메뉴 건너뛰기




Volumn 5, Issue 4, 2009, Pages

Amyloidogenesis Abolished by Proline Substitutions but Enhanced by Lipid Binding

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; HYDROPHOBICITY; MOLECULAR DYNAMICS; MOLECULES; RATS; SELF ASSEMBLY;

EID: 66249130413     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1000357     Document Type: Article
Times cited : (37)

References (87)
  • 3
    • 0033771793 scopus 로고    scopus 로고
    • Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?
    • Goldberg MS, Lansbury PT Jr (2000) Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? Nature Cell Biology 2: E115-119.
    • (2000) Nature Cell Biology , vol.2
    • Goldberg, M.S.1    Lansbury Jr, P.T.2
  • 4
    • 66349136559 scopus 로고    scopus 로고
    • Lipid Molecule Enhances Aggregation of hIAPP PLoS Computational Biology | www.ploscompbiol.org 12 April 2009 | 5 | Issue 4 | e1000357
    • Lipid Molecule Enhances Aggregation of hIAPP PLoS Computational Biology | www.ploscompbiol.org 12 April 2009 | Volume 5 | Issue 4 | e1000357
  • 5
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, et al. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci U S A 84: 8628-8632.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8628-8632
    • Cooper, G.J.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5
  • 6
    • 0024307842 scopus 로고
    • Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets
    • Lukinius A, Wilander E, Westermark GT, Engström U, Westermark P (1989) Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets. Diabetologia 32: 240-244.
    • (1989) Diabetologia , vol.32 , pp. 240-244
    • Lukinius, A.1    Wilander, E.2    Westermark, G.T.3    Engström, U.4    Westermark, P.5
  • 7
    • 0024413349 scopus 로고
    • Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects
    • Clark A, Edwards CA, Ostle LR, Sutton R, Rothbard JB, et al. (1989) Localisation of islet amyloid peptide in lipofuscin bodies and secretory granules of human B-cells and in islets of type-2 diabetic subjects. Cell and Tissue Research 257: 179-185.
    • (1989) Cell and Tissue Research , vol.257 , pp. 179-185
    • Clark, A.1    Edwards, C.A.2    Ostle, L.R.3    Sutton, R.4    Rothbard, J.B.5
  • 8
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid [beta] protein potently inhibit hippocampal long- term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV, Cullen WK, Anwyl R, et al. (2002) Naturally secreted oligomers of amyloid [beta] protein potently inhibit hippocampal long- term potentiation in vivo. Nature 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3    Cullen, W.K.4    Anwyl, R.5
  • 9
    • 0242668337 scopus 로고    scopus 로고
    • Common Structure of Soluble Amyloid Oligomers Implies Common Mecha- nism of Pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common Structure of Soluble Amyloid Oligomers Implies Common Mecha- nism 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
  • 10
    • 43949107500 scopus 로고    scopus 로고
    • Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide
    • Brender JR, Lee EL, Cavitt MA, Gafni A, Steel DG, et al. (2008) Amyloid Fiber Formation and Membrane Disruption are Separate Processes Localized in Two Distinct Regions of IAPP, the Type-2-Diabetes-Related Peptide. Journal of the American Chemical Society 130: 6424-6429.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 6424-6429
    • Brender, J.R.1    Lee, E.L.2    Cavitt, M.A.3    Gafni, A.4    Steel, D.G.5
  • 11
    • 4143094106 scopus 로고    scopus 로고
    • Phospholipid catalysis of diabetic amyloid assembly
    • Knight JD, Miranker AD (2004) Phospholipid catalysis of diabetic amyloid assembly. Journal of Molecular Biology 341: 1175-1187.
    • (2004) Journal of Molecular Biology , vol.341 , pp. 1175-1187
    • Knight, J.D.1    Miranker, A.D.2
  • 12
    • 50149121327 scopus 로고    scopus 로고
    • Calcium-activated membrane interaction of the islet amyloid polypeptide: Implications in the pathogenesis of type II diabetes mellitus
    • Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C (2008) Calcium-activated membrane interaction of the islet amyloid polypeptide: Implications in the pathogenesis of type II diabetes mellitus. Archives of Biochemistry and Biophysics 477: 291-298.
    • (2008) Archives of Biochemistry and Biophysics , vol.477 , pp. 291-298
    • Sciacca, M.F.M.1    Pappalardo, M.2    Milardi, D.3    Grasso, D.M.4    La Rosa, C.5
  • 13
    • 43149118349 scopus 로고    scopus 로고
    • Engel MFM, Khemtemourian L, Kleijer CC, Meeldijk HJD, Jacobs J, et al. (2008) Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proceedings of the National Academy of Sciences: 0708354105.
    • Engel MFM, Khemtemourian L, Kleijer CC, Meeldijk HJD, Jacobs J, et al. (2008) Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proceedings of the National Academy of Sciences: 0708354105.
  • 14
    • 57049086457 scopus 로고    scopus 로고
    • A Single Mutation in the Nonamyloidogenic Region of Islet Amyloid Polypeptide Greatly Reduces Toxicity
    • Brender JR, Hartman K, Reid KR, Kennedy RT, Ramamoorthy A (2008) A Single Mutation in the Nonamyloidogenic Region of Islet Amyloid Polypeptide Greatly Reduces Toxicity. Biochemistry 47: 12680-12688.
    • (2008) Biochemistry , vol.47 , pp. 12680-12688
    • Brender, J.R.1    Hartman, K.2    Reid, K.R.3    Kennedy, R.T.4    Ramamoorthy, A.5
  • 15
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • Brender JR, Durr UHN, Heyl D, Budarapu MB, Ramamoorthy A (2007) Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. Biochimica Et Biophysica Acta-Biomembranes 1768: 2026-2029.
    • (2007) Biochimica Et Biophysica Acta-Biomembranes 1768 , pp. 2026-2029
    • Brender, J.R.1    Durr, U.H.N.2    Heyl, D.3    Budarapu, M.B.4    Ramamoorthy, A.5
  • 16
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegen- erative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T, Lansbury PT (2002) Neurodegen- erative disease: Amyloid pores from pathogenic mutations. Nature 418: 291-291.
    • (2002) Nature , vol.418 , pp. 291-291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 19
    • 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
    • Jang H, Zheng J, Nussinov R (2007) Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process. Biophysical Journal 93: 1938-1949.
    • (2007) Biophysical Journal , vol.93 , pp. 1938-1949
    • Jang, H.1    Zheng, J.2    Nussinov, R.3
  • 20
    • 0014088274 scopus 로고
    • The lipid content of amyloid fibrils purified by a variety of methods
    • Kim IC, Shirahama T, Cohen AS (1967) The 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
    • Kim, I.C.1    Shirahama, T.2    Cohen, A.S.3
  • 22
    • 0031843985 scopus 로고    scopus 로고
    • Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry
    • Klein TR, Kirsch D, Kaufmann R, Riesner D (1998) Prion rods contain small amounts of two host sphingolipids as revealed by thin-layer chromatography and mass spectrometry. Biological Chemistry 379: 655-666.
    • (1998) Biological Chemistry , vol.379 , pp. 655-666
    • Klein, T.R.1    Kirsch, D.2    Kaufmann, R.3    Riesner, D.4
  • 24
    • 52949132646 scopus 로고    scopus 로고
    • Interaction of membrane- bound islet amyloid polypeptide with soluble and crystalline insulin
    • Knight JD, Williamson JA, Miranker AD (2008) Interaction of membrane- bound islet amyloid polypeptide with soluble and crystalline insulin. Protein Science 17: 1850-1856.
    • (2008) Protein Science , vol.17 , pp. 1850-1856
    • Knight, J.D.1    Williamson, J.A.2    Miranker, A.D.3
  • 25
    • 47749117154 scopus 로고    scopus 로고
    • Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding
    • Apostolidou M, Jayasinghe SA, Langen R (2008) Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. Journal of Biological Chemistry 283: 17205-17210.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 17205-17210
    • Apostolidou, M.1    Jayasinghe, S.A.2    Langen, R.3
  • 26
    • 38049072191 scopus 로고    scopus 로고
    • Islet Amyloid Polypeptide Forms Rigid Lipid-Protein Amyloid Fibrils on Supported Phospholipid Bilayers
    • Domanov YA, Kinnunen PKJ (2008) Islet Amyloid Polypeptide Forms Rigid Lipid-Protein Amyloid Fibrils on Supported Phospholipid Bilayers. Journal of Molecular Biology 376: 42-54.
    • (2008) Journal of Molecular Biology , vol.376 , pp. 42-54
    • Domanov, Y.A.1    Kinnunen, P.K.J.2
  • 27
    • 36049013172 scopus 로고    scopus 로고
    • Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy
    • Lopes DHJ, Meister A, Gohlke A, Hauser A, Blume A, et al. (2007) Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. Biophysical Journal 93: 3132-3141.
    • (2007) Biophysical Journal , vol.93 , pp. 3132-3141
    • Lopes, D.H.J.1    Meister, A.2    Gohlke, A.3    Hauser, A.4    Blume, A.5
  • 28
    • 0020375525 scopus 로고
    • Insular amyloidosis in spontaneously diabetic nonhuman primates
    • Palotay JL, Howard CF Jr (1982) Insular amyloidosis in spontaneously diabetic nonhuman primates. Vet Pathol Suppl 7: 181-192.
    • (1982) Vet Pathol , Issue.SUPPL. 7 , pp. 181-192
    • Palotay, J.L.1    Howard Jr, C.F.2
  • 29
    • 0015582085 scopus 로고
    • Light and electron microscopic studies of islet amyloid in diabetic cats
    • Johnson KH, Stevens JB (1973) Light and electron microscopic studies of islet amyloid in diabetic cats. Diabetes 22: 81-90.
    • (1973) Diabetes , vol.22 , pp. 81-90
    • Johnson, K.H.1    Stevens, J.B.2
  • 31
    • 0024427284 scopus 로고
    • Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone
    • Nishi M, Chan SJ, Nagamatsu S, Bell GI, Steiner DF (1989) Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone. Proc Natl Acad Sci U S A 86: 5738-5742.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 5738-5742
    • Nishi, M.1    Chan, S.J.2    Nagamatsu, S.3    Bell, G.I.4    Steiner, D.F.5
  • 32
    • 0024400674 scopus 로고
    • Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species
    • Betsholtz C, Christmansson L, Engstrom U, Rorsman F, Svensson V, et al. (1989) Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Lett 251: 261-264.
    • (1989) FEBS Lett , vol.251 , pp. 261-264
    • Betsholtz, C.1    Christmansson, L.2    Engstrom, U.3    Rorsman, F.4    Svensson, V.5
  • 33
    • 0034570847 scopus 로고    scopus 로고
    • Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP
    • Westermark GT, Gebre-Medhin S, Steiner DF, Westermark P (2000) Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP. Molecular Medicine 6: 998-1007.
    • (2000) Molecular Medicine , vol.6 , pp. 998-1007
    • Westermark, G.T.1    Gebre-Medhin, S.2    Steiner, D.F.3    Westermark, P.4
  • 36
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: A potential role for heteroaromatic interactions
    • Porat Y, Mazor Y, Efrat S, Gazit E (2004) Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 43: 14454-14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 37
    • 0036305837 scopus 로고    scopus 로고
    • Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis
    • Scrocchi LA, Chen Y, Waschuk S, Wang F, Cheung S, et al. (2002) Design of peptide-based inhibitors of human islet amyloid polypeptide fibrillogenesis. J Mol Biol 318: 697-706.
    • (2002) J Mol Biol , vol.318 , pp. 697-706
    • Scrocchi, L.A.1    Chen, Y.2    Waschuk, S.3    Wang, F.4    Cheung, S.5
  • 38
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson MR (2004) Techniques to study amyloid fibril formation in vitro. Methods 34: 151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 39
    • 2942672221 scopus 로고    scopus 로고
    • Rapid Photochemical Cross-Linking A New Tool for Studies of Metastable, Amyloidogenic Protein Assemblies
    • Bitan G, Teplow DB (2004) Rapid Photochemical Cross-Linking A New Tool for Studies of Metastable, Amyloidogenic Protein Assemblies. Accounts of Chemical Research 37: 357-364.
    • (2004) Accounts of Chemical Research , vol.37 , pp. 357-364
    • Bitan, G.1    Teplow, D.B.2
  • 40
    • 4544283591 scopus 로고    scopus 로고
    • In silico assembly of Alzheimer's Abeta16-22 peptide into beta-sheets
    • Santini S, Mousseau N, Derreumaux P (2004) In silico assembly of Alzheimer's Abeta16-22 peptide into beta-sheets. J Am Chem Soc 126: 11509-11516.
    • (2004) J Am Chem Soc , vol.126 , pp. 11509-11516
    • Santini, S.1    Mousseau, N.2    Derreumaux, P.3
  • 41
    • 66249108421 scopus 로고    scopus 로고
    • Urbanc B, Cruz L, Yun S, Buldyrev SV, Bitan G, et al. (2004) In silico study of amyloid I
    • Urbanc B, Cruz L, Yun S, Buldyrev SV, Bitan G, et al. (2004) In silico study of amyloid I
  • 42
    • 10644278760 scopus 로고    scopus 로고
    • Protein folding and oligomerization. Proceedings of the National Academy of Sciences of the United States of America 101: 17345-17350.
    • Protein folding and oligomerization. Proceedings of the National Academy of Sciences of the United States of America 101: 17345-17350.
  • 44
    • 0036784617 scopus 로고    scopus 로고
    • Molecular dynamics simulations of alanine rich {beta}-sheet oligomers: Insight into amyloid formation
    • Ma B, Nussinov R (2002) Molecular dynamics simulations of alanine rich {beta}-sheet oligomers: Insight into amyloid formation. Protein Science 11: 2335-2350.
    • (2002) Protein Science , vol.11 , pp. 2335-2350
    • Ma, B.1    Nussinov, R.2
  • 45
    • 0037627715 scopus 로고    scopus 로고
    • The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid- forming peptide from the yeast prion Sup35
    • Gsponer J, Haberthuer U, Caflisch A (2003) The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid- forming peptide from the yeast prion Sup35. Proceedings of the National Academy of Sciences of the United States of America 100: 5154-5159.
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , pp. 5154-5159
    • Gsponer, J.1    Haberthuer, U.2    Caflisch, A.3
  • 46
    • 0037337271 scopus 로고    scopus 로고
    • Dissecting the Assembly of A[beta]16-22 Amyloid Peptides into Antiparallel [beta] Sheets
    • Klimov DK, Thirumalai D (2003) Dissecting the Assembly of A[beta]16-22 Amyloid Peptides into Antiparallel [beta] Sheets. Structure 11: 295-307.
    • (2003) Structure , vol.11 , pp. 295-307
    • Klimov, D.K.1    Thirumalai, D.2
  • 48
    • 34848929022 scopus 로고    scopus 로고
    • Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils
    • doi:10.1371/journal.pcbi.0030173
    • Cheon M, Chang I, Mohanty S, Luheshi LM, Dobson CM, et al. (2007) Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils. PLoS Computational Biology 3: e173. doi:10.1371/journal.pcbi.0030173.
    • (2007) PLoS Computational Biology , vol.3
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5
  • 49
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant
    • Serio TR, Cashikar AG, Kowal AS, Sawicki GJ, Moslehi JJ, et al. (2000) Nucleated Conformational Conversion and the Replication of Conformational Information by a Prion Determinant. Science 289: 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1    Cashikar, A.G.2    Kowal, A.S.3    Sawicki, G.J.4    Moslehi, J.J.5
  • 50
    • 58149174069 scopus 로고    scopus 로고
    • Li D-W, Mohanty S, IrbǍck A, Huo S (2008) Formation and Growth of Oligomers: A Monte Carlo Study of an Amyloid Tau Fragment. PLoS Comput Biol 4: e1000238. doi:10.1371/journal.pcbi.1000238.
    • Li D-W, Mohanty S, IrbǍck A, Huo S (2008) Formation and Growth of Oligomers: A Monte Carlo Study of an Amyloid Tau Fragment. PLoS Comput Biol 4: e1000238. doi:10.1371/journal.pcbi.1000238.
  • 52
    • 0001616080 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics method for protein folding
    • Sugita Y, Okamoto Y (1999) Replica-exchange molecular dynamics method for protein folding. Chemical Physics Letters 314: 141-151.
    • (1999) Chemical Physics Letters , vol.314 , pp. 141-151
    • Sugita, Y.1    Okamoto, Y.2
  • 54
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides
    • Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL (2001) Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides. Journal of Physical Chemistry B 105: 6474-6487.
    • (2001) Journal of Physical Chemistry B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 55
    • 33847012626 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets
    • Ritzel RA, Meier JJ, Lin CY, Veldhuis JD, Butler PC (2007) Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. Diabetes 56: 65-71.
    • (2007) Diabetes , vol.56 , pp. 65-71
    • Ritzel, R.A.1    Meier, J.J.2    Lin, C.Y.3    Veldhuis, J.D.4    Butler, P.C.5
  • 56
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • 33-38
    • Humphrey W, Dalke A, Schulten K (1996) VMD: visual molecular dynamics. J Mol Graph 14: 33-38, 27-38.
    • (1996) J Mol Graph , vol.14 , pp. 27-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 57
    • 16344367783 scopus 로고    scopus 로고
    • Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations
    • Wu C, Lei H, Duan Y (2004) Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations. Biophys J 87: 3000-3009.
    • (2004) Biophys J , vol.87 , pp. 3000-3009
    • Wu, C.1    Lei, H.2    Duan, Y.3
  • 58
    • 10844230140 scopus 로고    scopus 로고
    • Replica exchange molecular dynamics simulations of amyloid peptide aggregation
    • Cecchini M, Rao F, Seeber M, Caflisch A (2004) Replica exchange molecular dynamics simulations of amyloid peptide aggregation. J Chem Phys 121: 10748-10756.
    • (2004) J Chem Phys , vol.121 , pp. 10748-10756
    • Cecchini, M.1    Rao, F.2    Seeber, M.3    Caflisch, A.4
  • 59
    • 66349136559 scopus 로고    scopus 로고
    • Lipid Molecule Enhances Aggregation of hIAPP PLoS Computational Biology | www.ploscompbiol.org 13 April 2009 | 5 | Issue 4 | e1000357
    • Lipid Molecule Enhances Aggregation of hIAPP PLoS Computational Biology | www.ploscompbiol.org 13 April 2009 | Volume 5 | Issue 4 | e1000357
  • 60
    • 0000740930 scopus 로고
    • The structural basis of pancreatic amyloid formation: Isotope-edited spectroscopy in the solid state
    • Ashburn TT, Auger M, Lansbury PT (1992) The structural basis of pancreatic amyloid formation: isotope-edited spectroscopy in the solid state. J Am Chem Soc 114: 790-791.
    • (1992) J Am Chem Soc , vol.114 , pp. 790-791
    • Ashburn, T.T.1    Auger, M.2    Lansbury, P.T.3
  • 61
    • 0000666695 scopus 로고
    • Rotational Resonance Solid-State NMR Elucidates a Structural Model of Pancreatic Amyloid
    • Griffiths JM, Ashburn TT, Auger M, Costa PR, Griffin RG, et al. (1995) Rotational Resonance Solid-State NMR Elucidates a Structural Model of Pancreatic Amyloid. J Am Chem Soc 117: 3539-3546.
    • (1995) J Am Chem Soc , vol.117 , pp. 3539-3546
    • Griffiths, J.M.1    Ashburn, T.T.2    Auger, M.3    Costa, P.R.4    Griffin, R.G.5
  • 62
    • 33745653278 scopus 로고    scopus 로고
    • The Organization of Aromatic Side Groups in an Amyloid Fibril Probed by Solid- State 2H and 19F NMR Spectroscopy
    • Jack E, Newsome M, Stockley PG, Radford SE, Middleton DA (2006) The Organization of Aromatic Side Groups in an Amyloid Fibril Probed by Solid- State 2H and 19F NMR Spectroscopy. J Am Chem Soc 128: 8098-8099.
    • (2006) J Am Chem Soc , vol.128 , pp. 8098-8099
    • Jack, E.1    Newsome, M.2    Stockley, P.G.3    Radford, S.E.4    Middleton, D.A.5
  • 63
    • 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
    • Madine J, Jack E, Stockley PG, Radford SE, Serpell LC, et al. (2008) 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. Journal of the American Chemical Society 130: 14990-15001.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Stockley, P.G.3    Radford, S.E.4    Serpell, L.C.5
  • 64
    • 33845213187 scopus 로고    scopus 로고
    • Secondary structure provides a template for the folding of nearby polypeptides
    • Kameda T, Takada S (2006) Secondary structure provides a template for the folding of nearby polypeptides. Proc Natl Acad Sci U S A 103: 17765-17770.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 17765-17770
    • Kameda, T.1    Takada, S.2
  • 65
    • 57049174009 scopus 로고    scopus 로고
    • Structures of Rat and Human Islet Amyloid Polypeptide IAPP1-19 in Micelles by NMR Spectroscopy
    • Nanga RPR, Brender JR, Xu J, Veglia G, Ramamoorthy A (2008) Structures of Rat and Human Islet Amyloid Polypeptide IAPP1-19 in Micelles by NMR Spectroscopy. Biochemistry 47: 12689-12697.
    • (2008) Biochemistry , vol.47 , pp. 12689-12697
    • Nanga, R.P.R.1    Brender, J.R.2    Xu, J.3    Veglia, G.4    Ramamoorthy, A.5
  • 67
    • 0141867848 scopus 로고    scopus 로고
    • alpha-Synuclein oligomerization: A role for lipids?
    • Welch K, Yuan J (2003) alpha-Synuclein oligomerization: a role for lipids? Trends in Neurosciences 26: 517-519.
    • (2003) Trends in Neurosciences , vol.26 , pp. 517-519
    • Welch, K.1    Yuan, J.2
  • 68
    • 36749033116 scopus 로고    scopus 로고
    • Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR
    • Luca S, Yau WM, Leapman R, Tycko R (2007) Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR. Biochemistry 46: 13505-13522.
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 69
    • 50049095633 scopus 로고    scopus 로고
    • Atomic structure of the cross-{beta} spine of islet amyloid polypeptide (amylin)
    • Wiltzius JJW, Sievers SA, Sawaya MR, Cascio D, Popov D, et al. (2008) Atomic structure of the cross-{beta} spine of islet amyloid polypeptide (amylin). Protein Sci 17: 1467-1474.
    • (2008) Protein Sci , vol.17 , pp. 1467-1474
    • Wiltzius, J.J.W.1    Sievers, S.A.2    Sawaya, M.R.3    Cascio, D.4    Popov, D.5
  • 70
    • 50049095633 scopus 로고    scopus 로고
    • Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin)
    • Wiltzius JJW, Sievers SA, Sawaya MR, Cascio D, Popov D, et al. (2008) Atomic structure of the cross-beta spine of islet amyloid polypeptide (amylin). Protein Sci 17: 1467-1474.
    • (2008) Protein Sci , vol.17 , pp. 1467-1474
    • Wiltzius, J.J.W.1    Sievers, S.A.2    Sawaya, M.R.3    Cascio, D.4    Popov, D.5
  • 71
    • 0038374923 scopus 로고    scopus 로고
    • Alessandro Mascioni FPUIARGV (2003) Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study. Biopolymers 69: 29-41.
    • Alessandro Mascioni FPUIARGV (2003) Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study. Biopolymers 69: 29-41.
  • 72
    • 0031974669 scopus 로고    scopus 로고
    • U. Ilangovan AR (1998) Conformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods. Biopolymers 45: 9-20.
    • U. Ilangovan AR (1998) Conformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods. Biopolymers 45: 9-20.
  • 73
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB (1996) On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci U S A 93: 1125-1129.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 74
    • 34047157022 scopus 로고    scopus 로고
    • Hydrophobic Cooperativity as a Mechanism for Amyloid Nucleation
    • Hills JRD, Brooks Iii CL (2007) Hydrophobic Cooperativity as a Mechanism for Amyloid Nucleation. Journal of Molecular Biology 368: 894-901.
    • (2007) Journal of Molecular Biology , vol.368 , pp. 894-901
    • Hills, J.R.D.1    Brooks Iii, C.L.2
  • 75
    • 33751016055 scopus 로고    scopus 로고
    • Characteristics of Fibers Formed by Cytochrome c and Induced by Anionic Phospholipids
    • Alakoskela J-M, Jutila A, Simonsen AC, Pirneskoski J, Pyhajoki S, et al. (2006) Characteristics of Fibers Formed by Cytochrome c and Induced by Anionic Phospholipids. Biochemistry 45: 13447-13453.
    • (2006) Biochemistry , vol.45 , pp. 13447-13453
    • Alakoskela, J.-M.1    Jutila, A.2    Simonsen, A.C.3    Pirneskoski, J.4    Pyhajoki, S.5
  • 76
    • 4043100348 scopus 로고    scopus 로고
    • Formation of Amyloid Fibers Triggered by Phosphatidylserine-Containing Membranes
    • Zhao H, Tuominen EKJ, Kinnunen PKJ (2004) Formation of Amyloid Fibers Triggered by Phosphatidylserine-Containing Membranes. Biochemistry 43: 10302-10307.
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, P.K.J.3
  • 77
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the Hydrophobic Core of Lipid Bilayers by the Human Antimicrobial Peptide LL-37
    • Henzler-Wildman KA, Martinez GV, Brown MF, Ramamoorthy A (2004) Perturbation of the Hydrophobic Core of Lipid Bilayers by the Human Antimicrobial Peptide LL-37. Biochemistry 43: 8459-8469.
    • (2004) Biochemistry , vol.43 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Brown, M.F.3    Ramamoorthy, A.4
  • 78
    • 33745747109 scopus 로고    scopus 로고
    • Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin
    • Ramamoorthy A, Thennarasu S, Lee D-K, Tan A, Maloy L (2006) Solid-State NMR Investigation of the Membrane-Disrupting Mechanism of Antimicrobial Peptides MSI-78 and MSI-594 Derived from Magainin 2 and Melittin. Biophysical Journal 91: 206-216.
    • (2006) Biophysical Journal , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Lee, D.-K.3    Tan, A.4    Maloy, L.5
  • 79
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin
    • Jorgensen WL, Tirado-Rives J (1988) The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimizations for crystals of cyclic peptides and crambin. J Am Chem Soc 110: 1657-1666.
    • (1988) J Am Chem Soc , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 80
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen WL, Maxwell DS, Tirado-Rives J (1996) Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids. J Am Chem Soc 118: 11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 81
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. Journal of Molecular Modeling 7: 306-317.
    • (2001) Journal of Molecular Modeling , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 83
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An NNlog (N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald: An NNlog (N) method for Ewald sums in large systems. The Journal of Chemical Physics 98: 10089-10092.
    • (1993) The Journal of Chemical Physics , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 84
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 85
    • 10844292652 scopus 로고    scopus 로고
    • Energy landscape of a small peptide revealed by dihedral angle principal component analysis
    • Mu Y, Nguyen PH, Stock G (2005) Energy landscape of a small peptide revealed by dihedral angle principal component analysis. Proteins 58: 45-52.
    • (2005) Proteins , vol.58 , pp. 45-52
    • Mu, Y.1    Nguyen, P.H.2    Stock, G.3
  • 86
    • 66249116486 scopus 로고    scopus 로고
    • Case TAD DA, Cheatham TE III, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Pearlman DA, Crowley M, Walker RC, Zhang W, Wang B, Hayik S, Roitberg A, Seabra G, Wong KF, Paesani F, Wu X, Brozell S, Tsui V, Gohlke H, Yang L, Tan C, Mongan J, Hornak V, Cui G, Beroza P, Mathews DH, Schafmeister C, Ross WS, Kollman PA (2006) AMBER 9. San Francisco: University of California.
    • Case TAD DA, Cheatham TE III, Simmerling CL, Wang J, Duke RE, Luo R, Merz KM, Pearlman DA, Crowley M, Walker RC, Zhang W, Wang B, Hayik S, Roitberg A, Seabra G, Wong KF, Paesani F, Wu X, Brozell S, Tsui V, Gohlke H, Yang L, Tan C, Mongan J, Hornak V, Cui G, Beroza P, Mathews DH, Schafmeister C, Ross WS, Kollman PA (2006) AMBER 9. San Francisco: University of California.
  • 87
    • 1842479952 scopus 로고    scopus 로고
    • Exploring protein native states and large-scale conformational changes with a modified generalized born model
    • Onufriev A, Bashford D, Case DA (2004) Exploring protein native states and large-scale conformational changes with a modified generalized born model. Proteins 55: 383-394.
    • (2004) Proteins , vol.55 , pp. 383-394
    • Onufriev, A.1    Bashford, D.2    Case, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.