Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils.
about
Self-propagation of pathogenic protein aggregates in neurodegenerative diseasesCross-seeding of misfolded proteins: implications for etiology and pathogenesis of protein misfolding diseasesGenesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion diseaseConformational switching within individual amyloid fibrils.Structural typing of systemic amyloidoses by luminescent-conjugated polymer spectroscopy.The irreversible binding of amyloid peptide substrates to insulin-degrading enzyme: a biological perspectiveC-terminal sequence of amyloid-resistant type F apolipoprotein A-II inhibits amyloid fibril formation of apolipoprotein A-II in mice.Caloric restriction reduces the systemic progression of mouse AApoAII amyloidosis.Switching in amyloid structure within individual fibrils: implication for strain adaptation, species barrier and strain classificationAnimal models of human amyloidoses: are transgenic mice worth the time and trouble?The amyloid interactome: Exploring protein aggregation.The amyloid state of proteins in human diseases.Molecular interaction between type 2 diabetes and Alzheimer's disease through cross-seeding of protein misfolding.Interfacial interaction and lateral association of cross-seeding assemblies between hIAPP and rIAPP oligomers.Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.Extracellular environment modulates the formation and propagation of particular amyloid structures.Bidirectional transcripts of the expanded C9orf72 hexanucleotide repeat are translated into aggregating dipeptide repeat proteins.Amyloidosis-inducing activity of blood cells in mouse AApoAII amyloidosis.Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules.Highly promiscuous nature of prion polymerization.Apolipoprotein A-II accelerates reactive AA amyloidosis.Apolipoprotein A-II induces acute-phase response associated AA amyloidosis in mice through conformational changes of plasma lipoprotein structure.AA amyloidosis-resistant CE/J mice haveSaa1andSaa2genes that encode an identical SAA isoformProtein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification
P2860
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P2860
Cross-seeding and cross-competition in mouse apolipoprotein A-II amyloid fibrils and protein A amyloid fibrils.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@en
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@nl
type
label
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@en
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@nl
prefLabel
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@en
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@nl
P2093
P2860
P1476
Cross-seeding and cross-compet ...... and protein A amyloid fibrils.
@en
P2093
Beiru Zhang
Fengxia Ge
Hironobu Naiki
Hiroshi Tomozawa
Huanyu Zhang
Jingmin Yan
Jinko Sawashita
Jinze Qian
Junjie Yao
Keiichi Higuchi
P2860
P304
P356
10.2353/AJPATH.2007.060576
P407
P577
2007-07-01T00:00:00Z