Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease.
about
CLAC binds to amyloid beta peptides through the positively charged amino acid cluster within the collagenous domain 1 and inhibits formation of amyloid fibrilsHuman serum albumin inhibits Abeta fibrillization through a "monomer-competitor" mechanismEffects of grape seed-derived polyphenols on amyloid beta-protein self-assembly and cytotoxicityMolecular basis for insulin fibril assemblySimilar promotion of Abeta1-42 fibrillogenesis by native apolipoprotein E epsilon3 and epsilon4 isoformsThe amyloid hypothesis of Alzheimer's disease at 25 yearsApolipoprotein E and apolipoprotein E receptors: normal biology and roles in Alzheimer diseaseInflammation and Alzheimer's diseaseUV-light exposed prion protein fails to form amyloid fibrilsThe binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.Intrinsic fibrillation of fast-acting insulin analogs.Selection of peptides binding to the amyloid b-protein reveals potential inhibitors of amyloid formation.Interactions between amyloid-β and hemoglobin: implications for amyloid plaque formation in Alzheimer's disease.Pseudophosphorylation and glycation of tau protein enhance but do not trigger fibrillization in vitro.Opposite roles of apolipoprotein E in normal brains and in Alzheimer's disease.Discovery of a brain promoter from the human transferrin gene and its utilization for development of transgenic mice that express human apolipoprotein E alleles.Identification and expression analysis of a potential familial Alzheimer disease gene on chromosome 1 related to AD3.Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's disease.Non-esterified fatty acids generate distinct low-molecular weight amyloid-β (Aβ42) oligomers along pathway different from fibril formationGenetic dissection of Alzheimer disease, a heterogeneous disorder.Astrocyte lipoproteins, effects of apoE on neuronal function, and role of apoE in amyloid-beta deposition in vivo.Influence of lipoproteins on microglial degradation of Alzheimer's amyloid beta-protein.The Alzheimer's A beta -peptide is deposited at sites of complement activation in pathologic deposits associated with aging and age-related macular degeneration.Pseudophosphorylation of tau protein directly modulates its aggregation kinetics.The role of apolipoprotein E in Alzheimer's disease.Physiopathological modulators of amyloid aggregation and novel pharmacological approaches in Alzheimer's disease.Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity.Structural complexity of a composite amyloid fibril.Follow-up plasma apolipoprotein E levels in the Australian Imaging, Biomarkers and Lifestyle Flagship Study of Ageing (AIBL) cohort.Age of onset in Huntington disease: sex specific influence of apolipoprotein E genotype and normal CAG repeat length.A three-stage kinetic model of amyloid fibrillation.Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion.Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.Tau isoform composition influences rate and extent of filament formationMeasurement of apolipoprotein E and amyloid β clearance rates in the mouse brain using bolus stable isotope labeling.Molecular interactions in the formation and deposition of beta2-microglobulin-related amyloid fibrils.Kinetic theory of fibrillogenesis of amyloid beta-protein.Apolipoprotein E, especially apolipoprotein E4, increases the oligomerization of amyloid β peptide.In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formationInhibition of amyloid peptide fibrillation by inorganic nanoparticles: functional similarities with proteins
P2860
Q24328940-391BB6C8-69FA-436D-8543-D8BE6D196976Q24646788-E4C27836-C923-4BFF-B085-8C9B88C42BFCQ24657235-FB82CDCE-3C0A-4E44-BBFA-8F1B1A928BAFQ24657505-6BBC1F44-E9E0-48EC-A8A3-F5D248443A6CQ24805441-03D4E4F7-2A95-456F-B3A9-6B0069F956FAQ26749528-C8FE59C2-449B-4E50-846D-AEED735DFA53Q26858870-30F21C51-9947-4558-8A3B-F0DE04AD637CQ28138617-1D2DC13B-0EA6-465D-88B5-46C622DB9E13Q28473110-D2E4B6E5-11A0-4429-83D3-3967ABA09C33Q30032680-60579432-D9E6-485A-A611-03FBAEB2CF9BQ30416114-C5C0E6DD-086E-45B9-9B33-152395D8CB35Q30805913-3C6059C0-4E96-4162-89B3-16F2A62F1291Q31050722-4C928C94-B7C8-4DF6-979C-8E74248D9D8CQ31111749-406AE712-5B80-4D71-803C-AB502E68598BQ31949934-C3733CD3-86A0-484D-8805-2578D8CDEBBFQ33648946-F1DF317E-AC3B-4836-AF82-B5A4F5077398Q33653843-9D8A38FC-D59A-4F4C-841E-660C78E74E57Q33718596-024728F9-0F66-4F13-A99C-3E416F9815AFQ33883804-EFEEC2BA-2D15-405F-BAE3-A93A95169657Q33909158-D807AAAB-48DD-4CA4-8D80-0EB1297C3C3FQ33998681-3056F020-EB2B-4003-A72A-D2DB6CB2F5A6Q33998693-CC10B0D2-E36D-46E8-B6D9-91F85C827630Q34154466-DBB1C3E5-1B96-46D2-ABF7-F06B896E52D6Q34478697-3877A743-80B6-4428-850A-6EDD94C97E72Q34603092-17190B5B-D852-4136-951E-425406F524D8Q34721350-EA8B6266-7069-44FD-8E7A-AE965FC55B4AQ34938739-30A25E97-DE35-4C43-87B6-48CDCAD90F1EQ35302543-D099F39F-16D9-4394-8890-92D3B2235CDAQ35342893-9442883F-5FFE-44AB-A3C4-764CC3F2D0DDQ35431655-219B4A32-319F-40E3-9F38-50C71F2E344AQ35753756-242FBDD0-E037-4C90-B029-6F3C464DBB67Q35917933-F5B75542-A8C3-4181-A673-EEA86777CBB1Q35922618-3D570B38-299B-4565-A842-D77AB56AF326Q36017002-7D667627-ED1D-416B-9EB3-4F473C58DA58Q36118225-C8AA78C0-C0F2-4456-9BC5-456BD5E52F7FQ36217094-7ACB9834-D6AE-467B-88DF-56C687BC2339Q36298130-18DBE7B0-B319-4817-8E83-4D7B5F7A91AEQ36384642-8552728C-C88B-48B8-A83C-CBE7BF4B160AQ36448995-1292F140-77B9-4672-B0B4-F513D6D39F33Q36452430-1BF7D7C0-4DC4-4861-A6B2-1E7D56838D24
P2860
Apolipoprotein E is a kinetic but not a thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@ast
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@en
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@nl
type
label
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@ast
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@en
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@nl
prefLabel
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@ast
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@en
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@nl
P2093
P2860
P356
P1476
Apolipoprotein E is a kinetic ...... reatment of Alzheimer disease.
@en
P2093
E P Berger
K H Weisgraber
P T Lansbury
P2860
P304
P356
10.1073/PNAS.92.3.763
P407
P577
1995-01-01T00:00:00Z