Molecular dynamics simulation studies of the structural response of an isolated Aβ1–42 monomer localized in the vicinity of the hydrophilic TiO2 surface
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[1] D. Klimov,et al. Binding to the lipid monolayer induces conformational transition in Aβ monomer , 2013, Journal of Molecular Modeling.
[2] Neelanjana Sengupta,et al. Critical roles of key domains in complete adsorption of Aβ peptide on single-walled carbon nanotubes: insights with point mutations and MD simulations. , 2013, Physical chemistry chemical physics : PCCP.
[3] J. Dutcher,et al. Using nanoscale substrate curvature to control the dimerization of a surface-bound protein. , 2012, ACS nano.
[4] Chiu Fan Lee,et al. Combined Effects of Agitation, Macromolecular Crowding, and Interfaces on Amyloidogenesis* , 2012, The Journal of Biological Chemistry.
[5] Florentina Tofoleanu,et al. Molecular interactions of Alzheimer's Aβ protofilaments with lipid membranes. , 2012, Journal of molecular biology.
[6] N. Buchete,et al. Alzheimer Aβ peptide interactions with lipid membranes , 2012, Prion.
[7] W. Scheper,et al. PEGylated nanoparticles bind to and alter amyloid-beta peptide conformation: toward engineering of functional nanomedicines for Alzheimer's disease. , 2012, ACS nano.
[8] I. Nabiev,et al. Molecular interaction of proteins and peptides with nanoparticles. , 2012, ACS nano.
[9] S. Andujar,et al. Amyloid-β fibril disruption by C60-molecular guidance for rational drug design. , 2012, Physical chemistry chemical physics : PCCP.
[10] S. Chong,et al. Impact of chemical heterogeneity on protein self-assembly in water , 2012, Proceedings of the National Academy of Sciences.
[11] Neelanjana Sengupta,et al. Adsorption mechanism and collapse propensities of the full-length, monomeric Aβ(1-42) on the surface of a single-walled carbon nanotube: a molecular dynamics simulation study. , 2012, Biophysical journal.
[12] Yinan Lin,et al. Structure, orientation, and surface interaction of Alzheimer amyloid-β peptides on the graphite. , 2012, Langmuir : the ACS journal of surfaces and colloids.
[13] Neelanjana Sengupta,et al. Effect of the A30P mutation on the structural dynamics of micelle-bound αSynuclein released in water: a molecular dynamics study , 2012, European Biophysics Journal.
[14] Chiu Fan Lee,et al. Enrichment of amyloidogenesis at an air-water interface. , 2012, Biophysical journal.
[15] N. Mousseau,et al. Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure. , 2012, The journal of physical chemistry. B.
[16] Jie Zheng,et al. Molecular dynamics simulations of low-ordered alzheimer β-amyloid oligomers from dimer to hexamer on self-assembled monolayers. , 2011, Langmuir : the ACS journal of surfaces and colloids.
[17] Grazia Daminelli,et al. Molecular dynamics simulations of the adsorption of bone morphogenetic protein-2 on surfaces with medical relevance. , 2011, Langmuir : the ACS journal of surfaces and colloids.
[18] R. Nussinov,et al. Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation. , 2011, Soft matter.
[19] N. Kotov,et al. Inhibition of amyloid peptide fibrillation by inorganic nanoparticles: functional similarities with proteins. , 2011, Angewandte Chemie.
[20] Son Tung Ngo,et al. Inhibition of aggregation of amyloid peptides by beta-sheet breaker peptides and their binding affinity. , 2011, The journal of physical chemistry. B.
[21] C. Chipot,et al. Free-Energy Landscape of the Helical Wrapping of a Carbon Nanotube by a Polysaccharide , 2011 .
[22] I. Banerjee,et al. Interactions of amyloid Aβ(1–42) peptide with self‐assembled peptide nanospheres , 2011, Journal of peptide science : an official publication of the European Peptide Society.
[23] Jie Zheng,et al. Alzheimer Abeta(1-42) monomer adsorbed on the self-assembled monolayers. , 2010, Langmuir : the ACS journal of surfaces and colloids.
[24] G. J. Martyna,et al. Conformational plasticity in an HIV-1 antibody epitope. , 2010, The journal of physical chemistry. B.
[25] E. Bramanti,et al. Effects of hypericin on the structure and aggregation properties of β-amyloid peptides , 2010, European Biophysics Journal.
[26] M. Carlo. Beta amyloid peptide: from different aggregation forms to the activation of different biochemical pathways , 2010, European Biophysics Journal.
[27] R. Nussinov,et al. Polymorphism in Alzheimer Aβ Amyloid Organization Reflects Conformational Selection in a Rugged Energy Landscape , 2010, Chemical reviews.
[28] Judianne Davis,et al. Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils , 2010, Nature Structural &Molecular Biology.
[29] M. Berkowitz,et al. Structure of the amyloid-beta (1-42) monomer absorbed to model phospholipid bilayers: a molecular dynamics study. , 2009, The journal of physical chemistry. B.
[30] Guanghong Wei,et al. Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition. , 2009, Biophysical journal.
[31] S. Maiti,et al. On the stability of the soluble amyloid aggregates. , 2009, Biophysical journal.
[32] B. Penke,et al. In silico study of full-length amyloid beta 1-42 tri- and penta-oligomers in solution. , 2009, The journal of physical chemistry. B.
[33] C. Robinson,et al. Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. , 2009, Nature chemistry.
[34] R. Leapman,et al. Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure , 2009, Proceedings of the National Academy of Sciences.
[35] M. Berkowitz,et al. Interaction between amyloid-beta (1-42) peptide and phospholipid bilayers: a molecular dynamics study. , 2009, Biophysical journal.
[36] Sandra C. Mwakwari,et al. Historic perspective on the use of AuNPs in medicine , 2008 .
[37] Mark E. Davis,et al. Nanoparticle therapeutics: an emerging treatment modality for cancer , 2008, Nature Reviews Drug Discovery.
[38] Lei Zhao,et al. TiO2 nanoparticles promote beta-amyloid fibrillation in vitro. , 2008, Biochemical and biophysical research communications.
[39] C. Hall. Thermodynamic and kinetic origins of Alzheimer's and related diseases: A chemical engineer's perspective , 2008 .
[40] G. Hummer,et al. Are current molecular dynamics force fields too helical? , 2008, Biophysical journal.
[41] R. Cappai,et al. Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity , 2008, Neurochemical Research.
[42] G. Gröbner,et al. Misfolding of amyloidogenic proteins at membrane surfaces: the impact of macromolecular crowding. , 2007, Journal of the American Chemical Society.
[43] Filip Braet,et al. Carbon nanotubes for biological and biomedical applications , 2007 .
[44] Xing Lu,et al. Dendrimer-Mediated Synthesis of Water-Dispersible Carbon-Nanotube-Supported Oxide Nanoparticles , 2007 .
[45] S. Radford,et al. Nucleation of protein fibrillation by nanoparticles , 2007, Proceedings of the National Academy of Sciences.
[46] Kristen M Kulinowski,et al. Nanoparticles as catalysts for protein fibrillation , 2007, Proceedings of the National Academy of Sciences.
[47] Yilin Yan,et al. The Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR study. , 2007, Journal of molecular biology.
[48] S. Ferreira,et al. Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts , 2007, Progress in Neurobiology.
[49] H. Huang,et al. The correlation between neurotoxicity, aggregative ability and secondary structure studied by sequence truncated Aβ peptides , 2007, FEBS letters.
[50] Joan-Emma Shea,et al. The structure of the Alzheimer amyloid beta 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent. , 2007, Journal of molecular biology.
[51] D. Selkoe,et al. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide , 2007, Nature Reviews Molecular Cell Biology.
[52] M. Prato,et al. Cellular uptake of functionalized carbon nanotubes is independent of functional group and cell type. , 2007, Nature nanotechnology.
[53] H. Wagner,et al. The role of surfactants in dispersion of carbon nanotubes. , 2006, Advances in colloid and interface science.
[54] M. Prato,et al. Carbon nanotubes as nanomedicines: from toxicology to pharmacology. , 2006, Advanced drug delivery reviews.
[55] A. Bonvin,et al. The α‐to‐β Conformational Transition of Alzheimer's Aβ‐(1–42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of β Conformation Seeding , 2006 .
[56] W. Norde,et al. Conformational changes of the amyloid beta-peptide (1-40) adsorbed on solid surfaces. , 2005, Macromolecular bioscience.
[57] G. Bitan,et al. Amyloid β-protein: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform , 2005 .
[58] D. Case,et al. Exploring protein native states and large‐scale conformational changes with a modified generalized born model , 2004, Proteins.
[59] Oleg Borodin,et al. Molecular Dynamics Study of the Influence of Solid Interfaces on Poly(ethylene oxide) Structure and Dynamics , 2003 .
[60] Carl W. Cotman,et al. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis , 2003, Science.
[61] Minyung Lee,et al. Fullerene inhibits β-amyloid peptide aggregation , 2003 .
[62] D. Teplow,et al. Kinetic Studies of Amyloid β-Protein Fibril Assembly , 2002, The Journal of Biological Chemistry.
[63] J. Hardy,et al. The Amyloid Hypothesis of Alzheimer ’ s Disease : Progress and Problems on the Road to Therapeutics , 2009 .
[64] R. Murphy,et al. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. , 2001, Biophysical journal.
[65] A. Minton,et al. The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media* , 2001, The Journal of Biological Chemistry.
[66] D. Case,et al. Modification of the Generalized Born Model Suitable for Macromolecules , 2000 .
[67] Laxmikant V. Kale,et al. NAMD2: Greater Scalability for Parallel Molecular Dynamics , 1999 .
[68] D. Holtzman,et al. In situ atomic force microscopy study of Alzheimer’s β-amyloid peptide on different substrates: New insights into mechanism of β-sheet formation , 1999 .
[69] A. Minton,et al. Adsorption of globular proteins on locally planar surfaces: models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria. , 1996, Biophysical journal.
[70] K Schulten,et al. VMD: visual molecular dynamics. , 1996, Journal of molecular graphics.
[71] D. Selkoe,et al. Amyloid β-peptide is produced by cultured cells during normal metabolism , 1992, Nature.
[72] K. Grzeschik,et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor , 1987, Nature.
[73] M. Karplus,et al. CHARMM: A program for macromolecular energy, minimization, and dynamics calculations , 1983 .
[74] Sihyun Ham,et al. Characterizing amyloid‐beta protein misfolding from molecular dynamics simulations with explicit water , 2011, J. Comput. Chem..
[75] Chewook Lee,et al. Charactering Amyloid-Beta Protein Misfolding from Molecular Dynamics Simulation with Explicit Water , 2010 .
[76] A. Bonvin,et al. The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding. , 2006, Chembiochem : a European journal of chemical biology.
[77] David,et al. In situ atomic force microscopy study of Alzheimer’s b-amyloid peptide on different substrates: New insights into mechanism of b-sheet formation , 1999 .
[78] A. Minton. Adsorption of globular proteins on locally planar surfaces. II. Models for the effect of multiple adsorbate conformations on adsorption equilibria and kinetics. , 1999, Biophysical journal.