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Meredith, Stephen C.
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Meredith, Stephen C.
Protein Structure, Secondary
Two-dimensional structure of beta-amyloid(10-35) fibrils.
Inhibition of beta-amyloid(40) fibrillogenesis and disassembly of beta-amyloid(40) fibrils by short beta-amyloid congeners containing N-methyl amino acids at alternate residues.
Structure-function relationships in side chain lactam cross-linked peptide models of a conserved N-terminal domain of apolipoprotein E.
Supramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.
Apolipoprotein A-I alpha -helices 7 and 8 modulate high density lipoprotein subclass distribution.
A designed Zn2+-binding amphiphilic polypeptide: energetic consequences of pi-helicity.
Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel.
Peptide-based inhibitors of amyloid assembly.
Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils.
Chaperone-like N-methyl peptide inhibitors of polyglutamine aggregation.
Spatial separation of beta-sheet domains of beta-amyloid: disruption of each beta-sheet by N-methyl amino acids.
Mechanism of cis-inhibition of polyQ fibrillation by polyP: PPII oligomers and the hydrophobic effect.
The Japanese mutant Aß (?E22-Aß(1-39)) forms fibrils instantaneously, with low-thioflavin T fluorescence: seeding of wild-type Aß(1-40) into atypical fibrils by ?E22-Aß(1-39).
Helix-turn-helix peptides that form alpha-helical fibrils: turn sequences drive fibril structure.
Structural and thermodynamic characterization of a bioactive peptide model of apolipoprotein E: side-chain lactam bridges to constrain the conformation.
Structure of substrate-free human insulin-degrading enzyme (IDE) and biophysical analysis of ATP-induced conformational switch of IDE.
High-resolution structure of a self-assembly-competent form of a hydrophobic peptide captured in a soluble beta-sheet scaffold.
The specific amino acid sequence between helices 7 and 8 influences the binding specificity of human apolipoprotein A-I for high density lipoprotein (HDL) subclasses: a potential for HDL preferential generation.
Molecular basis of substrate recognition and degradation by human presequence protease.
Elucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation.
Protein Structure Secondary