Show simple item record

AuthorNavalpur Annamalai, Karthikeyandc.contributor.author
Date of accession2018-01-18T15:23:08Zdc.date.accessioned
Available in OPARU since2018-01-18T15:23:08Zdc.date.available
Year of creation2017dc.date.created
Date of first publication2018-01-18dc.date.issued
AbstractAmyloid formation is the central event in diseases such as Alzheimer’s (AD), Parkinson’s (PD) and several other systemic amyloidotic diseases like light chain amyloidosis (AL amyloidosis). In systemic amyloidosis, the multi organ involvement and post-translation modifications adds more complexity in delineating the disease mechanism especially in the case of AL amyloidosis. The exact disease mechanism underlying AL amyloidosis in vivo is not completely understood. Systemic AL amyloidosis is very aggressive particularly when the cardiac system of the patient gets affected. AL protein sequence involved in the amyloid deposits is found to be varying among patients and is therefore difficult to rationalize a common amyloid motif for the cause of the debilitating disease. Hence, AL amyloidosis is considered as a highly heterogeneous disease which also raises a question if such heterogenic properties affect the fibrillar structure or not. So far, the structure of tissue derived AL fibril structure is not well characterized due to the difficulties in isolating the intact fibrils. The infiltration of amyloid fibrils into organs is believed to be the primary cause for systemic amyloidotic diseases. However, increasing evidence in neurodegenerative diseases like in AD suggests that apart from fibril deposition, the soluble amyloid species play an important role in causing the debilitating disease. It appears that, the presence of either fibril and or soluble amyloid species are toxic to the living cells. However, exact the mechanism underlying the toxicity induced by amyloid aggregates is unknown and it is due to the lack of knowledge of structural and molecular properties of tissue derived amyloid aggregates. In vivo formed amyloid aggregates are yet to be characterized which may lead to fundamental insights of protein misfolding disease. Here, isolation and characterization of amyloid aggregates from diseased tissue material is presented.dc.description.abstract
Languageendc.language.iso
PublisherUniversität Ulmdc.publisher
LicenseStandarddc.rights
Link to license texthttps://oparu.uni-ulm.de/xmlui/license_v3dc.rights.uri
KeywordAmyloid fibrildc.subject
Dewey Decimal GroupDDC 570 / Life sciencesdc.subject.ddc
Dewey Decimal GroupDDC 610 / Medicine & healthdc.subject.ddc
MeSHAlzheimer diseasedc.subject.mesh
MeSHParkinson diseasedc.subject.mesh
MeSHPrionsdc.subject.mesh
MeSHProtein foldingdc.subject.mesh
MeSHAmyloidosisdc.subject.mesh
TitleIsolation and characterisation of amyloid aggregates from disease tissuesdc.title
Resource typeDissertationdc.type
Date of acceptance2017-02-15dcterms.dateAccepted
RefereeFändrich, Marcusdc.contributor.referee
RefereeSchönfeld, Stefandc.contributor.referee
DOIhttp://dx.doi.org/10.18725/OPARU-5349dc.identifier.doi
PPN1659157773dc.identifier.ppn
URNhttp://nbn-resolving.de/urn:nbn:de:bsz:289-oparu-5406-4dc.identifier.urn
GNDParkinson-Krankheitdc.subject.gnd
GNDAlzheimerkrankheitdc.subject.gnd
GNDProteinfaltungdc.subject.gnd
GNDAmyloidosedc.subject.gnd
FacultyFakultät für Naturwissenschaftenuulm.affiliationGeneral
InstitutionInstitut für Proteinbiochemieuulm.affiliationSpecific
Shelfmark print versionW: W-H 15.414uulm.shelfmark
Grantor of degreeFakultät für Naturwissenschaftenuulm.thesisGrantor
DCMI TypeTextuulm.typeDCMI
CategoryPublikationenuulm.category
Bibliographyuulmuulm.bibliographie


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record