Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Effect of amino-acid substitutions on Alzheimer's amyloid-beta peptide-glycosaminoglycan interactions.

European journal of biochemistry - 1 Nov 2000

McLaurin J, Fraser P E

Abstract excerpt

One of the major clinical features of Alzheimer's disease is the presence of extracellular amyloid plaques that are associated with glycosaminoglycan-containing proteoglycans. It has been proposed that proteoglycans and glycosaminoglycans facilitate amyloid fibril formation and/or stabilize these aggregates. Characterization of proteoglycan-protein interactions has suggested that basic amino acids in a specific...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alanine
Share to Chondroitin Sulfates
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosaminoglycans

Share to Heparin

Share to Hydrogen Bonding

Share to Protein Structure, Quaternary

Share to Static Electricity

Source

Identifiers

PMID: 11029577
DOI: 10.1046/j.1432-1327.2000.01725.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of amino-acid substitutions on Alzheimer's amyloid-beta peptide-glycosaminoglycan interactions.PMID 11029577Read ↗

Effects of the mutations Glu22 to Gln and Ala21 to Gly on the aggregation of a synthetic fragment of the Alzheimer's amyloid beta/A4 peptide.Semantic proximity Read ↗

Key charged residues influence the amyloidogenic propensity of the helix-1 region of serum amyloid A.Semantic proximity Read ↗

Molecular characterization of the β-amyloid(4-10) epitope of plaque specific Aβ antibodies by affinity-mass spectrometry using alanine site mutation.Semantic proximity Read ↗

The structure analysis of Humanin analog, AGA-(C8R)HNG17, by circular dichroism and sedimentation equilibrium: comparison with the parent molecule.Semantic proximity Read ↗

Structural preferences of neuroprotective S14G-humanin peptide analyzed by molecular modeling and circular dichroism.Semantic proximity Read ↗

Effects of Familial Alzheimer's Disease Mutations on the Assembly of a β-Hairpin Peptide Derived from Aβ16-36.Semantic proximity Read ↗

Conformational Characterization of Native and L17A/F19A-Substituted Dutch-Type β-Amyloid Peptides.Semantic proximity Read ↗

Comparative analysis of human and Dutch-type Alzheimer beta-amyloid peptides by infrared spectroscopy and circular dichroism.Semantic proximity Read ↗

Using chiral peptide substitutions to probe the structure function relationship of a key residue of Aβ42.Semantic proximity Read ↗

L17A/F19A Substitutions Augment the α-Helicity of β-Amyloid Peptide Discordant Segment.Semantic proximity Read ↗

Solution structures in aqueous SDS micelles of two amyloid beta peptides of A beta(1-28) mutated at the alpha-secretase cleavage site (K16E, K16F).Semantic proximity Read ↗

Prevention of peptide fibril formation in an aqueous environment by mutation of a single residue to Aib.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.