's amyloid-β(1-42) fibrils
    • T. Lührs, and C. Ritter R. Riek 3D structure of Alzheimer's amyloid-β(1-42) fibrils Proc. Natl. Acad. Sci. USA 102 2005 17342 17347
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17342-17347
    • Lührs, T.1    Ritter, C.2    Riek, R.3
  • 44
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils
    • A.T. Petkova, W.M. Yau, and R. Tycko Experimental constraints on quaternary structure in Alzheimer's β-amyloid fibrils Biochemistry 45 2006 498 512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 45
    • 0037195098 scopus 로고    scopus 로고
    • Stabilities and conformations of Alzheimer's β -amyloid peptide oligomers (Abeta (16-22), Abeta (16-35), and Abeta (10-35)): Sequence effects
    • B. Ma, and R. Nussinov Stabilities and conformations of Alzheimer's β -amyloid peptide oligomers (Abeta (16-22), Abeta (16-35), and Abeta (10-35)): Sequence effects Proc. Natl. Acad. Sci. USA 99 2002 14126 14131
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14126-14131
    • Ma, B.1    Nussinov, R.2
  • 46
    • 0033856165 scopus 로고    scopus 로고
    • Amyloid fibril formation from full-length and fragments of amylin
    • C. Goldsbury, and K. Goldie U. Aebi Amyloid fibril formation from full-length and fragments of amylin J. Struct. Biol. 130 2000 352 362
    • (2000) J. Struct. Biol. , vol.130 , pp. 352-362
    • Goldsbury, C.1    Goldie, K.2    Aebi, U.3
  • 47
    • 57349120654 scopus 로고    scopus 로고
    • Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction
    • J. Madine, and E. Jack D.A. Middleton Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction J. Am. Chem. Soc. 130 2008 14990 15001
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Middleton, D.A.3
  • 48
    • 80855139866 scopus 로고    scopus 로고
    • Electroporation of the E. Coli and S. Aureus membranes: Molecular dynamics simulations of complex bacterial membranes
    • T.J. Piggot, D.A. Holdbrook, and S. Khalid Electroporation of the E. coli and S. Aureus membranes: molecular dynamics simulations of complex bacterial membranes J. Phys. Chem. B 115 2011 13381 13388
    • (2011) J. Phys. Chem. B , vol.115 , pp. 13381-13388
    • Piggot, T.J.1    Holdbrook, D.A.2    Khalid, S.3
  • 49
    • 0036212690 scopus 로고    scopus 로고
    • Simulations of zwitterionic and anionic phospholipid monolayers
    • Y.N. Kaznessis, S. Kim, and R.G. Larson Simulations of zwitterionic and anionic phospholipid monolayers Biophys. J. 82 2002 1731 1742
    • (2002) Biophys. J. , vol.82 , pp. 1731-1742
    • Kaznessis, Y.N.1    Kim, S.2    Larson, R.G.3
  • 50
    • 22244486627 scopus 로고    scopus 로고
    • Molecular dynamics simulations and 2H NMR study of the GalCer/DPPG lipid bilayer
    • T. Zaraiskaya, and K.R. Jeffrey Molecular dynamics simulations and 2H NMR study of the GalCer/DPPG lipid bilayer Biophys. J. 88 2005 4017 4031
    • (2005) Biophys. J. , vol.88 , pp. 4017-4031
    • Zaraiskaya, T.1    Jeffrey, K.R.2
  • 51
    • 58749103337 scopus 로고    scopus 로고
    • Membrane thickening by the antimicrobial peptide PGLa
    • G. Pabst, and S.L. Grage A. Hickel Membrane thickening by the antimicrobial peptide PGLa Biophys. J. 95 2008 5779 5788
    • (2008) Biophys. J. , vol.95 , pp. 5779-5788
    • Pabst, G.1    Grage, S.L.2    Hickel, A.3
  • 52
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • B. Hess, and C. Kutzner E. Lindahl GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 4 2008 435 447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 53
    • 33947139278 scopus 로고    scopus 로고
    • Setting up and running molecular dynamics simulations of membrane proteins
    • C. Kandt, W.L. Ash, and D.P. Tieleman Setting up and running molecular dynamics simulations of membrane proteins Methods 41 2007 475 488
    • (2007) Methods , vol.41 , pp. 475-488
    • Kandt, C.1    Ash, W.L.2    Tieleman, D.P.3
  • 54
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 55
    • 0033556236 scopus 로고    scopus 로고
    • Peptide folding: When simulation meets experiment
    • X. Daura, and K. Gademann A. Mark Peptide folding: when simulation meets experiment Angew. Chem. Int. Ed. 38 1999 236 240
    • (1999) Angew. Chem. Int. Ed. , vol.38 , pp. 236-240
    • Daura, X.1    Gademann, K.2    Mark, A.3
  • 56
    • 33748573642 scopus 로고    scopus 로고
    • The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores
    • O. Beckstein, and M.S.P. Sansom The influence of geometry, surface character, and flexibility on the permeation of ions and water through biological pores Phys. Biol. 1 2004 42 52
    • (2004) Phys. Biol. , vol.1 , pp. 42-52
    • Beckstein, O.1    Sansom, M.S.P.2
  • 57
    • 65549083717 scopus 로고    scopus 로고
    • GridMAT-MD: A grid-based membrane analysis tool for use with molecular dynamics
    • W.J. Allen, J.A. Lemkul, and D.R. Bevan GridMAT-MD: a grid-based membrane analysis tool for use with molecular dynamics J. Comput. Chem. 30 2009 1952 1958
    • (2009) J. Comput. Chem. , vol.30 , pp. 1952-1958
    • Allen, W.J.1    Lemkul, J.A.2    Bevan, D.R.3
  • 58
    • 61449455404 scopus 로고    scopus 로고
    • Dynamics and energetics of permeation through aquaporins. What do we learn from molecular dynamics simulations?
    • E. Beitz, Springer Berlin
    • J.S. Hub, H. Grubmüller, and B.L. de Groot Dynamics and energetics of permeation through aquaporins. What do we learn from molecular dynamics simulations? E. Beitz, Aquaporins, Vol. 190, Handbook of Experimental Pharmacology 2009 Springer Berlin 57 76
    • (2009) Aquaporins, Vol. 190, Handbook of Experimental Pharmacology , pp. 57-76
    • Hub, J.S.1    Grubmüller, H.2    De Groot, B.L.3
  • 59
    • 77957110065 scopus 로고    scopus 로고
    • Potentials of mean force and permeabilities for carbon dioxide, ammonia, and water flux across a Rhesus protein channel and lipid membranes
    • J.S. Hub, and F.K. Winkler B.L. de Groot Potentials of mean force and permeabilities for carbon dioxide, ammonia, and water flux across a Rhesus protein channel and lipid membranes J. Am. Chem. Soc. 132 2010 13251 13263
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13251-13263
    • Hub, J.S.1    Winkler, F.K.2    De Groot, B.L.3
  • 60
    • 73649113467 scopus 로고    scopus 로고
    • Analysis of anisotropic local field in sum frequency generation spectroscopy with the charge response kernel water model
    • T. Ishiyama, and A. Morita Analysis of anisotropic local field in sum frequency generation spectroscopy with the charge response kernel water model J. Chem. Phys. 131 2009 244714
    • (2009) J. Chem. Phys. , vol.131 , pp. 244714
    • Ishiyama, T.1    Morita, A.2
  • 61
    • 77952043061 scopus 로고    scopus 로고
    • Vibrational sum-frequency generation spectroscopy at the water/lipid interface: Molecular dynamics simulation study
    • Y. Nagata, and S. Mukamel Vibrational sum-frequency generation spectroscopy at the water/lipid interface: molecular dynamics simulation study J. Am. Chem. Soc. 132 2010 6434 6442
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6434-6442
    • Nagata, Y.1    Mukamel, S.2
  • 62
    • 79961051077 scopus 로고    scopus 로고
    • Interpretation of the water surface vibrational sum-frequency spectrum
    • P.A. Pieniazek, C.J. Tainter, and J.L. Skinner Interpretation of the water surface vibrational sum-frequency spectrum J. Chem. Phys. 135 2011 044701
    • (2011) J. Chem. Phys. , vol.135 , pp. 044701
    • Pieniazek, P.A.1    Tainter, C.J.2    Skinner, J.L.3
  • 63
    • 1642327373 scopus 로고    scopus 로고
    • A unified treatment of selection rules and symmetry relations for sum-frequency and second harmonic spectroscopies
    • A.J. Moad, and G.J. Simpson A unified treatment of selection rules and symmetry relations for sum-frequency and second harmonic spectroscopies J. Phys. Chem. B 108 2004 3548 3562
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3548-3562
    • Moad, A.J.1    Simpson, G.J.2
  • 65
    • 84869868315 scopus 로고    scopus 로고
    • How the amyloid-β peptide and membranes affect each other: An extensive simulation study
    • C. Poojari, A. Kukol, and B. Strodel How the amyloid-β peptide and membranes affect each other: an extensive simulation study Biochim. Biophys. Acta. (Biomembr.) 1828 2013 327 339
    • (2013) Biochim. Biophys. Acta. (Biomembr.) , vol.1828 , pp. 327-339
    • Poojari, C.1    Kukol, A.2    Strodel, B.3
  • 66
    • 84887897788 scopus 로고    scopus 로고
    • Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations
    • In press
    • P. Poojari, and B. Strodel Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations PLoS ONE 2013 In press
    • (2013) PLoS ONE
    • Poojari, P.1    Strodel, B.2
  • 67
    • 84863289390 scopus 로고    scopus 로고
    • How type II diabetes-related islet amyloid polypeptide damages lipid bilayers
    • C.-C. Lee, Y. Sun, and H.W. Huang How type II diabetes-related islet amyloid polypeptide damages lipid bilayers Biophys. J. 102 2012 1059 1068
    • (2012) Biophys. J. , vol.102 , pp. 1059-1068
    • Lee, C.-C.1    Sun, Y.2    Huang, H.W.3
  • 68
    • 84255160660 scopus 로고    scopus 로고
    • Cholesterol effect on water permeability through DPPC and PSM lipid bilayers: A molecular dynamics study
    • H. Saito, and W. Shinoda Cholesterol effect on water permeability through DPPC and PSM lipid bilayers: a molecular dynamics study J. Phys. Chem. B 115 2011 15241 15250
    • (2011) J. Phys. Chem. B , vol.115 , pp. 15241-15250
    • Saito, H.1    Shinoda, W.2
  • 69
    • 38949167084 scopus 로고    scopus 로고
    • New structures help the modeling of toxic amyloidbeta ion channels
    • H. Jang, and J. Zheng R. Nussinov New structures help the modeling of toxic amyloidbeta ion channels Trends Biochem. Sci. 33 2008 91 100
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 91-100
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 70
    • 34548788549 scopus 로고    scopus 로고
    • Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process
    • H. Jang, J. Zheng, and R. Nussinov Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process Biophys. J. 93 2007 1938 1949
    • (2007) Biophys. J. , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 71
    • 72549099399 scopus 로고    scopus 로고
    • Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channels
    • H. Jang, and F.T. Arce R. Nussinov Misfolded amyloid ion channels present mobile beta-sheet subunits in contrast to conventional ion channels Biophys. J. 97 2009 3029 3037
    • (2009) Biophys. J. , vol.97 , pp. 3029-3037
    • Jang, H.1    Arce, F.T.2    Nussinov, R.3
  • 72
    • 79959651424 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link
    • H. Jang, and F.T. Arce R. Lal Antimicrobial protegrin-1 forms amyloid-like fibrils with rapid kinetics suggesting a functional link Biophys. J. 100 2011 1775 1783
    • (2011) Biophys. J. , vol.100 , pp. 1775-1783
    • Jang, H.1    Arce, F.T.2    Lal, R.3
  • 73
    • 84856262919 scopus 로고    scopus 로고
    • Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions
    • R. Capone, and H. Jang R. Lal Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions Biochemistry 51 2012 776 785
    • (2012) Biochemistry , vol.51 , pp. 776-785
    • Capone, R.1    Jang, H.2    Lal, R.3
  • 74
    • 79957527414 scopus 로고    scopus 로고
    • Polymorphism of amyloid β peptide in different environments: Implications for membrane insertion and pore formation
    • F.T. Arce, and H. Jang R. Lal Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation Soft Matter 7 2011 5267 5273
    • (2011) Soft Matter , vol.7 , pp. 5267-5273
    • Arce, F.T.1    Jang, H.2    Lal, R.3
  • 75
    • 84858308911 scopus 로고    scopus 로고
    • All-D-enantiomer of β-amyloid peptide forms ion channels in lipid bilayers
    • R. Capone, and H. Jang R. Lal All-D-enantiomer of β-amyloid peptide forms ion channels in lipid bilayers J. Chem. Theory Comput. 8 2012 1143 1152
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1143-1152
    • Capone, R.1    Jang, H.2    Lal, R.3
  • 76
    • 84856298593 scopus 로고    scopus 로고
    • Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: Relevance to the ion channel mechanism of AD pathology
    • L. Connelly, and H. Jang R. Lal Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology J. Phys. Chem. B 116 2012 1728 1735
    • (2012) J. Phys. Chem. B , vol.116 , pp. 1728-1735
    • Connelly, L.1    Jang, H.2    Lal, R.3
  • 77
    • 77957105623 scopus 로고    scopus 로고
    • Transmembrane structures for Alzheimer's Aβ(1-42) oligomers
    • B. Strodel, and J.W. Lee D.J. Wales Transmembrane structures for Alzheimer's Aβ(1-42) oligomers J. Am. Chem. Soc. 132 2010 13300 13312
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13300-13312
    • Strodel, B.1    Lee, J.W.2    Wales, D.J.3
  • 78
    • 77955654930 scopus 로고    scopus 로고
    • The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes
    • L. Khemtémourian, and M.F. Engel J.A. Killian The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes Eur. Biophys. J. 39 2010 1359 1364
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1359-1364
    • Khemtémourian, L.1    Engel, M.F.2    Killian, J.A.3
  • 79
    • 69949118458 scopus 로고    scopus 로고
    • PACKMOL: A package for building initial configurations for molecular dynamics simulations
    • L. Martínez, and R. Andrade J.M. Martínez PACKMOL: a package for building initial configurations for molecular dynamics simulations J. Comput. Chem. 30 2009 2157 2164
    • (2009) J. Comput. Chem. , vol.30 , pp. 2157-2164
    • Martínez, L.1    Andrade, R.2    Martínez, J.M.3
  • 80
    • 36449007043 scopus 로고
    • Computer simulation of liquid/liquid interfaces. II. Surface tension-area dependence of a bilayer and monolayer
    • S.E. Feller, Y. Zhang, and R.W. Pastor Computer simulation of liquid/liquid interfaces. II. Surface tension-area dependence of a bilayer and monolayer J. Chem. Phys. 103 1995 10267 10276
    • (1995) J. Chem. Phys. , vol.103 , pp. 10267-10276
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.