메뉴 건너뛰기




Volumn 117, Issue 50, 2013, Pages 16076-16085

Mutations and seeding of amylin fibril-like oligomers

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID DISEASE; FIBRIL STRUCTURE; IN-SILICO; MOLECULAR MECHANISM; PROTEIN SOLUTION; SIDE-CHAINS; STRUCTURAL STABILITIES; WILD TYPES;

EID: 84890909128     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp409777p     Document Type: Article
Times cited : (28)

References (64)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, And Human Disease Annu. Rev. Biochem. 2006, 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 84863988708 scopus 로고    scopus 로고
    • A Molecular History of the Amyloidoses
    • Buxbaum, J. N.; Linke, R. P. A Molecular History of the Amyloidoses J. Mol. Biol. 2012, 421, 142-159
    • (2012) J. Mol. Biol. , vol.421 , pp. 142-159
    • Buxbaum, J.N.1    Linke, R.P.2
  • 3
    • 84858374665 scopus 로고    scopus 로고
    • The Amyloid State of Proteins in Human Diseases
    • Eisenberg, D.; Jucker, M. The Amyloid State of Proteins in Human Diseases Cell 2012, 148, 1188-1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 4
    • 84876492200 scopus 로고    scopus 로고
    • The Supramolecular Chemistry of beta-Sheets
    • Cheng, P. N.; Pham, J. D.; Nowick, J. S. The Supramolecular Chemistry of beta-Sheets J. Am. Chem. Soc. 2013, 135, 5477-5492
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 5477-5492
    • Cheng, P.N.1    Pham, J.D.2    Nowick, J.S.3
  • 5
    • 0030908095 scopus 로고    scopus 로고
    • Models of Amyloid Seeding in Alzheimier'S Disease and Scrapie: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
    • Harper, J. D.; Lansbury, P. T. Models of Amyloid Seeding in Alzheimier'S Disease and Scrapie: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins Annu. Rev. Biochem. 1997, 66, 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 6
    • 84876208687 scopus 로고    scopus 로고
    • From Soluble A beta to Progressive A beta Aggregation: Could Prion-Like Templated Misfolding Play a Role?
    • Eisele, Y. S. From Soluble A beta to Progressive A beta Aggregation: Could Prion-Like Templated Misfolding Play a Role? Brain Pathol. 2013, 23, 333-341
    • (2013) Brain Pathol. , vol.23 , pp. 333-341
    • Eisele, Y.S.1
  • 7
    • 84890121878 scopus 로고    scopus 로고
    • Amylin deposition in the brain: A second amyloid in Alzheimer's disease?
    • In Press. DOI: 10.1002/ana.23956.
    • Jackson, K.; Barisone, G. A.; Diaz, E.; Jin, L. W.; DeCarli, C.; Despa, F. Amylin deposition in the brain: a second amyloid in Alzheimer's disease? Ann. Neurol. In Press. DOI: 10.1002/ana.23956.
    • Ann. Neurol.
    • Jackson, K.1    Barisone, G.A.2    Diaz, E.3    Jin, L.W.4    Decarli, C.5    Despa, F.6
  • 8
    • 0027195933 scopus 로고
    • Seeding One-Dimensional Crystallization of Amyloid - A Pathogenic Mechanism in Alzheimers-Disease and Scrapie
    • Jarrett, J. T.; Lansbury, P. T. Seeding One-Dimensional Crystallization of Amyloid-a Pathogenic Mechanism in Alzheimers-Disease and Scrapie Cell 1993, 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 9
    • 84874812945 scopus 로고    scopus 로고
    • Evidence of pi-Stacking Interactions in the Self-Assembly of hIAPP(22-29)
    • Profit, A. A.; Felsen, V.; Chinwong, J.; Mojica, E. R. E.; Desamero, R. Z. B. Evidence of pi-Stacking Interactions in the Self-Assembly of hIAPP(22-29) Proteins 2013, 81, 690-703
    • (2013) Proteins , vol.81 , pp. 690-703
    • Profit, A.A.1    Felsen, V.2    Chinwong, J.3    Mojica, E.R.E.4    Desamero, R.Z.B.5
  • 10
    • 84857793669 scopus 로고    scopus 로고
    • Role of Amino Acid Hydrophobicity, Aromaticity, and Molecular Volume on IAPP(20-29) Amyloid Self-Assembly
    • Doran, T. M.; Kamens, A. J.; Byrnes, N. K.; Nilsson, B. L. Role of Amino Acid Hydrophobicity, Aromaticity, And Molecular Volume on IAPP(20-29) Amyloid Self-Assembly Proteins 2012, 80, 1053-1065
    • (2012) Proteins , vol.80 , pp. 1053-1065
    • Doran, T.M.1    Kamens, A.J.2    Byrnes, N.K.3    Nilsson, B.L.4
  • 12
    • 77953442000 scopus 로고    scopus 로고
    • Interaction of hIAPP with Model Raft Membranes and Pancreatic beta-Cells: Cytotoxicity of hIAPP Oligomers
    • Weise, K.; Radovan, D.; Gohlke, A.; Opitz, N.; Winter, R. Interaction of hIAPP with Model Raft Membranes and Pancreatic beta-Cells: Cytotoxicity of hIAPP Oligomers ChemBioChem 2010, 11, 1280-1290
    • (2010) ChemBioChem , vol.11 , pp. 1280-1290
    • Weise, K.1    Radovan, D.2    Gohlke, A.3    Opitz, N.4    Winter, R.5
  • 17
    • 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, P. G.; Radford, S. E.; Serpell, L. C.; Middleton, D. A. 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. 2008, 130, 14990-15001
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Stockley, P.G.3    Radford, S.E.4    Serpell, L.C.5    Middleton, D.A.6
  • 18
    • 36749033116 scopus 로고    scopus 로고
    • Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR
    • Luca, S.; Yau, W. M.; Leapman, R.; Tycko, R. Peptide Conformation and Supramolecular Organization in Amylin Fibrils: Constraints from Solid-State NMR Biochemistry 2007, 46, 13505-13522
    • (2007) Biochemistry , vol.46 , pp. 13505-13522
    • Luca, S.1    Yau, W.M.2    Leapman, R.3    Tycko, R.4
  • 19
    • 84870831546 scopus 로고    scopus 로고
    • Molecular Dynamics Simulation Study on the Molecular Structures of the Amylin Fibril Models
    • Xu, W. X.; Su, H. B.; Zhang, J. Z. H.; Mu, Y. G. Molecular Dynamics Simulation Study on the Molecular Structures of the Amylin Fibril Models J. Phys. Chem. B 2012, 116, 13991-13999
    • (2012) J. Phys. Chem. B , vol.116 , pp. 13991-13999
    • Xu, W.X.1    Su, H.B.2    Zhang, J.Z.H.3    Mu, Y.G.4
  • 20
    • 78651268241 scopus 로고    scopus 로고
    • Structural Polymorphism of Human Islet Amyloid Polypeptide (hIAPP) Oligomers Highlights the Importance of Interfacial Residue Interactions
    • Zhao, J.; Yu, X. A.; Liang, G. Z.; Zheng, J. Structural Polymorphism of Human Islet Amyloid Polypeptide (hIAPP) Oligomers Highlights the Importance of Interfacial Residue Interactions Biomacromolecules 2011, 12, 210-220
    • (2011) Biomacromolecules , vol.12 , pp. 210-220
    • Zhao, J.1    Yu, X.A.2    Liang, G.Z.3    Zheng, J.4
  • 21
    • 79955852760 scopus 로고    scopus 로고
    • Heterogeneous Triangular Structures of Human Islet Amyloid Polypeptide (Amylin) with Internal Hydrophobic Cavity and External Wrapping Morphology Reveal the Polymorphic Nature of Amyloid Fibrils
    • Zhao, J.; Yu, X.; Liang, G. Z.; Zheng, J. Heterogeneous Triangular Structures of Human Islet Amyloid Polypeptide (Amylin) with Internal Hydrophobic Cavity and External Wrapping Morphology Reveal the Polymorphic Nature of Amyloid Fibrils Biomacromolecules 2011, 12, 1781-1794
    • (2011) Biomacromolecules , vol.12 , pp. 1781-1794
    • Zhao, J.1    Yu, X.2    Liang, G.Z.3    Zheng, J.4
  • 22
    • 84904042704 scopus 로고    scopus 로고
    • Full Length Amylin Oligomer Aggregation: Insights from Molecular Dynamics Simulations and Implications for Design of Aggregation Inhibitors
    • In Press. DOI: 10.1080/07391102.
    • Berhanu, W. M.; Masunov, A. E. Full Length Amylin Oligomer Aggregation: Insights from Molecular Dynamics Simulations and Implications for Design of Aggregation Inhibitors. J. Biomol. Struct. Dyn. In Press. DOI: 10.1080/07391102.
    • J. Biomol. Struct. Dyn.
    • Berhanu, W.M.1    Masunov, A.E.2
  • 23
    • 84872579755 scopus 로고    scopus 로고
    • Role of Aromatic Interactions in Amyloid Formation by Islet Amyloid Polypeptide
    • Tu, L. H.; Raleigh, D. P. Role of Aromatic Interactions in Amyloid Formation by Islet Amyloid Polypeptide Biochemistry 2013, 52, 333-342
    • (2013) Biochemistry , vol.52 , pp. 333-342
    • Tu, L.H.1    Raleigh, D.P.2
  • 24
    • 84880638556 scopus 로고    scopus 로고
    • Structure-Based Discovery of Fiber-Binding Compounds That Reduce the Cytotoxicity of Amyloid beta
    • Jiang, L.; Liu, C.; Leibly, D.; Landau, M.; Zhao, M.; Hughes, M. P.; DS., E. Structure-Based Discovery of Fiber-Binding Compounds That Reduce the Cytotoxicity of Amyloid beta Elife 2013, 2, e00857
    • (2013) Elife , vol.2 , pp. 00857
    • Jiang, L.1    Liu, C.2    Leibly, D.3    Landau, M.4    Zhao, M.5    Hughes, M.P.6
  • 25
    • 84881124929 scopus 로고    scopus 로고
    • Conformational Stability of Fibrillar Amyloid-Beta Oligomers via Protofilament Pair Formation-A Systematic Computational Study
    • Kahler, A.; Sticht, H.; AHC, H. Conformational Stability of Fibrillar Amyloid-Beta Oligomers via Protofilament Pair Formation-A Systematic Computational Study PLoS ONE 2013, 8, e70521
    • (2013) PLoS ONE , vol.8 , pp. 70521
    • Kahler, A.1    Sticht, H.2    Ahc, H.3
  • 26
    • 84879988933 scopus 로고    scopus 로고
    • In Silico Investigation and Targeting of Amyloid β Oligomers of Different Size
    • Autieroa, I.; Saviano, M.; Langella, E. In Silico Investigation and Targeting of Amyloid β Oligomers of Different Size Mol. BioSyst. 2013, 9, 2118-2124
    • (2013) Mol. BioSyst. , vol.9 , pp. 2118-2124
    • Autieroa, I.1    Saviano, M.2    Langella, E.3
  • 27
    • 84864235878 scopus 로고    scopus 로고
    • Alternative Packing Modes As Basis for Amyloid Polymorphismin Five Fragments
    • Berhanu, W. M.; Masunov, A. E. Alternative Packing Modes As Basis for Amyloid Polymorphismin Five Fragments Pept. Sci. 2012, 98, 131-144
    • (2012) Pept. Sci. , vol.98 , pp. 131-144
    • Berhanu, W.M.1    Masunov, A.E.2
  • 28
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters
    • Hornak, V.; Abel, R.; Okur, A.; Strockbine, B.; Roitberg, A.; Simmerling, C. Comparison of Multiple Amber Force Fields and Development of Improved Protein Backbone Parameters Proteins 2006, 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 30
    • 80052503022 scopus 로고    scopus 로고
    • Computational Electrophysiology: The Molecular Dynamics of Ion Channel Permeation and Selectivity in Atomistic Detail
    • Kutzner, C.; Grubmuller, H.; de Groot, B. L.; Zachariae, U. Computational Electrophysiology: The Molecular Dynamics of Ion Channel Permeation and Selectivity in Atomistic Detail Biophys. J. 2011, 101, 809-817
    • (2011) Biophys. J. , vol.101 , pp. 809-817
    • Kutzner, C.1    Grubmuller, H.2    De Groot, B.L.3    Zachariae, U.4
  • 31
    • 84864187173 scopus 로고    scopus 로고
    • Structure and Dynamics of Amyloid-b Segmental Polymorphisms
    • Workalemahu, M. B.; Hansmann, U. H. E. Structure and Dynamics of Amyloid-b Segmental Polymorphisms PLoS ONE 2012, 7, e41479
    • (2012) PLoS ONE , vol.7 , pp. 41479
    • Workalemahu, M.B.1    Hansmann, U.H.E.2
  • 32
    • 84856723314 scopus 로고    scopus 로고
    • Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation
    • Ndlovu, H.; Ashcroft, A. E.; Radford, S. E.; Harris, S. A. Effect of Sequence Variation on the Mechanical Response of Amyloid Fibrils Probed by Steered Molecular Dynamics Simulation Biophys. J. 2012, 102, 587-596
    • (2012) Biophys. J. , vol.102 , pp. 587-596
    • Ndlovu, H.1    Ashcroft, A.E.2    Radford, S.E.3    Harris, S.A.4
  • 34
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An n. Log(n) Method for Ewald Sums in Large Systems
    • Darden, T.; York, D.; Pedersen, L. Particle Mesh Ewald-an n. log(n) Method for Ewald Sums in Large Systems J. Chem. Phys. 1993, 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 36
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation
    • Hess, B. P-LINCS: A Parallel Linear Constraint Solver for Molecular Simulation J. Chem. Theory Comput. 2008, 4, 116-122
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 37
    • 84986440341 scopus 로고
    • Settle - An Analytical Version of the Shake and Rattle Algorithm for Rigid Water Models
    • Miyamoto, S.; Kollman, P. A. Settle-an Analytical Version of the Shake and Rattle Algorithm for Rigid Water Models J. Comput. Chem. 1992, 13, 952-962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 38
    • 33846086933 scopus 로고    scopus 로고
    • Canonical Sampling through Velocity Rescaling
    • Bussi, G.; Donadio, D.; Parrinello, M. Canonical Sampling through Velocity Rescaling J. Chem. Phys. 2007, 126, 014101
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 39
    • 60749136514 scopus 로고    scopus 로고
    • Isothermal-Isobaric Molecular Dynamics Using Stochastic Velocity Rescaling
    • Bussi, G.; Zykova-Timan, T.; Parrinello, M. Isothermal-Isobaric Molecular Dynamics Using Stochastic Velocity Rescaling J. Chem. Phys. 2009, 130, 074101
    • (2009) J. Chem. Phys. , vol.130 , pp. 074101
    • Bussi, G.1    Zykova-Timan, T.2    Parrinello, M.3
  • 40
    • 0019707626 scopus 로고
    • Polymorphic Transitions in Single-Crystals - A New Molecular-Dynamics Method
    • Parrinello, M.; Rahman, A. Polymorphic Transitions in Single-Crystals-a New Molecular-Dynamics Method J. Appl. Phys. 1981, 52, 7182-7190
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 42
    • 84873685394 scopus 로고    scopus 로고
    • Comparative Molecular Dynamics Study of Human Islet Amyloid Polypeptide (IAPP) and Rat IAPP Oligomers
    • Liang, G. Z.; Zhao, J.; Yu, X.; Zheng, J. Comparative Molecular Dynamics Study of Human Islet Amyloid Polypeptide (IAPP) and Rat IAPP Oligomers Biochemistry 2013, 52, 1089-1100
    • (2013) Biochemistry , vol.52 , pp. 1089-1100
    • Liang, G.Z.1    Zhao, J.2    Yu, X.3    Zheng, J.4
  • 44
    • 84882907930 scopus 로고    scopus 로고
    • The Stability of Cylindrin β-Barrel Amyloid Oligomer Models-a Molecular Dynamics Study
    • Workalemahu, M. B.; Hansmann, U. H. E. The Stability of Cylindrin β-Barrel Amyloid Oligomer Models-a Molecular Dynamics Study Proteins 2013, 81, 1542-1555
    • (2013) Proteins , vol.81 , pp. 1542-1555
    • Workalemahu, M.B.1    Hansmann, U.H.E.2
  • 46
    • 84883418395 scopus 로고    scopus 로고
    • Structural Similarities and Differences between Amyloidogenic and Non-Amyloidogenic Islet Amyloid Polypeptide (IAPP) Sequences and Implications for the Dual Physiological and Pathological Activities of These Peptides
    • Wu, C.; Shea, J.-E. Structural Similarities and Differences between Amyloidogenic and Non-Amyloidogenic Islet Amyloid Polypeptide (IAPP) Sequences and Implications for the Dual Physiological and Pathological Activities of These Peptides PLoS Comput Biol 2013, 9, e1003211-1003223
    • (2013) PLoS Comput Biol , vol.9 , pp. 1003211-1003223
    • Wu, C.1    Shea, J.-E.2
  • 49
    • 84859489661 scopus 로고    scopus 로고
    • Microcin Amyloid Fibrils A Are Reservoir of Toxic Oligomeric Species
    • Shahnawaz, M.; Soto, C. Microcin Amyloid Fibrils A Are Reservoir of Toxic Oligomeric Species J. Biol. Chem. 2012, 287, 11665-11676
    • (2012) J. Biol. Chem. , vol.287 , pp. 11665-11676
    • Shahnawaz, M.1    Soto, C.2
  • 51
    • 0020997912 scopus 로고
    • Dictionary of Protein Secondary Structure - Pattern-Recognition of Hydrogen-Bonded and Geometrical Features
    • Kabsch, W.; Sander, C. Dictionary Of Protein Secondary Structure-Pattern-Recognition Of Hydrogen-Bonded And Geometrical Features Biopolymers 1983, 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 52
    • 0034521981 scopus 로고    scopus 로고
    • Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models
    • Kollman, P. A.; Massova, I.; Reyes, C.; Kuhn, B.; Huo, S. H.; Chong, L.; Lee, M.; Lee, T.; Duan, Y.; Wang, W. Calculating Structures and Free Energies of Complex Molecules: Combining Molecular Mechanics and Continuum Models Acc. Chem. Res. 2000, 33, 889-897
    • (2000) Acc. Chem. Res. , vol.33 , pp. 889-897
    • Kollman, P.A.1    Massova, I.2    Reyes, C.3    Kuhn, B.4    Huo, S.H.5    Chong, L.6    Lee, M.7    Lee, T.8    Duan, Y.9    Wang, W.10
  • 53
    • 84888387835 scopus 로고    scopus 로고
    • In Silico Cross Seeding of Aβ and Amylin Fibril-Like Oligomers
    • Berhanu, W.; Fatih, Y.; Hansmann, U., In Silico Cross Seeding of Aβ and Amylin Fibril-Like Oligomers. ACS Neurosci. 2013, 4, 1488-1500.
    • (2013) ACS Neurosci. , vol.4 , pp. 1488-1500
    • Berhanu, W.1    Fatih, Y.2    Hansmann, U.3
  • 54
    • 70349658765 scopus 로고    scopus 로고
    • Thermodynamic Selection of Steric Zipper Patterns in the Amyloid Cross-beta Spine
    • Park, J.; Kahng, B.; Hwang, W. Thermodynamic Selection of Steric Zipper Patterns in the Amyloid Cross-beta Spine PLoS Comput. Biol. 2009, 5 (9) e1000492
    • (2009) PLoS Comput. Biol. , vol.5 , Issue.9 , pp. 1000492
    • Park, J.1    Kahng, B.2    Hwang, W.3
  • 55
    • 84883174330 scopus 로고    scopus 로고
    • Hot-Spot Mapping of the Interactions between Chymosin and Bovine kappa-Casein
    • Sorensen, J.; Palmer, D. S.; Schiott, B. Hot-Spot Mapping of the Interactions between Chymosin and Bovine kappa-Casein J. Agric. Food Chem. 2013, 61, 7949-7959
    • (2013) J. Agric. Food Chem. , vol.61 , pp. 7949-7959
    • Sorensen, J.1    Palmer, D.S.2    Schiott, B.3
  • 56
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems
    • Butterfield, S. M.; Lashuel, H. A. Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems Angew. Chem., Int. Ed. 2010, 49, 5628-5654
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 57
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-beta Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain
    • Lasagna-Reeves, C. A.; Glabe, C. G.; Kayed, R. Amyloid-beta Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain J. Biol. Chem. 2011, 286, 22122-22130
    • (2011) J. Biol. Chem. , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 58
    • 84883075131 scopus 로고    scopus 로고
    • Structures of Oligomers of a Peptide from β-Amyloid
    • Pham, J. D.; Chim, N.; Goulding, C. W.; Nowick, J. S. Structures of Oligomers of a Peptide from β-Amyloid J. Am. Chem. Soc. 2013, 135, 12460-12467
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 12460-12467
    • Pham, J.D.1    Chim, N.2    Goulding, C.W.3    Nowick, J.S.4
  • 59
    • 79960449390 scopus 로고    scopus 로고
    • Structure and Membrane Orientation of IAPP in Its Natively Amidated Form at Physiological pH in a Membrane Environment
    • Nanga, R. P. R.; Brender, J. R.; Vivekanandan, S.; Ramamoorthy, A. Structure and Membrane Orientation of IAPP in Its Natively Amidated Form at Physiological pH in a Membrane Environment Biochim. Biophys. 2011, 1808, 2337-2342
    • (2011) Biochim. Biophys. , vol.1808 , pp. 2337-2342
    • Nanga, R.P.R.1    Brender, J.R.2    Vivekanandan, S.3    Ramamoorthy, A.4
  • 62
    • 84883240288 scopus 로고    scopus 로고
    • Dynamics of Water in the Amphiphilic Pore of Amyloid β Fibrils
    • GhattyVenkataKrishna, P. K.; Mostofian, B. Dynamics of Water in the Amphiphilic Pore of Amyloid β Fibrils Chem. Phys. Lett. 2013, 582, 1-5
    • (2013) Chem. Phys. Lett. , vol.582 , pp. 1-5
    • Ghattyvenkatakrishna, P.K.1    Mostofian, B.2
  • 63
    • 84885641038 scopus 로고    scopus 로고
    • Identification of a Common Binding Mode for Imaging Agents to Amyloid Fibrils from Molecular Dynamics Simulations
    • Skeby, K. K.; Sørensen, J.; Schiøtt, B. Identification of a Common Binding Mode for Imaging Agents to Amyloid Fibrils from Molecular Dynamics Simulations J. Am. Chem. Soc. 2013, 135, 15114-15128
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 15114-15128
    • Skeby, K.K.1    Sørensen, J.2    Schiøtt, B.3
  • 64
    • 84880638556 scopus 로고    scopus 로고
    • Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta
    • Jiang, L.; Liu, C.; Leibly, D.; Landau, M.; Zhao, M.; Hughes, M. P.; Eisenberg, D. S. Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta Elife 2013, 16, e00857
    • (2013) Elife , vol.16 , pp. 00857
    • Jiang, L.1    Liu, C.2    Leibly, D.3    Landau, M.4    Zhao, M.5    Hughes, M.P.6    Eisenberg, D.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.