Matches in SemOpenAlex for { <https://semopenalex.org/work/W2914961812> ?p ?o ?g. }
Showing items 1 to 83 of
83
with 100 items per page.
- W2914961812 endingPage "492a" @default.
- W2914961812 startingPage "492a" @default.
- W2914961812 abstract "The aberrant folding of proteins leading to the formation of characteristic cross-β-sheet rich amyloid structures is implicated in the pathogenesis of a variety of debilitating diseases. In many cases, often depending upon amino acid composition, only a small segment of a large protein participates in amyloid core formation and is in fact capable of self-assembling into amyloid, independent of the rest of the protein. Therefore, such peptide fragments serve as useful model systems for protein aggregation studies. An important factor that has often been underestimated while using peptides to mimic full length protein, is the charge on the peptide termini. We have investigated the effect of the termini on aggregation of amyloidogenic peptides from microtubule associated intrinsically disordered protein Tau, implicated in Alzheimer's disease (AD) and Tauopathies. Unlike other amyloidogenic proteins, Tau is highly soluble and does not readily aggregate without anionic co-factors, such as heparin. Our experiments show that modification of the termini can drastically modulate the fibrillation of hexapeptide from repeat 3 (R3)-paired helical filament 6 (PHF6) and full length R3 of Tau, both with and without heparin. We found that even without heparin, PHF6 and R3 peptides that were capped at both the termini readily formed amyloid fibrils. In presence of heparin, only PHF6 with free termini and PHF6 with free N-terminus were unable to form fibrils. Our molecular dynamics simulations on PHF6 capping variants agree well with our experiments and provide insights into how terminal capping affects the self-assembly process. In addition to the effect of terminal capping on Tau fibrillation, we are also studying cross-interactions between peptides associated with AD and Type-2-diabetes, in order to understand the underlying link between these highly prevalent diseases. I will discuss some of our recent results from these studies." @default.
- W2914961812 created "2019-02-21" @default.
- W2914961812 creator A5007621409 @default.
- W2914961812 creator A5012132404 @default.
- W2914961812 creator A5027376067 @default.
- W2914961812 creator A5029066415 @default.
- W2914961812 creator A5033847316 @default.
- W2914961812 creator A5036970981 @default.
- W2914961812 creator A5047173012 @default.
- W2914961812 date "2019-02-01" @default.
- W2914961812 modified "2023-10-18" @default.
- W2914961812 title "Terminal Capping of Amyloidogenic Tau Fragments Modulates their Fibrillation Propensity" @default.
- W2914961812 doi "https://doi.org/10.1016/j.bpj.2018.11.2653" @default.
- W2914961812 hasPublicationYear "2019" @default.
- W2914961812 type Work @default.
- W2914961812 sameAs 2914961812 @default.
- W2914961812 citedByCount "0" @default.
- W2914961812 crossrefType "journal-article" @default.
- W2914961812 hasAuthorship W2914961812A5007621409 @default.
- W2914961812 hasAuthorship W2914961812A5012132404 @default.
- W2914961812 hasAuthorship W2914961812A5027376067 @default.
- W2914961812 hasAuthorship W2914961812A5029066415 @default.
- W2914961812 hasAuthorship W2914961812A5033847316 @default.
- W2914961812 hasAuthorship W2914961812A5036970981 @default.
- W2914961812 hasAuthorship W2914961812A5047173012 @default.
- W2914961812 hasBestOaLocation W29149618121 @default.
- W2914961812 hasConcept C119599485 @default.
- W2914961812 hasConcept C12554922 @default.
- W2914961812 hasConcept C127413603 @default.
- W2914961812 hasConcept C142724271 @default.
- W2914961812 hasConcept C179104552 @default.
- W2914961812 hasConcept C185592680 @default.
- W2914961812 hasConcept C204328495 @default.
- W2914961812 hasConcept C27523624 @default.
- W2914961812 hasConcept C2776545253 @default.
- W2914961812 hasConcept C2777633098 @default.
- W2914961812 hasConcept C2779134260 @default.
- W2914961812 hasConcept C2779281246 @default.
- W2914961812 hasConcept C2994168385 @default.
- W2914961812 hasConcept C3019447875 @default.
- W2914961812 hasConcept C55493867 @default.
- W2914961812 hasConcept C71924100 @default.
- W2914961812 hasConcept C86803240 @default.
- W2914961812 hasConcept C95444343 @default.
- W2914961812 hasConceptScore W2914961812C119599485 @default.
- W2914961812 hasConceptScore W2914961812C12554922 @default.
- W2914961812 hasConceptScore W2914961812C127413603 @default.
- W2914961812 hasConceptScore W2914961812C142724271 @default.
- W2914961812 hasConceptScore W2914961812C179104552 @default.
- W2914961812 hasConceptScore W2914961812C185592680 @default.
- W2914961812 hasConceptScore W2914961812C204328495 @default.
- W2914961812 hasConceptScore W2914961812C27523624 @default.
- W2914961812 hasConceptScore W2914961812C2776545253 @default.
- W2914961812 hasConceptScore W2914961812C2777633098 @default.
- W2914961812 hasConceptScore W2914961812C2779134260 @default.
- W2914961812 hasConceptScore W2914961812C2779281246 @default.
- W2914961812 hasConceptScore W2914961812C2994168385 @default.
- W2914961812 hasConceptScore W2914961812C3019447875 @default.
- W2914961812 hasConceptScore W2914961812C55493867 @default.
- W2914961812 hasConceptScore W2914961812C71924100 @default.
- W2914961812 hasConceptScore W2914961812C86803240 @default.
- W2914961812 hasConceptScore W2914961812C95444343 @default.
- W2914961812 hasIssue "3" @default.
- W2914961812 hasLocation W29149618121 @default.
- W2914961812 hasOpenAccess W2914961812 @default.
- W2914961812 hasPrimaryLocation W29149618121 @default.
- W2914961812 hasRelatedWork W1969967781 @default.
- W2914961812 hasRelatedWork W1976335728 @default.
- W2914961812 hasRelatedWork W1989759841 @default.
- W2914961812 hasRelatedWork W1998269242 @default.
- W2914961812 hasRelatedWork W2022018538 @default.
- W2914961812 hasRelatedWork W2071845315 @default.
- W2914961812 hasRelatedWork W2591940366 @default.
- W2914961812 hasRelatedWork W2779456541 @default.
- W2914961812 hasRelatedWork W2811153050 @default.
- W2914961812 hasRelatedWork W4280617682 @default.
- W2914961812 hasVolume "116" @default.
- W2914961812 isParatext "false" @default.
- W2914961812 isRetracted "false" @default.
- W2914961812 magId "2914961812" @default.
- W2914961812 workType "article" @default.