Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. - Wikidata - awgldk - TriplyDB

Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

http://www.wikidata.org/entity/Q43203312

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Ubiquitous amyloids The effect of the cosolvent trifluoroethanol on a tryptophan side chain orientation in the hydrophobic core of troponin C Conformational Conversion during Amyloid Formation at Atomic Resolution Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Structural insights into the aggregation behavior of Murraya koenigii miraculin-like protein below pH 7.5 Identification of fibrillogenic regions in human triosephosphate isomerase.The model of amyloid aggregation of Escherichia coli RNA polymerase σ70 subunit based on AFM data and in vitro assays.Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Influence of the stability of a fused protein and its distance to the amyloidogenic segment on fibril formation.Crowding alone cannot account for cosolute effect on amyloid aggregation High-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119.Describing sequence-ensemble relationships for intrinsically disordered proteins.Potential therapeutic strategies for Alzheimer's disease targeting or beyond β-amyloid: insights from clinical trials In vitro aggregation behavior of a non-amyloidogenic λ light chain dimer deriving from U266 multiple myeloma cells.Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1 Prion protein misfolding.Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.Quantitative Analyses of Force-Induced Amyloid Formation in Candida albicans Als5p: Activation by Standard Laboratory Procedures.A desolvation model for trifluoroethanol-induced aggregation of enhanced green fluorescent protein.Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulations Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules A common beta-sheet architecture underlies in vitro and in vivo beta2-microglobulin amyloid fibrils Continuous dissolution of structure during the unfolding of a small protein.Molecular simulations of protein disorder.Biochemical and biophysical features of both oligomer/fibril and cell membrane in amyloid cytotoxicity.Treatment strategies targeting amyloid β-protein.Autophagy protein p62/SQSTM1 is involved in HAMLET-induced cell death by modulating apotosis in U87MG cells Force Sensitivity in Saccharomyces cerevisiae Flocculins.Function, structure, and stability of enzymes confined in agarose gels.The importance of a gatekeeper residue on the aggregation of transthyretin: implications for transthyretin-related amyloidoses Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein.Using empirical phase diagrams to understand the role of intramolecular dynamics in immunoglobulin G stability Insights into the disparate action of osmolytes and macromolecular crowders on amyloid formation.Existence of different structural intermediates on the fibrillation pathway of human serum albumin.Trifluoroethanol modulates amyloid formation by the all α-helical URN1 FF domain.Kinetic analysis of amyloid formation in the presence of heparan sulfate: faster unfolding and change of pathway Amyloid formation in denatured single-mutant lysozymes where residual structures are modulated.Fibril growth kinetics reveal a region of beta2-microglobulin important for nucleation and elongation of aggregation.Shear flow promotes amyloid-{beta} fibrilization.

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P2860

Amyloid fibril formation can proceed from different conformations of a partially unfolded protein.

http://www.wikidata.org/entity/Q43203312

description

2005 nî lūn-bûn

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Amyloid fibril formation can p ...... a partially unfolded protein.

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BIOPHYSJ.105.068726

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Biophysical Journal

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Amyloid fibril formation can p ...... a partially unfolded protein.

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P2093

Fabrizio Chiti

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P2860

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Tertiary structures of amyloidogenic and non-amyloidogenic transthyretin variants: new model for amyloid fibril formation

The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state

Protein folding and misfolding

Ultrastructural organization of amyloid fibrils by atomic force microscopy.

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

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4201-4210

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scholarly article

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10.1529/BIOPHYSJ.105.068726

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6

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89

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Martino Calamai

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2005-09-16T00:00:00Z

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7593733

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16169975

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Acylphosphatase

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