Pages that link to "Q28487771"

The following pages link to Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K (Q28487771):

Displaying 28 items.

• Post translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease (Q33776138) (← links)
• The H50Q mutation induces a 10-fold decrease in the solubility of α-synuclein. (Q35002998) (← links)
• Amyloid polymorphism: structural basis and neurobiological relevance (Q35586308) (← links)
• High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR. (Q36217985) (← links)
• Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants (Q36298004) (← links)
• Potential Role of Caffeine in the Treatment of Parkinson's Disease (Q37129378) (← links)
• Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. (Q37278078) (← links)
• Biophysical groundwork as a hinge to unravel the biology of α-synuclein aggregation and toxicity (Q38180144) (← links)
• α-Synuclein Misfolding Versus Aggregation Relevance to Parkinson's Disease: Critical Assessment and Modeling (Q38241438) (← links)
• The effects of pdr1, djr1.1 and pink1 loss in manganese-induced toxicity and the role of α-synuclein in C. elegans (Q38279572) (← links)
• MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images (Q38381825) (← links)
• ɑ-Synuclein strains and the variable pathologies of synucleinopathies (Q38753941) (← links)
• Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils (Q39027293) (← links)
• The Contribution of α-Synuclein Spreading to Parkinson's Disease Synaptopathy (Q39108546) (← links)
• Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence (Q39149504) (← links)
• Irisflorentin improves α-synuclein accumulation and attenuates 6-OHDA-induced dopaminergic neuron degeneration, implication for Parkinson's disease therapy (Q41369321) (← links)
• In vitro aggregation assays for the characterization of α-synuclein prion-like properties. (Q41821396) (← links)
• A sensitive assay reveals structural requirements for α-synuclein fibril growth. (Q47580400) (← links)
• A Protofilament-Protofilament Interface in the Structure of Mouse α-Synuclein Fibrils (Q57181907) (← links)
• Physiological carboxy-truncation of α-synuclein potentiates the prion-like formation of pathological inclusions (Q57458019) (← links)
• Computational insights into the role of α-strand/sheet in aggregation of α-synuclein (Q60912226) (← links)
• Mechanisms of Strain Diversity of Disease-Associated in-Register Parallel β-Sheet Amyloids and Implications About Prion Strains (Q64251983) (← links)
• Phase transitions and structure analysis in wild-type, A30P, E46K, and A53T mutants of α-synuclein (Q86957603) (← links)
• The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure (Q89517784) (← links)
• Synaptic vesicle mimics affect the aggregation of wild-type and A53T α-synuclein variants differently albeit similar membrane affinity (Q90362291) (← links)
• Navigating the dynamic landscape of alpha-synuclein morphology: a review of the physiologically relevant tetrameric conformation (Q90396213) (← links)
• Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs (Q91152187) (← links)
• Parkinson's disease associated mutation E46K of α-synuclein triggers the formation of a distinct fibril structure (Q95840158) (← links)