Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.
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Facilitated aggregation of FG nucleoporins under molecular crowding conditionsIntrinsically disordered proteins are potential drug targetsTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environmentThe Surprising Role of Amyloid Fibrils in HIV InfectionAmyloid fibers provide structural integrity to Bacillus subtilis biofilms.Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneThe amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.Residue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assemblyAn accessory protein required for anchoring and assembly of amyloid fibres in B. subtilis biofilms.Fairy "tails": flexibility and function of intrinsically disordered extensions in the photosynthetic world.The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A.Nanoimaging for protein misfolding diseases.Drug targets from genetics: α-synuclein.Intrinsically disordered proteins and novel strategies for drug discovery.Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.Promising in Vitro anti-Alzheimer Properties for a Ruthenium(III) Complex.Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein.Amyloid and Alzheimer's disease.Dynamic domains of amyloid fibrils can be site-specifically assigned with proton detected 3D NMR spectroscopyHow disorder influences order and vice versa--mutual effects in fusion proteins containing an intrinsically disordered and a globular protein.Is there a biological cost of protein disorder? Analysis of cancer-associated mutationsHelD, an RNA Polymerase Interacting Helicase, Forms Amyloid-Like Fibrils
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P2860
Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 27 August 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Structural disorder in amyloid ...... amic interactions of proteins.
@en
Structural disorder in amyloid ...... amic interactions of proteins.
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type
label
Structural disorder in amyloid ...... amic interactions of proteins.
@en
Structural disorder in amyloid ...... amic interactions of proteins.
@nl
prefLabel
Structural disorder in amyloid ...... amic interactions of proteins.
@en
Structural disorder in amyloid ...... amic interactions of proteins.
@nl
P2860
P1433
P1476
Structural disorder in amyloid ...... amic interactions of proteins.
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P2093
P2860
P304
P356
10.1111/J.1742-4658.2009.07250.X
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P577
2009-08-27T00:00:00Z