The oligomerization mediated by the alanine 397 residue in the transmembrane domain is crucial to sydecan-3 functions.
Sign Up to like & getrecommendations! Published in 2020 at "Cellular signalling"
DOI: 10.1016/j.cellsig.2020.109544
Abstract: Syndecans are single-pass transmembrane proteins on the cell surface that are involved in various cellular functions. Previously, we reported that both homo- and hetero-form of syndecan dimers affected their functionality. However, little is known about… read more here.
Keywords: transmembrane; alanine 397; transmembrane domain; oligomer formation ... See more keywords
On the Applicability of Force Fields To Study the Aggregation of Amyloidogenic Peptides Using Molecular Dynamics Simulations.
Sign Up to like & getrecommendations! Published in 2018 at "Journal of chemical theory and computation"
DOI: 10.1021/acs.jctc.8b00579
Abstract: Molecular dynamics simulations play an essential role in understanding biomolecular processes such as protein aggregation at temporal and spatial resolutions which are not attainable by experimental methods. For a correct modeling of protein aggregation, force… read more here.
Keywords: aggregation; molecular dynamics; oligomer formation; force ... See more keywords
Oligomer Formation Propensities of Dimeric Bundle Peptides Correlate with Cell Penetration Abilities
Sign Up to like & getrecommendations! Published in 2018 at "ACS Central Science"
DOI: 10.1021/acscentsci.8b00262
Abstract: LK-3, an amphipathic dimeric peptide linked by two disulfide bonds, and related isomeric bundles were synthesized, and their cell penetrating abilities were investigated. The measurements using size exclusion chromatography and dynamic light scattering show that… read more here.
Keywords: cell penetration; cell penetrating; cell; oligomer formation ... See more keywords
Monosialotetrahexosylganglioside Promotes Early Aβ42 Oligomer Formation and Maintenance.
Sign Up to like & getrecommendations! Published in 2022 at "ACS chemical neuroscience"
DOI: 10.1021/acschemneuro.2c00221
Abstract: The aggregation of the amyloid beta (Aβ) peptide is associated with Alzheimer's disease (AD) pathogenesis. Cell membrane composition, especially monosialotetrahexosylganglioside (GM1), is known to promote the formation of Aβ fibrils, yet little is known about… read more here.
Keywords: formation; early oligomer; formation maintenance; oligomer formation ... See more keywords
Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer’s Disease
Sign Up to like & getrecommendations! Published in 2022 at "Molecules"
DOI: 10.3390/molecules27248804
Abstract: The brains of Alzheimer’s disease (AD) patients contain numerous amyloid plaques that are diagnostic of the disease. The plaques are primarily composed of the amyloidogenic peptides proteins Aβ40 and Aβ42, which are derived by the… read more here.
Keywords: membrane mimicking; disease; alzheimer disease; amyloid membrane ... See more keywords