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Oligomers of the Prion Protein Fragment 106−126 Are Likely Assembled from β-Hairpins in Solution, and Methionine Oxidation Inhibits Assembly without Altering the Peptide’s Monomeric Conformation
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Peptide Folding: When Simulation Meets Experiment
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Transport Properties of Ions in Gases
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Prion protein (PrP) with amino‐proximal deletions restoring susceptibility of PrP knockout mice to scrapie.
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Exploring protein native states and large‐scale conformational changes with a modified generalized born model
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Knowledge‐based protein secondary structure assignment
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A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular Dichroism
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Prion Protein Peptides: Optimal Toxicity and Peptide Blockade of Toxicity
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Cytotoxicity of Prion Protein Peptide (PrP106–126) Differs in Mechanism from the Cytotoxic Activity of the Alzheimer's Disease Amyloid Peptide, Aβ25–35
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Gas-Phase Conformations: The Ion Mobility/Ion Chromatography Method
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The development/application of a ‘minimalist’ organic/biochemical molecular mechanic force field using a combination of ab initio calculations and experimental data
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Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide
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An exact hard-spheres scattering model for the mobilities of polyatomic ions
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Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes
inferredcites →https://doi.org/10.1016/j.febslet.2004.09.073openalex-snapshot
Amyloid aggregates of the prion peptide PrP106–126 are destabilised by oxidation and by the action of dendrimers
inferredcites →https://doi.org/10.1016/j.ijms.2006.07.021openalex-snapshot
An investigation of the mobility separation of some peptide and protein ions using a new hybrid quadrupole/travelling wave IMS/oa-ToF instrument
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B-DNA Helix Stability in a Solvent-Free Environment
inferredcites →https://doi.org/10.1016/j.jmb.2006.07.032openalex-snapshot
Folding Landscapes of the Alzheimer Amyloid-β(12-28) Peptide
inferredcites →https://doi.org/10.1016/j.jmb.2009.01.029openalex-snapshot
The Structure of Aβ42 C-Terminal Fragments Probed by a Combined Experimental and Theoretical Study
inferredcites →https://doi.org/10.1016/s0009-2614(99)01123-9openalex-snapshot
Replica-exchange molecular dynamics method for protein folding
inferredcites →https://doi.org/10.1016/s0014-5793(02)02638-8openalex-snapshot
Methionine oxidation inhibits fibrillation of human α‐synuclein in vitro
inferredcites →https://doi.org/10.1016/s0021-9258(17)37129-6openalex-snapshot
Conformational polymorphism of the amyloidogenic and neurotoxic peptide homologous to residues 106-126 of the prion protein.
inferredcites →https://doi.org/10.1016/s0047-6374(01)00249-4openalex-snapshot
Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
inferredcites →https://doi.org/10.1016/s1387-3806(01)00517-6openalex-snapshot
Design of a new electrospray ion mobility mass spectrometer
inferredcites →https://doi.org/10.1021/bi051369+openalex-snapshot
Methionine Oxidation Interferes with Conversion of the Prion Protein into the Fibrillar Proteinase K-Resistant Conformation
inferredcites →https://doi.org/10.1021/bi8009339openalex-snapshot
Methionine Oxidation Inhibits Assembly and Promotes Disassembly of Apolipoprotein C-II Amyloid Fibrils
inferredcites →https://doi.org/10.1021/j100133a011openalex-snapshot
Carbon cluster cations with up to 84 atoms: structures, formation mechanism, and reactivity
inferredcites →https://doi.org/10.1021/ja044531popenalex-snapshot
Amyloid β-Protein: Monomer Structure and Early Aggregation States of Aβ42 and Its Pro 19 Alloform
inferredcites →https://doi.org/10.1021/ja051699hopenalex-snapshot
A Strand-Loop-Strand Structure Is a Possible Intermediate in Fibril Elongation: Long Time Simulations of Amyloid-β Peptide (10−35)
inferredcites →https://doi.org/10.1021/jp052722oopenalex-snapshot
Conformational Polymorphism of the PrP106−126 Peptide in Different Environments: A Molecular Dynamics Study
inferredcites →https://doi.org/10.1021/jp055568eopenalex-snapshot
Amyloid β-Peptide Oligomerization in S ilico : Dimer and Trimer
inferredcites →https://doi.org/10.1021/jp076450wopenalex-snapshot
Computational Study on the Structural Diversity of Amyloid Beta Peptide (Aβ10-35) Oligomers
inferredcites →https://doi.org/10.1021/jp800282xopenalex-snapshot
A Test on Peptide Stability of AMBER Force Fields with Implicit Solvation
inferredcites →https://doi.org/10.1021/jp801175wopenalex-snapshot
Spermine Binding to Parkinson’s Protein α-Synuclein and Its Disease-Related A30P and A53T Mutants
inferredcites →https://doi.org/10.1021/jp961623vopenalex-snapshot
Structural Information from Ion Mobility Measurements: Effects of the Long-Range Potential
inferredcites →https://doi.org/10.1038/362543a0openalex-snapshot
Neurotoxicity of a prion protein fragment
inferredcites →https://doi.org/10.1038/380345a0openalex-snapshot
Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
inferredcites →https://doi.org/10.1038/nchem.247openalex-snapshot
Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease
inferredcites →https://doi.org/10.1038/nm0797-750openalex-snapshot
Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an α-helix
inferredcites →https://doi.org/10.1038/nprot.2006.202openalex-snapshot
Using circular dichroism spectra to estimate protein secondary structure
inferredcites →https://doi.org/10.1039/b407928kopenalex-snapshot
Conformational properties of peptide fragments homologous to the 106–114 and 106–126 residues of the human prion protein: a CD and NMR spectroscopic study
inferredcites →https://doi.org/10.1042/0264-6021:3420207openalex-snapshot
Molecular determinants of the physicochemical properties of a critical prion protein region comprising residues 106‒126
inferredcites →https://doi.org/10.1046/j.1432-1327.1999.00985.xopenalex-snapshot
Determination of solution conformations of PrP106–126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics
inferredcites →https://doi.org/10.1046/j.1471-4159.1999.0731557.xopenalex-snapshot
The Hydrophobic Core Sequence Modulates the Neurotoxic and Secondary Structure Properties of the Prion Peptide 106‐126
inferredcites →https://doi.org/10.1063/1.448118openalex-snapshot
Molecular dynamics with coupling to an external bath
inferredcites →https://doi.org/10.1073/pnas.0703700104openalex-snapshot
Protein folding by zipping and assembly
inferredcites →https://doi.org/10.1073/pnas.2433563100openalex-snapshot
NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106–126
inferredcites →https://doi.org/10.1073/pnas.90.20.9678openalex-snapshot
Synthetic peptides homologous to prion protein residues 106-147 form amyloid-like fibrils in vitro.
inferredcites →https://doi.org/10.1073/pnas.90.23.10962openalex-snapshot
Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
inferredcites →https://doi.org/10.1073/pnas.93.26.15457openalex-snapshot
Recombinant scrapie-like prion protein of 106 amino acids is soluble
inferredcites →https://doi.org/10.1074/jbc.c000579200openalex-snapshot
In Vivo Cytotoxicity of the Prion Protein Fragment 106–126
inferredcites →https://doi.org/10.1074/jbc.c200338200openalex-snapshot
Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Aβ-(1–42) Peptide of Alzheimer's Disease
inferredcites →https://doi.org/10.1074/jbc.m500210200openalex-snapshot
Amidation and Structure Relaxation Abolish the Neurotoxicity of the Prion Peptide PrP106–126 in Vivo and in Vitro
inferredcites →https://doi.org/10.1080/00268979400101241openalex-snapshot
Multiple time scale methods for constant pressure molecular dynamics simulations of molecular systems
inferredcites →https://doi.org/10.1097/00001756-199410270-00017openalex-snapshot
Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
inferredcites →https://doi.org/10.1103/physrevlett.57.2607openalex-snapshot
Replica Monte Carlo Simulation of Spin-Glasses
inferredcites →https://doi.org/10.1110/ps.051762406openalex-snapshot
Amyloid β‐protein monomer structure: A computational and experimental study
inferredcites →https://doi.org/10.1111/j.1742-4658.2006.05532.xopenalex-snapshot
Oxidation inhibits amyloid fibril formation of transthyretin
inferredcites →https://doi.org/10.1126/science.1675487openalex-snapshot
Molecular Biology of Prion Diseases
inferredcites →https://doi.org/10.1143/jpsj.65.1604openalex-snapshot
Exchange Monte Carlo Method and Application to Spin Glass Simulations
inferredcites →https://doi.org/10.1146/annurev.biochem.75.101304.123901openalex-snapshot
Protein Misfolding, Functional Amyloid, and Human Disease
inferredcites →https://doi.org/10.1523/jneurosci.23-02-00462.2003openalex-snapshot
In VivoandIn VitroNeurotoxicity of the Human Prion Protein (PrP) Fragment P118–135 Independently of PrP Expression
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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inferred← citeshttps://doi.org/10.1016/j.biocel.2011.01.022openalex-snapshot
Heat shock protein 104 inhibited the fibrillization of prion peptide 106–126 and disassembled prion peptide 106–126 fibrils in vitro
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β-Turn exchanges in the α-synuclein segment 44-TKEG-47 reveal high sequence fidelity requirements of amyloid fibril elongation
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