Seeding specificity in amyloid growth induced by heterologous fibrils. - Wikidata - wikimedia - TriplyDB

Seeding specificity in amyloid growth induced by heterologous fibrils.

Seeding specificity in amyloid growth induced by heterologous fibrils.

http://www.wikidata.org/entity/Q44748898

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Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseases Neuroendocrine hormone amylin in diabetes Assessing the causes and consequences of co-polymerization in amyloid formation Cross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseases On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Phage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitope The catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesis Disassembly of shank and homer synaptic clusters is driven by soluble beta-amyloid(1-40) through divergent NMDAR-dependent signalling pathways Bridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive Potential β-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Conformational switching within individual amyloid fibrils.A scFv antibody targeting common oligomeric epitope has potential for treating several amyloidoses.Structural properties of Abeta protofibrils stabilized by a small molecule.Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease.Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts.The effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formation In-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Orthogonal cross-seeding: an approach to explore protein aggregates in living cells.CDK5 is essential for soluble amyloid β-induced degradation of GKAP and remodeling of the synaptic actin cytoskeleton Curli provide the template for understanding controlled amyloid propagation polyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reaction Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20 Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols Vascular and metabolic dysfunction in Alzheimer's disease: a review.Amylin deposition in the brain: A second amyloid in Alzheimer disease?A distinct subfraction of Aβ is responsible for the high-affinity Pittsburgh compound B-binding site in Alzheimer's disease brain Noncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspective Serine protease HtrA1 accumulates in corneal transforming growth factor beta induced protein (TGFBIp) amyloid deposits Observations in APP bitransgenic mice suggest that diffuse and compact plaques form via independent processes in Alzheimer's disease.Normal-repeat-length polyglutamine peptides accelerate aggregation nucleation and cytotoxicity of expanded polyglutamine proteins Mutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formation General amyloid inhibitors? A critical examination of the inhibition of IAPP amyloid formation by inositol stereoisomers.Heterologous aggregates promote de novo prion appearance via more than one mechanism.Amyloid polymorphism: structural basis and neurobiological relevance.Computational re-engineering of Amylin sequence with reduced amyloidogenic potential.Polyglutamine expansion alters the dynamics and molecular architecture of aggregates in dentatorubropallidoluysian atrophy Localization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.

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P2860

Seeding specificity in amyloid growth induced by heterologous fibrils.

http://www.wikidata.org/entity/Q44748898

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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name

Seeding specificity in amyloid growth induced by heterologous fibrils.

@en

Seeding specificity in amyloid growth induced by heterologous fibrils.

@nl

type

label

Seeding specificity in amyloid growth induced by heterologous fibrils.

@en

Seeding specificity in amyloid growth induced by heterologous fibrils.

@nl

prefLabel

Seeding specificity in amyloid growth induced by heterologous fibrils.

@en

Seeding specificity in amyloid growth induced by heterologous fibrils.

@nl

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Journal of Biological Chemistry

P1476

Seeding specificity in amyloid growth induced by heterologous fibrils.

@en

P2093

Angela D Williams

http://www.w3.org/2001/XMLSchema#string

Brian O'Nuallain

http://www.w3.org/2001/XMLSchema#string

Per Westermark

http://www.w3.org/2001/XMLSchema#string

Ronald Wetzel

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P2860

Solubilization and disaggregation of polyglutamine peptides

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation

Use of gene knockouts in cultured cells to study apoptosis.

Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23.

Fourteen and counting: unraveling trinucleotide repeat diseases.

Amyloid fibrils from muscle myoglobin.

Specificity in intracellular protein aggregation and inclusion body formation.

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17490-17499

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scholarly article

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10.1074/JBC.M311300200

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279

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