Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/4199
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dc.contributor.authorSubramanian, Sarada-
dc.contributor.authorMadhavadas, Sowmya-
dc.contributor.authorBalasubramanian, Preetha-
dc.date.accessioned2009-05-15T09:06:50Z-
dc.date.available2009-05-15T09:06:50Z-
dc.date.issued2009-05-
dc.identifier.issn0019-5189-
dc.identifier.urihttp://hdl.handle.net/123456789/4199-
dc.description309-313en_US
dc.description.abstractMany neurodegenerative diseases result due to the accumulation of misfolded proteins as amyloid fibrils. Although the protein components of these fibrils from different disease states differ considerably, they appear to share common structure. Among these conformational disorders, Alzheimer’s disease (AD) and prion diseases exhibit significant overlap in their mechanism of pathogenesis. The present report demonstrates that antibodies directed against the prion protein repeat motif, Tyr-Tyr-Arg motif, recognize recombinantly expressed human amyloid ß (Aß) aggregates in enzyme linked immunosorbent assay. In addition, these antibodies dissociate the preformed aggregates of Aß in vitro. These findings illustrate an important property of conformation dependent antibodies viz., they specifically recognize the protein deposits associated with pathology and not the protein in normal tissue. These antibodies may benefit the development of approaches towards prevention and treatment of protein misfolding diseases.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.sourceIJEB Vol.47(05) [May 2009]en_US
dc.subjectAggregationen_US
dc.subjectAmyloid ßen_US
dc.subjectAntibodiesen_US
dc.subjectELISAen_US
dc.subjectFluorescenceen_US
dc.subjectThioflavin Ten_US
dc.titleInfluence of conformational antibodies on dissociation of fibrillar amyloid ß (Aß1-42) in vitroen_US
dc.typeArticleen_US
Appears in Collections:IJEB Vol.47(05) [May 2009]

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