Seeding specificity in amyloid growth induced by heterologous fibrils.
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Molecular cross talk between misfolded proteins in animal models of Alzheimer's and prion diseasesNeuroendocrine hormone amylin in diabetesAssessing the causes and consequences of co-polymerization in amyloid formationCross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseasesOn the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP PeptidesPhage display and peptide mapping of an immunoglobulin light chain fibril-related conformational epitopeThe catalytic domain of insulin-degrading enzyme forms a denaturant-resistant complex with amyloid beta peptide: implications for Alzheimer disease pathogenesisDisassembly of shank and homer synaptic clusters is driven by soluble beta-amyloid(1-40) through divergent NMDAR-dependent signalling pathwaysBridging Type 2 Diabetes and Alzheimer's Disease: Assembling the Puzzle Pieces in the Quest for the Molecules With Therapeutic and Preventive Potentialβ-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 modelDynamics 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 formationIn-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 cytoskeletonCurli provide the template for understanding controlled amyloid propagationpolyglutamine aggregation nucleation: thermodynamics of a highly unfavorable protein folding reactionSensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanolsVascular 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 brainNoncerebral Amyloidoses: Aspects on Seeding, Cross-Seeding, and Transmission.The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspectiveSerine protease HtrA1 accumulates in corneal transforming growth factor beta induced protein (TGFBIp) amyloid depositsObservations 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 proteinsMutational analysis of preamyloid intermediates: the role of his-tyr interactions in islet amyloid formationGeneral 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 atrophyLocalization of a conformational epitope common to non-native and fibrillar immunoglobulin light chains.
P2860
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P2860
Seeding specificity in amyloid growth induced by heterologous fibrils.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
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
P2093
P2860
P356
P1476
Seeding specificity in amyloid growth induced by heterologous fibrils.
@en
P2093
Angela D Williams
Brian O'Nuallain
Per Westermark
Ronald Wetzel
P2860
P304
17490-17499
P356
10.1074/JBC.M311300200
P407
P577
2004-01-29T00:00:00Z