Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein

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Intrinsically disordered protein

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Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe

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Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. Wright

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Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein

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Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation

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Identification of two distinct synucleins from human brain

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α-Synuclein Fibrillogenesis Is Nucleation-dependent

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Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein Aggregation

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Effect of Familial Parkinson's Disease Point Mutations A30P and A53T on the Structural Properties, Aggregation, and Fibrillation of Human α-Synuclein

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Mutant and Wild Type Human α-Synucleins Assemble into Elongated Filaments with Distinct Morphologies in Vitro

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Synthetic filaments assembled from C‐terminally truncated α‐synuclein

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Forcing Thermodynamically Unfolded Proteins to Fold

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Pesticides directly accelerate the rate of α‐synuclein fibril formation: a possible factor in Parkinson's disease

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Fatal attractions: abnormal protein aggregation and neuron death in Parkinson's disease and Lewy body dementia

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Association-induced folding of globular proteins

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Association of partially‐folded intermediates of staphylococcal nuclease induces structure and stability

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A Wide-Bandpass Multilayer Monochromator for Biological Small-Angle Scattering and Fiber Diffraction Studies

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Small-angle x-ray scattering/diffraction system for studies of biological and other materials at the Stanford Synchrotron Radiation Laboratory (abstract)a)

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Conformational constraints for amyloid fibrillation: the importance of being unfolded

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Implication of Trimethylamine N-Oxide (TMAO) in Disease: Potential Biomarker or New Therapeutic Target

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Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation

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What Macromolecular Crowding Can Do to a Protein

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Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: α-Synuclein

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Investigating the Trimethylamine N-Oxide (TMAO) Induced Structure of α-Synuclein

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Osmolyte Trimethylamine N-Oxide Converts Recombinant α-Helical Prion Protein to its Soluble β-Structured Form at High Temperature

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Osmolyte-induced folding of the intrinsically disordered protein alpha-synuclein

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The osmolyte trimethylamine‐N‐oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

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The Addition of an Osmolyte, Trimethylamine N-Oxide Promotes Secondary Structure Heterogeneity Among Amyloid Fibrils

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