Matches in SemOpenAlex for { <https://semopenalex.org/work/W4252663069> ?p ?o ?g. }
Showing items 1 to 75 of
75
with 100 items per page.
- W4252663069 endingPage "516a" @default.
- W4252663069 startingPage "516a" @default.
- W4252663069 abstract "Light chain (AL) amyloidosis is a protein misfolding disease where immunoglobulin light chains sample partially folded states that lead to misfolding and amyloid formation, resulting in organ dysfunction and death. In vivo, amyloid deposits are found in the extracellular space and involve a variety of accessory molecules such as glycosaminoglycans, one of the main components of the extracellular matrix. Glycosaminoglycans are a group of negatively charged, heteropolysaccharides composed of repeating disaccharide units. In this study, we investigated the effect of glycosaminoglycans on the kinetics of amyloid fibril formation of three AL cardiac amyloidosis light chains. These proteins have similar thermodynamic stability but exhibit different kinetics of fibril formation. We also studied single restorative and reciprocal mutants and wild type germline control protein. We found that the type of glycosaminoglycan has different effect on the kinetics of fibril formation, and this effect seems to be associated with the natural propensity of each AL protein to form fibrils. Heparan sulfate accelerated AL-12, AL-09, κI Y87H, and AL-103 H92D fibril formation, it delayed fibril formation for AL-103 and did not promote any fibril formation for AL-12 R65S, AL-103 delP95aIns or κI O18/O8. Chondroitin sulfate A on the other hand, shows a strong fibril formation inhibition for all proteins. We propose that Heparan sulfate facilitates the formation of transient amyloidogenic conformations of AL light chains, hereby promoting amyloid formation, whereas Chondroitin sulfate A kinetically traps partially unfolded intermediates and further fibril elongation into fibrils is inhibited, resulting in formation/accumulation of oligomeric/protofibrillar aggregates." @default.
- W4252663069 created "2022-05-12" @default.
- W4252663069 creator A5006035574 @default.
- W4252663069 creator A5031685457 @default.
- W4252663069 creator A5049125050 @default.
- W4252663069 creator A5060332444 @default.
- W4252663069 date "2015-01-01" @default.
- W4252663069 modified "2023-10-18" @default.
- W4252663069 title "Differential Effects on Light Chain Amyloid Formation Depend on Mutations and Type of Glycosaminoglycans" @default.
- W4252663069 doi "https://doi.org/10.1016/j.bpj.2014.11.2828" @default.
- W4252663069 hasPublicationYear "2015" @default.
- W4252663069 type Work @default.
- W4252663069 citedByCount "0" @default.
- W4252663069 crossrefType "journal-article" @default.
- W4252663069 hasAuthorship W4252663069A5006035574 @default.
- W4252663069 hasAuthorship W4252663069A5031685457 @default.
- W4252663069 hasAuthorship W4252663069A5049125050 @default.
- W4252663069 hasAuthorship W4252663069A5060332444 @default.
- W4252663069 hasBestOaLocation W42526630691 @default.
- W4252663069 hasConcept C121332964 @default.
- W4252663069 hasConcept C12554922 @default.
- W4252663069 hasConcept C142724271 @default.
- W4252663069 hasConcept C148898269 @default.
- W4252663069 hasConcept C153074725 @default.
- W4252663069 hasConcept C179104552 @default.
- W4252663069 hasConcept C185592680 @default.
- W4252663069 hasConcept C189165786 @default.
- W4252663069 hasConcept C204328495 @default.
- W4252663069 hasConcept C27523624 @default.
- W4252663069 hasConcept C2777633098 @default.
- W4252663069 hasConcept C2778041096 @default.
- W4252663069 hasConcept C2779553658 @default.
- W4252663069 hasConcept C2779951007 @default.
- W4252663069 hasConcept C55493867 @default.
- W4252663069 hasConcept C62520636 @default.
- W4252663069 hasConcept C71924100 @default.
- W4252663069 hasConcept C86803240 @default.
- W4252663069 hasConceptScore W4252663069C121332964 @default.
- W4252663069 hasConceptScore W4252663069C12554922 @default.
- W4252663069 hasConceptScore W4252663069C142724271 @default.
- W4252663069 hasConceptScore W4252663069C148898269 @default.
- W4252663069 hasConceptScore W4252663069C153074725 @default.
- W4252663069 hasConceptScore W4252663069C179104552 @default.
- W4252663069 hasConceptScore W4252663069C185592680 @default.
- W4252663069 hasConceptScore W4252663069C189165786 @default.
- W4252663069 hasConceptScore W4252663069C204328495 @default.
- W4252663069 hasConceptScore W4252663069C27523624 @default.
- W4252663069 hasConceptScore W4252663069C2777633098 @default.
- W4252663069 hasConceptScore W4252663069C2778041096 @default.
- W4252663069 hasConceptScore W4252663069C2779553658 @default.
- W4252663069 hasConceptScore W4252663069C2779951007 @default.
- W4252663069 hasConceptScore W4252663069C55493867 @default.
- W4252663069 hasConceptScore W4252663069C62520636 @default.
- W4252663069 hasConceptScore W4252663069C71924100 @default.
- W4252663069 hasConceptScore W4252663069C86803240 @default.
- W4252663069 hasIssue "2" @default.
- W4252663069 hasLocation W42526630691 @default.
- W4252663069 hasOpenAccess W4252663069 @default.
- W4252663069 hasPrimaryLocation W42526630691 @default.
- W4252663069 hasRelatedWork W158672605 @default.
- W4252663069 hasRelatedWork W1820293477 @default.
- W4252663069 hasRelatedWork W1970703718 @default.
- W4252663069 hasRelatedWork W2011688759 @default.
- W4252663069 hasRelatedWork W2026394030 @default.
- W4252663069 hasRelatedWork W2074197051 @default.
- W4252663069 hasRelatedWork W2091387031 @default.
- W4252663069 hasRelatedWork W2094794511 @default.
- W4252663069 hasRelatedWork W2100555760 @default.
- W4252663069 hasRelatedWork W2103997070 @default.
- W4252663069 hasVolume "108" @default.
- W4252663069 isParatext "false" @default.
- W4252663069 isRetracted "false" @default.
- W4252663069 workType "article" @default.