Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q33817987

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Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopy Conformational equilibria in monomeric alpha-synuclein at the single-molecule level Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein protein The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease Residual structure, backbone dynamics, and interactions within the synuclein family Dynamic structural flexibility of α-synuclein Mechanisms of amyloid formation revealed by solution NMR Electrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomics QM/MM molecular dynamics studies of metal binding proteins Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biophysical characterization of α-synuclein and its controversial structure Exploring the accessible conformations of N-terminal acetylated α-synuclein Intrinsically disordered -subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein Peptide Investigation of Homeodomain Membrane Translocation Properties: Insights from the Structure Determination of Engrailed-2 Homeodomain in Aqueous and Membrane-Mimetic Environments Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings Sequestration of a β-hairpin for control of α-synuclein aggregation The contribution of alpha synuclein to neuronal survival and function - Implications for Parkinson's disease Structural polymorphism of 441-residue tau at single residue resolution Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence In-cell NMR characterization of the secondary structure populations of a disordered conformation of α-synuclein within E. coli cells Targeting the intrinsically disordered structural ensemble of α-synuclein by small molecules as a potential therapeutic strategy for Parkinson's disease Effects of Mutations on the Reconfiguration Rate of α-Synuclein Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain.NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein.Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.Macromolecular and Small Molecular Crowding Have Similar Effects on α-Synuclein Structure.MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions.Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?Methionine oxidation stabilizes non-toxic oligomers of alpha-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions Average conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.The Chemistry of Neurodegeneration: Kinetic Data and Their Implications.

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P2860

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

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Release of long-range tertiary ...... y unstructured alpha-synuclein

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Release of long-range tertiary ...... y unstructured alpha-synuclein

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Release of long-range tertiary ...... y unstructured alpha-synuclein

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Proceedings of the National Academy of Sciences of the United States of America

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Release of long-range tertiary ...... y unstructured alpha-synuclein

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Carlos W Bertoncini

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Christian Griesinger

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Claudio O Fernandez

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Young-Sang Jung

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P2860

Alpha-synuclein in Lewy bodies

The Xplor-NIH NMR molecular structure determination package

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

MOLMOL: a program for display and analysis of macromolecular structures

NMR View: A computer program for the visualization and analysis of NMR data

Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra

Alpha-synuclein and neurodegenerative diseases

Protein folding and misfolding

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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