| scholarly article | Q13442814 |
| P2093 | author name string | Yuri L Lyubchenko | |
| Simon Sherman | |||
| Alexander Rubinstein | |||
| P2860 | cites work | Dissection of the de novo designed peptide alpha t alpha: stability and properties of the intact molecule and its constituent helices | Q74533427 |
| Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates | Q78177648 | ||
| Protein conformational transitions coupled to binding in molecular recognition of unstructured proteins: hierarchy of structural loss from all-atom Monte Carlo simulations of p27Kip1 unfolding-unbinding and structural determinants of the binding mec | Q80828507 | ||
| Protein interactions and misfolding analyzed by AFM force spectroscopy | Q81486582 | ||
| The effect of Abeta conformation on the metal affinity and aggregation mechanism studied by circular dichroism spectroscopy | Q83282127 | ||
| A revised set of potentials for beta-turn formation in proteins | Q24675540 | ||
| A seven-helix coiled coil | Q24679459 | ||
| Comparison of simple potential functions for simulating liquid water | Q26778447 | ||
| The Alzheimer's peptide a beta adopts a collapsed coil structure in water | Q27626446 | ||
| Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
| The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics | Q27860914 | ||
| Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution | Q28286232 | ||
| Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico | Q28383620 | ||
| A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR | Q28387681 | ||
| Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils | Q28388148 | ||
| Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes | Q29397708 | ||
| Alzheimer's disease: the amyloid cascade hypothesis | Q29547160 | ||
| Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils | Q29617476 | ||
| Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide congener in solution | Q30625922 | ||
| Molecular dynamics simulations of Alzheimer's beta-amyloid protofilaments | Q31010167 | ||
| Simulation study on the disordered state of an Alzheimer's beta amyloid peptide Abeta(12 36) in water consisting of random-structural, beta-structural, and helical clusters. | Q31119925 | ||
| Synaptic targeting by Alzheimer's-related amyloid beta oligomers. | Q33288786 | ||
| Complementary packing of alpha-helices in proteins | Q33334182 | ||
| Long timescale simulations | Q33885203 | ||
| Conformational transition of amyloid beta-peptide | Q33936728 | ||
| Repacking protein cores with backbone freedom: structure prediction for coiled coils | Q33977493 | ||
| In vitro characterization of conditions for amyloid-beta peptide oligomerization and fibrillogenesis | Q34166792 | ||
| Relationship between ion pair geometries and electrostatic strengths in proteins | Q34178725 | ||
| Influence of the solvent structure on the electrostatic interactions in proteins | Q34186996 | ||
| Solvent and mutation effects on the nucleation of amyloid beta-protein folding | Q34234780 | ||
| Helix to helix packing in proteins | Q34283185 | ||
| Interfaces and the driving force of hydrophobic assembly | Q34455286 | ||
| Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies | Q34811887 | ||
| Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide | Q34984717 | ||
| Progress towards a molecular-level structural understanding of amyloid fibrils | Q35753224 | ||
| Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics study | Q35794575 | ||
| Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleus | Q36082193 | ||
| Linking folding with aggregation in Alzheimer's beta-amyloid peptides | Q36089177 | ||
| Strategies and rationales for the de novo design of a helical hairpin peptide | Q36279033 | ||
| Nanoimaging for protein misfolding and related diseases | Q36528645 | ||
| Simulations as analytical tools to understand protein aggregation and predict amyloid conformation | Q36578700 | ||
| Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach | Q36596611 | ||
| Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant | Q36639472 | ||
| Computer simulations of Alzheimer's amyloid beta-protein folding and assembly | Q36683230 | ||
| Kinetics of peptide folding: computer simulations of SYPFDV and peptide variants in water. | Q36885424 | ||
| Structures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions | Q36983848 | ||
| Aqueous urea solution destabilizes Abeta(16-22) oligomers | Q37570941 | ||
| Molecular dynamics simulation of amyloid beta dimer formation | Q40298901 | ||
| Realistic simulations of native-protein dynamics in solution and beyond | Q40832976 | ||
| Standard structures in proteins | Q40846153 | ||
| Alzheimer amyloid abeta1-42 channels: effects of solvent, pH, and Congo Red. | Q41684348 | ||
| The aggregation kinetics of Alzheimer's beta-amyloid peptide is controlled by stochastic nucleation | Q41839526 | ||
| Stabilization of discordant helices in amyloid fibril-forming proteins | Q41841421 | ||
| Amyloid beta-protein monomer structure: a computational and experimental study. | Q42150321 | ||
| On the nucleation of amyloid beta-protein monomer folding | Q42215600 | ||
| Structure of the 21-30 fragment of amyloid beta-protein. | Q43072330 | ||
| Nanomedicine and protein misfolding diseases. | Q43185664 | ||
| Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy | Q43642578 | ||
| Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis | Q43753104 | ||
| Assessing equilibration and convergence in biomolecular simulations | Q44060639 | ||
| Beta-hairpin conformation of fibrillogenic peptides: structure and alpha-beta transition mechanism revealed by molecular dynamics simulations | Q45028392 | ||
| A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes | Q46212322 | ||
| A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils | Q46813521 | ||
| Methods for molecular dynamics simulations of protein folding/unfolding in solution | Q47609594 | ||
| Preformed structural elements feature in partner recognition by intrinsically unstructured proteins | Q47692263 | ||
| The structure of the Alzheimer amyloid beta 10-35 peptide probed through replica-exchange molecular dynamics simulations in explicit solvent. | Q51926777 | ||
| Left-handed polyproline II helices commonly occur in globular proteins. | Q52402236 | ||
| A strand-loop-strand structure is a possible intermediate in fibril elongation: long time simulations of amyloid-beta peptide (10-35). | Q52566956 | ||
| Substitutions at codon 22 of Alzheimer's abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells. | Q53235221 | ||
| Temperature-induced conformational changes in amyloid beta(1-40) peptide investigated by simultaneous FT-IR microspectroscopy with thermal system. | Q53240966 | ||
| Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores. | Q53360220 | ||
| Dissecting the assembly of Abeta16-22 amyloid peptides into antiparallel beta sheets. | Q53658048 | ||
| Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems | Q56750591 | ||
| Insights into the amyloid folding problem from solid-state NMR | Q57188281 | ||
| Structural Analysis of Peptide Substrates for Mucin-Type O-Glycosylation† | Q57195406 | ||
| Molecular dynamics with coupling to an external bath | Q57569060 | ||
| Misfolding of the amyloid β-protein: A molecular dynamics study | Q57795080 | ||
| A linear 23-residue peptide reveals a propensity to form an unusual native-like conformation | Q71576911 | ||
| Temperature-dependent beta-sheet formation in beta-amyloid Abeta(1-40) peptide in water: uncoupling beta-structure folding from aggregation | Q73293381 | ||
| Charge alterations of E22 enhance the pathogenic properties of the amyloid beta-protein | Q73760285 | ||
| Pathogenic effects of D23N Iowa mutant amyloid beta -protein | Q74147666 | ||
| Folding-unfolding thermodynamics of a beta-heptapeptide from equilibrium simulations | Q74452346 | ||
| Calculations on folding of segment B1 of streptococcal protein G | Q74507082 | ||
| P433 | issue | 1 | |
| P304 | page(s) | 31-43 | |
| P577 | publication date | 2009-01-10 | |
| P1433 | published in | Prion | Q26842757 |
| P1476 | title | Dynamic properties of pH-dependent structural organization of the amyloidogenic beta-protein (1-40). | |
| P478 | volume | 3 |
| Q27305237 | Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics study |
| Q36881483 | Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein |
| Q37781245 | Nanoimaging for prion related diseases |
| Q37776219 | Nanoimaging for protein misfolding diseases |
| Q33605232 | Nanoprobing of misfolding and interactions of amyloid β 42 protein |
| Q38053449 | Potential sources of interference on Abeta immunoassays in biological samples |
| Q37351690 | α-Synuclein misfolding assessed with single molecule AFM force spectroscopy: effect of pathogenic mutations |
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