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Heme minimizes Parkinson’s disease-associated toxicity by inducing a conformational distortion in the oligomers of alpha-Synuclein
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/(sici)1097-0320(19980101)31:1<1::aid-cyto1>3.0.co;2-ropenalex-snapshot
Annexin V-Affinity assay: A review on an apoptosis detection system based on phosphatidylserine exposure
inferredcites →https://doi.org/10.1002/jcc.20084openalex-snapshot
UCSF Chimera—A visualization system for exploratory research and analysis
inferredcites →https://doi.org/10.1002/mds.25421openalex-snapshot
Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease
inferredcites →https://doi.org/10.1007/978-1-4757-3061-6openalex-snapshot
Principles of Fluorescence Spectroscopy
inferredcites →https://doi.org/10.1016/0079-6107(93)90006-6openalex-snapshot
Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy
inferredcites →https://doi.org/10.1016/0263-7855(96)00018-5openalex-snapshot
VMD: Visual molecular dynamics
inferredcites →https://doi.org/10.1016/j.bbamem.2009.03.010openalex-snapshot
Lipid bilayer disruption by oligomeric α-synuclein depends on bilayer charge and accessibility of the hydrophobic core
inferredcites →https://doi.org/10.1016/j.jmb.2008.03.017openalex-snapshot
Characterization of Conformational and Dynamic Properties of Natively Unfolded Human and Mouse α-Synuclein Ensembles by NMR: Implication for Aggregation
inferredcites →https://doi.org/10.1016/j.jsb.2004.06.006openalex-snapshot
XMIPP: a new generation of an open-source image processing package for electron microscopy
inferredcites →https://doi.org/10.1016/j.jsb.2006.05.009openalex-snapshot
EMAN2: An extensible image processing suite for electron microscopy
inferredcites →https://doi.org/10.1016/j.jsb.2012.09.006openalex-snapshot
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
inferredcites →https://doi.org/10.1016/j.ymeth.2009.04.005openalex-snapshot
Molecular dynamics flexible fitting: A practical guide to combine cryo-electron microscopy and X-ray crystallography
inferredcites →https://doi.org/10.1016/s0022-2836(02)00735-0openalex-snapshot
α-Synuclein, Especially the Parkinson's Disease-associated Mutants, Forms Pore-like Annular and Tubular Protofibrils
inferredcites →https://doi.org/10.1016/s0076-6879(99)09020-5openalex-snapshot
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
inferredcites →https://doi.org/10.1021/acs.biochem.5b00280openalex-snapshot
Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation
inferredcites →https://doi.org/10.1021/acschemneuro.8b00436openalex-snapshot
Conformational-Switch Based Strategy Triggered by [18] π Heteroannulenes toward Reduction of Alpha Synuclein Oligomer Toxicity
inferredcites →https://doi.org/10.1021/acschemneuro.9b00090openalex-snapshot
Cryo-Electron Microscopy Uncovers Key Residues within the Core of Alpha-Synuclein Fibrils
inferredcites →https://doi.org/10.1021/bi0102398openalex-snapshot
Vesicle Permeabilization by Protofibrillar α-Synuclein: Implications for the Pathogenesis and Treatment of Parkinson's Disease
inferredcites →https://doi.org/10.1021/bi0260841openalex-snapshot
Peroxidase Activity as a Tool for Studying the Folding of c -Type Cytochromes
inferredcites →https://doi.org/10.1021/cn500168xopenalex-snapshot
Early Sodium Dodecyl Sulfate Induced Collapse of α-Synuclein Correlates with Its Amyloid Formation
inferredcites →https://doi.org/10.1021/ja1084578openalex-snapshot
Active Site Environment of Heme-Bound Amyloid β Peptide Associated with Alzheimer’s Disease
inferredcites →https://doi.org/10.1021/la503749eopenalex-snapshot
Attenuation of the Early Events of α-Synuclein Aggregation: A Fluorescence Correlation Spectroscopy and Laser Scanning Microscopy Study in the Presence of Surface-Coated Fe3O4Nanoparticles
inferredcites →https://doi.org/10.1038/399a032openalex-snapshot
Prospects for new restorative and neuroprotective treatments in Parkinson's disease
inferredcites →https://doi.org/10.1038/nature10324openalex-snapshot
α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
inferredcites →https://doi.org/10.1038/nchembio.283openalex-snapshot
A causative link between the structure of aberrant protein oligomers and their toxicity
inferredcites →https://doi.org/10.1038/ncomms6857openalex-snapshot
Small molecule-mediated stabilization of vesicle-associated helical α-synuclein inhibits pathogenic misfolding and aggregation
inferredcites →https://doi.org/10.1038/nprot.2007.452openalex-snapshot
Preparation of macromolecular complexes for cryo-electron microscopy
inferredcites →https://doi.org/10.1038/nprot.2007.474openalex-snapshot
Visualization of macromolecular complexes using cryo-electron microscopy with FEI Tecnai transmission electron microscopes
inferredcites →https://doi.org/10.1038/nprot.2008.156openalex-snapshot
SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
inferredcites →https://doi.org/10.1038/nsmb.3194openalex-snapshot
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
inferredcites →https://doi.org/10.1038/s41422-018-0075-xopenalex-snapshot
Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy
inferredcites →https://doi.org/10.1038/s41467-018-05971-2openalex-snapshot
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
inferredcites →https://doi.org/10.1042/bj20090379openalex-snapshot
Antiparallel β-sheet: a signature structure of the oligomeric amyloid β-peptide
inferredcites →https://doi.org/10.1042/bj20111924openalex-snapshot
Toxic prefibrillar α-synuclein amyloid oligomers adopt a distinctive antiparallel β-sheet structure
inferredcites →https://doi.org/10.1073/pnas.0502066102openalex-snapshot
Amyloid ion channels: A common structural link for protein-misfolding disease
inferredcites →https://doi.org/10.1073/pnas.0908005106openalex-snapshot
Exogenous α-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells
inferredcites →https://doi.org/10.1073/pnas.1100976108openalex-snapshot
In vivo demonstration that α-synuclein oligomers are toxic
inferredcites →https://doi.org/10.1073/pnas.1113260108openalex-snapshot
A soluble α-synuclein construct forms a dynamic tetramer
inferredcites →https://doi.org/10.1073/pnas.1421204112openalex-snapshot
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation
inferredcites →https://doi.org/10.1073/pnas.1524128113openalex-snapshot
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading
inferredcites →https://doi.org/10.1074/jbc.m111.242958openalex-snapshot
Toward the Discovery of Effective Polycyclic Inhibitors of α-Synuclein Amyloid Assembly
inferredcites →https://doi.org/10.1103/physreve.89.032712openalex-snapshot
Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters
inferredcites →https://doi.org/10.1111/j.1582-4934.2010.01239.xopenalex-snapshot
A comparison of the biochemical modifications caused by toxic and non‐toxic protein oligomers in cells
inferredcites →https://doi.org/10.1126/science.1079469openalex-snapshot
Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis
inferredcites →https://doi.org/10.1126/science.aan6160openalex-snapshot
Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
inferredcites →https://doi.org/10.1146/annurev.biophys.31.082901.134202openalex-snapshot
Single-Particle Imaging of Macromolecules by Cryo-Electron Microscopy
inferredcites →https://doi.org/10.1371/journal.pgen.1006098openalex-snapshot
C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease
inferredcites →https://doi.org/10.1371/journal.pone.0039465openalex-snapshot
Alpha-Synuclein Cell-to-Cell Transfer and Seeding in Grafted Dopaminergic Neurons In Vivo
inferredcites →https://doi.org/10.18632/oncotarget.7046openalex-snapshot
Neuronal hemoglobin in mitochondria is reduced by forming a complex with α-synuclein in aging monkey brains
inferredcites →https://doi.org/10.2174/156720508784533312openalex-snapshot
Amyloidogenesis of Natively Unfolded Proteins
inferredcites →https://doi.org/10.7554/elife.36402openalex-snapshot
Cryo-EM structure of alpha-synuclein fibrils
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1007/978-981-15-5530-5_10openalex-snapshot
Protein Folding, Dynamics and Aggregation at Single-Molecule Resolution
inferred← citeshttps://doi.org/10.1016/j.abb.2021.109022openalex-snapshot
Influence of in vitro neuronal membranes on the anti-amyloidogenic activity of gallic acid: Implication for the therapy of Alzheimer's disease
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2021.08.198openalex-snapshot
Caffeic acid for the prevention and treatment of Alzheimer's disease: The effect of lipid membranes on the inhibition of aggregation and disruption of Aβ fibrils
inferred← citeshttps://doi.org/10.1021/acschemneuro.1c00210openalex-snapshot
Vitamin B12 Inhibits Aβ Fibrillation and Disaggregates Preformed Fibrils in the Presence of Synthetic Neuronal Membranes
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