NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
about
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyDJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formationCa2+ binding to alpha-synuclein regulates ligand binding and oligomerizationAcceleration of alpha-synuclein aggregation by homologous peptidesDequalinium-induced protofibril formation of alpha-synucleinα-Synuclein as an intrinsically disordered monomer--fact or artefact?Interactions between fatty acids and alpha-synucleinMultiple system atrophy: cellular and molecular pathology.Alternative splicing in concert with protein intrinsic disorder enables increased functional diversity in multicellular organismsα-Synuclein occurs physiologically as a helically folded tetramer that resists aggregationSite-specific interaction between α-synuclein and membranes probed by NMR-observed methionine oxidation ratesIdentification, analysis, and prediction of protein ubiquitination sitesCurcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st centurySecondary structure and dynamics of micelle bound beta- and gamma-synucleinalpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodiesIntrabody and Parkinson's diseaseResidual structure, backbone dynamics, and interactions within the synuclein familyDisProt: the Database of Disordered ProteinsDefinition of a molecular pathway mediating α-synuclein neurotoxicityα-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formationProperties of native brain α-synucleinOrder, Disorder, and Everything in BetweenVersatile Structures of α-SynucleinDynamic structural flexibility of α-synucleinComputational approaches for inferring the functions of intrinsically disordered proteinsRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biophysical characterization of α-synuclein and its controversial structureMultiple system atrophy: a clinical and neuropathological perspectiveExploring the accessible conformations of N-terminal acetylated α-synucleinWhat macromolecular crowding can do to a proteinFunction and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescenceNeuropathology in mice expressing mouse alpha-synucleinRNA chaperoning and intrinsic disorder in the core proteins of FlaviviridaeComparison of anionic and cationic trypsinogens: The anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structureThe Arabidopsis COP9 Signalosome Subunit 7 Is a Model PCI Domain Protein with Subdomains Involved in COP9 Signalosome AssemblyStructural Basis of Molecular Recognition of the Leishmania Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) at Membrane SurfacesThe Synaptic Function of α-SynucleinAlpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicityYGR198w (YPP1) targets A30P alpha-synuclein to the vacuole for degradation.
P2860
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P2860
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
@en
type
label
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
@en
prefLabel
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
@en
P2093
P356
P1433
P1476
NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded.
@en
P2093
P304
13709-13715
P356
10.1021/BI961799N
P407
P577
1996-10-01T00:00:00Z