scholarly article | Q13442814 |
review article | Q7318358 |
P2093 | author name string | Anthony L Fink | |
P433 | issue | 9 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Synuclein | Q24767155 |
fibrillation | Q1001150 | ||
P304 | page(s) | 628-634 | |
P577 | publication date | 2006-09-01 | |
P1433 | published in | Accounts of Chemical Research | Q899474 |
P1476 | title | The aggregation and fibrillation of alpha-synuclein | |
P478 | volume | 39 |
Q41840011 | 19F NMR studies of alpha-synuclein conformation and fibrillation |
Q42055565 | A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation |
Q96126454 | A nanobody-based fluorescent reporter reveals human α-synuclein in the cell cytosol |
Q30838501 | A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity |
Q35840376 | A novel resource for studying function and dysfunction of α-synuclein: mouse lines for modulation of endogenous Snca gene expression. |
Q36398309 | A polymer physics perspective on driving forces and mechanisms for protein aggregation |
Q42366153 | A study on the modulation of alpha-synuclein fibrillation by Scutellaria pinnatifida extracts and its neuroprotective properties |
Q35863939 | Aggregation of αSynuclein promotes progressive in vivo neurotoxicity in adult rat dopaminergic neurons |
Q46687858 | Alpha-Synuclein Fibrils Interact with Dopamine Reducing its Cytotoxicity on PC12 Cells. |
Q57821667 | Alpha-Synuclein Modulates the Physical Properties of DNA |
Q41875033 | Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation |
Q38618665 | Alpha-synuclein in alpha-helical conformation at air-water interface: implication of conformation and orientation changes during its accumulation/aggregation |
Q35150090 | Alpha-synuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases |
Q90731164 | Alterations in the nigrostriatal system following conditional inactivation of α-synuclein in neurons of adult and aging mice |
Q30481562 | At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation |
Q35806485 | Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts |
Q30421397 | Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature? |
Q34020622 | Baicalein reduces E46K alpha-synuclein aggregation in vitro and protects cells against E46K alpha-synuclein toxicity in cell models of familiar Parkinsonism. |
Q33665421 | Binding of alpha-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes. |
Q33470625 | Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein |
Q37605018 | Brain iron homeostasis: from molecular mechanisms to clinical significance and therapeutic opportunities |
Q46844887 | Changes in interfacial properties of alpha-synuclein preceding its aggregation |
Q43256880 | Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein |
Q28831283 | Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein |
Q30379490 | Clearance and phosphorylation of alpha-synuclein are inhibited in methionine sulfoxide reductase a null yeast cells. |
Q36107686 | Common structural features of toxic intermediates from α-synuclein and GroES fibrillogenesis detected using cryogenic coherent X-ray diffraction imaging. |
Q60912226 | Computational insights into the role of α-strand/sheet in aggregation of α-synuclein |
Q41256282 | Conformational dynamics of α-synuclein: insights from mass spectrometry |
Q64123712 | Conservation of the Amyloid Interactome Across Diverse Fibrillar Structures |
Q39774554 | Converse modulation of toxic alpha-synuclein oligomers in living cells by N'-benzylidene-benzohydrazide derivates and ferric iron |
Q42131522 | Conversion of natively unstructured α-synuclein to its α-helical conformation significantly attenuates production of reactive oxygen species |
Q59600524 | Copper chaperone blocks amyloid formation via ternary complex |
Q41876014 | Could α-synuclein amyloid-like aggregates trigger a prionic neuronal invasion? |
Q34524912 | Covalent α-synuclein dimers: chemico-physical and aggregation properties |
Q46069820 | Creation of aggregation-defective α-synuclein variants by engineering the sequence connecting β-strand-forming domains |
Q37431675 | Crowded cell-like environment accelerates the nucleation step of amyloidogenic protein misfolding. |
Q42014258 | Cu(II) promotes amyloid pore formation |
Q61446034 | Dementia with Lewy bodies: an update and outlook |
Q38542133 | Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state |
Q54257505 | Detection of amyloid fibrils in Parkinson's disease using plasmonic chirality. |
Q53244268 | Detection of oligomers and fibrils of α-synuclein by AIEgen with strong fluorescence. |
Q64093661 | Differential Aggregation and Phosphorylation of Alpha Synuclein in Membrane Compartments Associated With Parkinson Disease |
Q90319955 | Differential effects of Cu2+ and Fe3+ ions on in vitro amyloid formation of biologically-relevant α-synuclein variants |
Q21132346 | Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy |
Q28392011 | Dopamine and paraquat enhance α-synuclein-induced alterations in membrane conductance |
Q41865629 | Drug Targeting of alpha-Synuclein Oligomerization in Synucleinopathies |
Q35994848 | Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering |
Q40155070 | Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein |
Q64054875 | Dysregulated Lipid Metabolism and Its Role in α-Synucleinopathy in Parkinson's Disease |
Q47147437 | EGCG-mediated Protection of the Membrane Disruption and Cytotoxicity Caused by the 'Active Oligomer' of α-Synuclein |
Q33550002 | Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change. |
Q33665675 | Effect of dioxygen on copper(II) binding to alpha-synuclein. |
Q46390730 | Effects of oxidation, pH and lipids on amyloidogenic peptide structure: implications for fibril formation? |
Q39293862 | Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein |
Q41879283 | Electron paramagnetic resonance spectroscopy measures the distance between the external β-strands of folded α-synuclein in amyloid fibrils |
Q34994184 | Elevated alpha-synuclein impairs innate immune cell function and provides a potential peripheral biomarker for Parkinson's disease |
Q41837154 | Elucidating the aggregation number of dopamine-induced α-synuclein oligomeric assemblies |
Q39485110 | Explaining the structural plasticity of α-synuclein |
Q26852660 | Exploring the accessible conformations of N-terminal acetylated α-synuclein |
Q41664033 | Facile methodology for monitoring amyloid-β fibrillization |
Q39027293 | Familial Mutations May Switch Conformational Preferences in α-Synuclein Fibrils |
Q35199433 | Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein |
Q92623198 | Folding of copper proteins: role of the metal? |
Q28472448 | Formation of toxic oligomeric alpha-synuclein species in living cells |
Q27026292 | Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence |
Q64866213 | Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils |
Q33399100 | Granular assembly of alpha-synuclein leading to the accelerated amyloid fibril formation with shear stress |
Q34170760 | Hsp70 and its molecular role in nervous system diseases |
Q30354048 | Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces |
Q36631756 | Hydrodynamic size-based separation and characterization of protein aggregates from total cell lysates |
Q41314313 | Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli |
Q37302816 | Immune-directed gene therapeutic development for Alzheimer's, prion, and Parkinson's diseases |
Q36939712 | In vitro study of α-synuclein protofibrils by cryo-EM suggests a Cu(2+)-dependent aggregation pathway |
Q64764829 | In-vitro and in-silico investigation of protective mechanisms of crocin against E46K α-synuclein amyloid formation |
Q46786568 | Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization |
Q24298231 | Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds |
Q33375727 | Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region |
Q44171513 | Inhibition of amyloid fibril growth and dissolution of amyloid fibrils by curcumin-gold nanoparticles. |
Q37577611 | Interaction between alpha-synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease. |
Q47270597 | Interfacial Properties of NTAIL, an Intrinsically Disordered Protein |
Q35548280 | Intracellular screening of a peptide library to derive a potent peptide inhibitor of α-synuclein aggregation |
Q36569512 | Intrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanopores |
Q90122841 | Investigating the Effects of O-GlcNAc Modifications in Parkinson's Disease Using Semisynthetic α-Synuclein |
Q36659034 | Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading |
Q34499321 | Kinetics of amyloid aggregation: a study of the GNNQQNY prion sequence |
Q33724346 | Lipid classes and fatty acid patterns are altered in the brain of γ-synuclein null mutant mice |
Q41065976 | Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation |
Q41908259 | Long-range distances in amyloid fibrils of α-synuclein from PELDOR spectroscopy |
Q37454199 | Low micromolar zinc accelerates the fibrillization of human tau via bridging of Cys-291 and Cys-322. |
Q34602533 | Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation |
Q30395345 | Macromolecular and Small Molecular Crowding Have Similar Effects on α-Synuclein Structure. |
Q33366459 | Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases |
Q36303237 | Mechanisms of protein fibril formation: nucleated polymerization with competing off-pathway aggregation |
Q35789622 | Mechanisms of protein oligomerization: inhibitor of functional amyloids templates α-synuclein fibrillation |
Q39640471 | Mega assemblages of oligomeric aerolysin-like toxins stabilized by toxin-associating membrane proteins |
Q33844949 | Metabolic Investigations of the Molecular Mechanisms Associated with Parkinson's Disease |
Q39274942 | Mimicking the plant cell interior under water stress by macromolecular crowding: disordered dehydrin proteins are highly resistant to structural collapse |
Q47677223 | Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation |
Q36872325 | Modulating the Amyloidogenesis of α-Synuclein |
Q33392127 | Modulation of alpha-synuclein expression in transgenic animals for modelling synucleinopathies--is the juice worth the squeeze? |
Q38213838 | Monoamine oxidase and α-synuclein as targets in Parkinson's disease therapy |
Q34074933 | Multifunctional D2/D3 agonist D-520 with high in vivo efficacy: modulator of toxicity of alpha-synuclein aggregates |
Q40778644 | Mutant alpha-synuclein overexpression mediates early proinflammatory activity |
Q40968608 | Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species |
Q37776219 | Nanoimaging for protein misfolding diseases |
Q39149504 | Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence |
Q37418238 | Neurochemical approaches in the laboratory diagnosis of Parkinson and Parkinson dementia syndromes: a review |
Q43206102 | Neurodegeneration and Cancer: Where the Disorder Prevails |
Q36200921 | O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease |
Q45937542 | O-GlcNAc modification inhibits the calpain-mediated cleavage of α-synuclein. |
Q39238586 | O-GlcNAc modification prevents peptide-dependent acceleration of α-synuclein aggregation |
Q45948370 | O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding. |
Q37182845 | On the key role played by altered protein conformation in Parkinson's disease |
Q38085689 | Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies. |
Q37045173 | Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity |
Q34002451 | Potential pharmacological chaperones targeting cancer-associated MCL-1 and Parkinson disease-associated α-synuclein |
Q34416878 | Probing the Micelle‐Bound Aggregation‐Prone State of α‐Synuclein with 19F NMR Spectroscopy |
Q90103351 | Propofol Attenuates α-Synuclein Aggregation and Neuronal Damage in a Mouse Model of Ischemic Stroke |
Q36982260 | Protein aggregation processes: In search of the mechanism |
Q37918059 | Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis |
Q89424515 | Real-time determination of aggregated alpha-synuclein induced membrane disruption at neuroblastoma cells using scanning ion conductance microscopy |
Q34999535 | Recent advances in our understanding of neurodegeneration |
Q38199448 | Redox control of enzymatic functions: The electronics of life's circuitry. |
Q42426545 | Redox reactions of the α-synuclein-Cu(2+) complex and their effects on neuronal cell viability |
Q92942837 | Reducing the Amyloidogenicity of Functional Amyloid Protein FapC Increases Its Ability To Inhibit α-Synuclein Fibrillation |
Q54787321 | Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting. |
Q37922607 | Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases |
Q37989861 | Role of the ubiquitin-proteasome system in nervous system function and disease: using C. elegans as a dissecting tool |
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