Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.
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An atomic model for the pleated beta-sheet structure of abeta amyloid protofilamentsElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsSupramolecular structure in full-length Alzheimer's beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance.Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMRA structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMRThe effect of a DeltaK280 mutation on the unfolded state of a microtubule-binding repeat in TauUltrafast colorimetric determination of predominant protein structure evolution with gold nanoplasmonic particles.Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (A beta 1-40), which may potentially inhibit the fibril formation.Amyloid fibers are water-filled nanotubes.Mechanisms of enzymatic degradation of amyloid Beta microfibrils generating nanofilaments and nanospheres related to cytotoxicity.Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filamentsAmyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths.Theoretical models of the ion channel structure of amyloid beta-protein.In situ characterization of beta-amyloid in Alzheimer's diseased tissue by synchrotron Fourier transform infrared microspectroscopyPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils.Amyloid structure: conformational diversity and consequences.Molecular organization of amyloid protofilament-like assembly of betabellin 15D: helical array of beta-sandwiches.Tetrameric assembly of full-sequence protein zero myelin glycoprotein by synchrotron x-ray scatteringA general model for amyloid fibril assembly based on morphological studies using atomic force microscopy.Biomimetic organization: Octapeptide self-assembly into nanotubes of viral capsid-like dimension.Structure of core domain of fibril-forming PHF/Tau fragments.Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects.Mutational analysis of the structural organization of polyglutamine aggregates.The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant.Physiopathological modulators of amyloid aggregation and novel pharmacological approaches in Alzheimer's disease.Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition.Molecular alignment within beta-sheets in Abeta(14-23) fibrils: solid-state NMR experiments and theoretical predictions.The solubilization of model Alzheimer tangles: reversing the beta-sheet conformation induced by aluminum with silicatesThe environmental dependency of protein folding best explains prion and amyloid diseases.Breakdown of hierarchical architecture in cellulose during dilute acid pretreatmentsDisaggregation of Alzheimer beta-amyloid by site-directed mAb.Doxycycline hinders phenylalanine fibril assemblies revealing a potential novel therapeutic approach in phenylketonuriaFibril formation from the amyloid-β peptide is governed by a dynamic equilibrium involving association and dissociation of the monomer.In situ atomic force microscopy study of Alzheimer's beta-amyloid peptide on different substrates: new insights into mechanism of beta-sheet formationModulating amyloid self-assembly and fibril morphology with Zn(II)Controlling amyloid growth in multiple dimensions.Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy.Toward understanding amyloid aggregationAmyloid structure exhibits polymorphism on multiple length scales in human brain tissue.
P2860
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P2860
Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.
description
1993 nî lūn-bûn
@nan
1993 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@ast
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@en
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@nl
type
label
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@ast
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@en
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@nl
prefLabel
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@ast
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@en
Structure of beta-crystallite ...... analysis by x-ray diffraction.
@nl
P2860
P921
P1433
P1476
Structure of beta-crystallite ...... analysis by x-ray diffraction
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(93)81393-6
P407
P577
1993-02-01T00:00:00Z