Residual structure, backbone dynamics, and interactions within the synuclein family
about
The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicityIntrinsically disordered proteins in a physics-based worldExploring the accessible conformations of N-terminal acetylated α-synucleinMyosin Binding Protein C Positioned to Play a Key Role in Regulation of Muscle Contraction: Structure and Interactions of Domain C1Structural polymorphism of 441-residue tau at single residue resolutionMechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescenceInvestigation of intramolecular dynamics and conformations of α-, β- and γ-synucleinExamining protein surface structure in highly conserved sequence variants with mass spectrometry.Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?Protein structure evolution in liquid DESI as revealed by selective noncovalent adduct protein probing.Gamma-synucleinopathy: neurodegeneration associated with overexpression of the mouse protein.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactionsAn introduction to biological NMR spectroscopy.Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopyThe amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.The lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Expanding the proteome: disordered and alternatively folded proteins.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomerA relationship between the transient structure in the monomeric state and the aggregation propensities of α-synuclein and β-synucleinLife-time expression of the proteins peroxiredoxin, beta-synuclein, PARK7/DJ-1, and stathmin in the primary visual and primary somatosensory cortices in rats.Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2.Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein.Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein.Oligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).The conformational ensembles of α-synuclein and tau: combining single-molecule FRET and simulations.Contrasting effects of α-synuclein and γ-synuclein on the phenotype of cysteine string protein α (CSPα) null mutant mice suggest distinct function of these proteins in neuronal synapses.Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits.Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopyBiophysical characterization of intrinsically disordered proteins.Folding and misfolding of alpha-synuclein on membranes.Hunting the chameleon: structural conformations of the intrinsically disordered protein alpha-synuclein.Role of the interdomain linker in distance determination for remote cleavage by homing endonuclease I-TevI.Identification of gamma-synuclein as a new PCBP1-interacting protein.Explaining the structural plasticity of α-synuclein.Investigation of the Polymeric Properties of α-Synuclein and Comparison with NMR Experiments: A Replica Exchange Molecular Dynamics Study.Hydrogen exchange of monomeric alpha-synuclein shows unfolded structure persists at physiological temperature and is independent of molecular crowding in Escherichia coli.19F NMR studies of alpha-synuclein conformation and fibrillationCharacterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation.
P2860
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P2860
Residual structure, backbone dynamics, and interactions within the synuclein family
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Residual structure, backbone dynamics, and interactions within the synuclein family
@ast
Residual structure, backbone dynamics, and interactions within the synuclein family
@en
Residual structure, backbone dynamics, and interactions within the synuclein family
@nl
type
label
Residual structure, backbone dynamics, and interactions within the synuclein family
@ast
Residual structure, backbone dynamics, and interactions within the synuclein family
@en
Residual structure, backbone dynamics, and interactions within the synuclein family
@nl
prefLabel
Residual structure, backbone dynamics, and interactions within the synuclein family
@ast
Residual structure, backbone dynamics, and interactions within the synuclein family
@en
Residual structure, backbone dynamics, and interactions within the synuclein family
@nl
P2860
P1476
Residual structure, backbone dynamics, and interactions within the synuclein family
@en
P2093
David Eliezer
Yoon-Hui Sung
P2860
P304
P356
10.1016/J.JMB.2007.07.008
P407
P577
2007-09-21T00:00:00Z