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Extent of N-terminus exposure by altered long-range interactions of monomeric alpha-synuclein determines its aggregation propensity

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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/ana.10795openalex-snapshot

The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia

inferredcites →https://doi.org/10.1002/ana.23894openalex-snapshot

G51D α‐synuclein mutation causes a novel Parkinsonian–pyramidal syndrome

inferredcites →https://doi.org/10.1002/anie.201309001openalex-snapshot

Sequestration of a β‐Hairpin for Control of α‐Synuclein Aggregation

inferredcites →https://doi.org/10.1002/anie.201503018openalex-snapshot

Contact between the β1 and β2 Segments of α‐Synuclein that Inhibits Amyloid Formation

inferredcites →https://doi.org/10.1002/cbic.200800581openalex-snapshot

Pathogenic Mutations Shift the Equilibria of α‐Synuclein Single Molecules towards Structured Conformers

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/10.1002/pro.149openalex-snapshot

Charge neutralization and collapse of the C‐terminal tail of alpha‐synuclein at low pH

inferredcites →https://doi.org/10.1002/pro.3412openalex-snapshot

Exploring the role of post‐translational modifications in regulating α‐synuclein interactions by studying the effects of phosphorylation on nanobody binding

inferredcites →https://doi.org/10.1002/prot.22604openalex-snapshot

Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: Conformational heterogeneity of α‐synuclein

inferredcites →https://doi.org/10.1006/jmbi.2001.4538openalex-snapshot

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

inferredcites →https://doi.org/10.1007/978-1-4939-2978-8_1openalex-snapshot

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

inferredcites →https://doi.org/10.1007/s13361-018-2002-2openalex-snapshot

Native Top-Down Mass Spectrometry and Ion Mobility MS for Characterizing the Cobalt and Manganese Metal Binding of α-Synuclein Protein

inferredcites →https://doi.org/10.1016/j.bbadis.2008.07.004openalex-snapshot

Impact of Tyr to Ala mutations on α-synuclein fibrillation and structural properties

inferredcites →https://doi.org/10.1016/j.bbadis.2009.12.004openalex-snapshot

Methionine oxidation stabilizes non-toxic oligomers of α-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions

inferredcites →https://doi.org/10.1016/j.bpj.2013.07.044openalex-snapshot

Identification of Fibril-Like Tertiary Contacts in Soluble Monomeric α-Synuclein

inferredcites →https://doi.org/10.1016/j.bpj.2017.08.027openalex-snapshot

Modification of C Terminus Provides New Insights into the Mechanism of α-Synuclein Aggregation

inferredcites →https://doi.org/10.1016/j.ceca.2009.12.003openalex-snapshot

Calcium, cellular aging, and selective neuronal vulnerability in Parkinson's disease

inferredcites →https://doi.org/10.1016/j.jasms.2004.08.003openalex-snapshot

α-Synuclein: Stable compact and extended monomeric structures and pH dependence of dimer formation

inferredcites →https://doi.org/10.1016/j.jmb.2007.07.008openalex-snapshot

Residual Structure, Backbone Dynamics, and Interactions within the Synuclein Family

inferredcites →https://doi.org/10.1016/j.jmb.2009.06.063openalex-snapshot

Structural Reorganization of α-Synuclein at Low pH Observed by NMR and REMD Simulations

inferredcites →https://doi.org/10.1016/j.jmb.2011.05.046openalex-snapshot

Conserved C-Terminal Charge Exerts a Profound Influence on the Aggregation Rate of α-Synuclein

inferredcites →https://doi.org/10.1016/j.mcp.2016.11.001openalex-snapshot

Genetics of Parkinson's disease

inferredcites →https://doi.org/10.1016/j.neurobiolaging.2014.03.024openalex-snapshot

A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology

inferredcites →https://doi.org/10.1016/j.tcb.2017.02.002openalex-snapshot

α-Synuclein – Regulator of Exocytosis, Endocytosis, or Both?

inferredcites →https://doi.org/10.1016/j.tibs.2018.11.005openalex-snapshot

The Cellular Environment Affects Monomeric α-Synuclein Structure

inferredcites →https://doi.org/10.1021/acs.analchem.6b00731openalex-snapshot

Opposite Structural Effects of Epigallocatechin-3-gallate and Dopamine Binding to α-Synuclein

inferredcites →https://doi.org/10.1021/acs.analchem.8b01264openalex-snapshot

Different Structural Conformers of Monomeric α-Synuclein Identified after Lyophilizing and Freezing

inferredcites →https://doi.org/10.1021/acschemneuro.7b00149openalex-snapshot

Perturbation in Long-Range Contacts Modulates the Kinetics of Amyloid Formation in α-Synuclein Familial Mutants

inferredcites →https://doi.org/10.1021/acschemneuro.8b00052openalex-snapshot

Pulsed Hydrogen–Deuterium Exchange Illuminates the Aggregation Kinetics of α-Synuclein, the Causative Agent for Parkinson’s Disease

inferredcites →https://doi.org/10.1021/bi020429yopenalex-snapshot

The N-Terminal Repeat Domain of α-Synuclein Inhibits β-Sheet and Amyloid Fibril Formation

inferredcites →https://doi.org/10.1021/bi027363ropenalex-snapshot

Role of α-Synuclein Carboxy-Terminus on Fibril Formation in Vitro

inferredcites →https://doi.org/10.1021/bi1010927openalex-snapshot

The Conformation and the Aggregation Kinetics of α-Synuclein Depend on the Proline Residues in Its C-Terminal Region

inferredcites →https://doi.org/10.1021/bi401037zopenalex-snapshot

α-Synuclein Misfolding Assessed with Single Molecule AFM Force Spectroscopy: Effect of Pathogenic Mutations

inferredcites →https://doi.org/10.1021/bi401427topenalex-snapshot

A Four-Amino Acid Linker between Repeats in the α-Synuclein Sequence Is Important for Fibril Formation

inferredcites →https://doi.org/10.1021/bi5010365openalex-snapshot

The Newly Discovered Parkinson’s Disease Associated Finnish Mutation (A53E) Attenuates α-Synuclein Aggregation and Membrane Binding

inferredcites →https://doi.org/10.1021/cn200074dopenalex-snapshot

Phosphorylation of α-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of α-Synuclein in the Pathogenesis of Parkinson’s Disease and Related Disorders

inferredcites →https://doi.org/10.1021/cn300198qopenalex-snapshot

Structures and Free Energy Landscapes of the Wild-Type and A30P Mutant-Type α-Synuclein Proteins with Dynamics

inferredcites →https://doi.org/10.1021/cn3002027openalex-snapshot

Structures of the E46K Mutant-Type α-Synuclein Protein and Impact of E46K Mutation on the Structures of the Wild-Type α-Synuclein Protein

inferredcites →https://doi.org/10.1021/ja044834jopenalex-snapshot

Mapping Long-Range Interactions in α-Synuclein using Spin-Label NMR and Ensemble Molecular Dynamics Simulations

inferredcites →https://doi.org/10.1021/ja0618649openalex-snapshot

Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement

inferredcites →https://doi.org/10.1021/ja9105495openalex-snapshot

Detection of Transient Interchain Interactions in the Intrinsically Disordered Protein α-Synuclein by NMR Paramagnetic Relaxation Enhancement

inferredcites →https://doi.org/10.1038/ncb748openalex-snapshot

α-Synuclein is phosphorylated in synucleinopathy lesions

inferredcites →https://doi.org/10.1038/nchembio.1750openalex-snapshot

Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation

inferredcites →https://doi.org/10.1038/ncomms12563openalex-snapshot

Structural basis of synaptic vesicle assembly promoted by α-synuclein

inferredcites →https://doi.org/10.1038/ng0298-106openalex-snapshot

AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

inferredcites →https://doi.org/10.1038/nn.4529openalex-snapshot

α-Synuclein promotes dilation of the exocytotic fusion pore

inferredcites →https://doi.org/10.1038/s41467-018-03111-4openalex-snapshot

C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction

inferredcites →https://doi.org/10.1038/s41593-019-0423-2openalex-snapshot

Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes

inferredcites →https://doi.org/10.1038/s41598-018-20320-5openalex-snapshot

Molecular Role of Ca2+ and Hard Divalent Metal Cations on Accelerated Fibrillation and Interfibrillar Aggregation of α-Synuclein

inferredcites →https://doi.org/10.1038/srep41051openalex-snapshot

Evidence for Intramolecular Antiparallel Beta-Sheet Structure in Alpha-Synuclein Fibrils from a Combination of Two-Dimensional Infrared Spectroscopy and Atomic Force Microscopy

inferredcites →https://doi.org/10.1039/b926659copenalex-snapshot

Metalloproteomics and metal toxicology of α-synuclein

inferredcites →https://doi.org/10.1039/c7cc09597jopenalex-snapshot

Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

inferredcites →https://doi.org/10.1073/pnas.0407146102openalex-snapshot

Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

inferredcites →https://doi.org/10.1073/pnas.0507405102openalex-snapshot

Structure and properties of α-synuclein and other amyloids determined at the amino acid level

inferredcites →https://doi.org/10.1073/pnas.0809232106openalex-snapshot

Interplay of α-synuclein binding and conformational switching probed by single-molecule fluorescence

inferredcites →https://doi.org/10.1073/pnas.1604645113openalex-snapshot

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation

inferredcites →https://doi.org/10.1074/jbc.c500288200openalex-snapshot

Familial Mutants of α-Synuclein with Increased Neurotoxicity Have a Destabilized Conformation

inferredcites →https://doi.org/10.1074/jbc.m008919200openalex-snapshot

A Hydrophobic Stretch of 12 Amino Acid Residues in the Middle of α-Synuclein Is Essential for Filament Assembly

inferredcites →https://doi.org/10.1074/jbc.m010907200openalex-snapshot

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

inferredcites →https://doi.org/10.1074/jbc.m101181200openalex-snapshot

Ca2+ Binding to α-Synuclein Regulates Ligand Binding and Oligomerization

inferredcites →https://doi.org/10.1074/jbc.m106777200openalex-snapshot

Residual Structure and Dynamics in Parkinson's Disease-associated Mutants of α-Synuclein

inferredcites →https://doi.org/10.1074/jbc.m109541200openalex-snapshot

Biophysical Properties of the Synucleins and Their Propensities to Fibrillate

inferredcites →https://doi.org/10.1074/jbc.m112.383711openalex-snapshot

Characterization of Semisynthetic and Naturally Nα-Acetylated α-Synuclein in Vitro and in Intact Cells

inferredcites →https://doi.org/10.1074/jbc.m115.705095openalex-snapshot

Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization

inferredcites →https://doi.org/10.1074/jbc.m117.795617openalex-snapshot

Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T

inferredcites →https://doi.org/10.1074/jbc.m600933200openalex-snapshot

Phosphorylation of Ser-129 Is the Dominant Pathological Modification of α-Synuclein in Familial and Sporadic Lewy Body Disease

inferredcites →https://doi.org/10.1074/jbc.m800747200openalex-snapshot

Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

inferredcites →https://doi.org/10.1101/500058openalex-snapshot

The making of a Lewy body: the role of alpha-synuclein post-fibrillization modifications in regulating the formation and the maturation of pathological inclusions.

inferredcites →https://doi.org/10.1126/science.276.5321.2045openalex-snapshot

Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease

inferredcites →https://doi.org/10.1186/s13024-020-00380-wopenalex-snapshot

Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein

inferredcites →https://doi.org/10.1371/journal.pcbi.1006859openalex-snapshot

Conformational ensemble of native α-synuclein in solution as determined by short-distance crosslinking constraint-guided discrete molecular dynamics simulations

inferredcites →https://doi.org/10.7554/elife.46112openalex-snapshot

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.jmb.2021.166878openalex-snapshot

Brazilin Removes Toxic Alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium

inferred← citeshttps://doi.org/10.1021/acs.analchem.6c00544openalex-snapshot

Nanopipettes Enable Native Mass Spectrometry Studies of the Intrinsically Disordered Protein α-Synuclein in Biochemical Buffers

inferred← citeshttps://doi.org/10.1038/s41467-021-21027-4openalex-snapshot

The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition

inferred← citeshttps://doi.org/10.3389/fneur.2021.661117openalex-snapshot

Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications

inferred← citeshttps://doi.org/10.70675/b306d45azfd69z4b88z80c0z948cf17c885copenalex-snapshot

Dynamics of pathological aggregates and fibers

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