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A DNA-mediated search for optimal combinations of protein binders
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg.
Uppsala universitet, Medicinska och farmaceutiska vetenskapsområdet, Medicinska fakulteten, Institutionen för immunologi, genetik och patologi, Molekylära verktyg.
(engelsk)Manuskript (preprint) (Annet vitenskapelig)
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-204810OAI: oai:DiVA.org:uu-204810DiVA, id: diva2:640369
Tilgjengelig fra: 2013-08-13 Laget: 2013-08-12 Sist oppdatert: 2014-01-08
Inngår i avhandling
1. DNA-Mediated Detection and Profiling of Protein Complexes
Åpne denne publikasjonen i ny fane eller vindu >>DNA-Mediated Detection and Profiling of Protein Complexes
2013 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Proteins are the effector molecules of life. They are encoded in DNA that is inherited from generation to generation, but most cellular functions are executed by proteins. Proteins rarely act on their own – most actions are carried out through an interplay of tens of proteins and other biomolecules.

Here I describe how synthetic DNA can be used to study proteins and protein complexes. Variants of proximity ligation assays (PLA) are used to generate DNA reporter molecules upon proximal binding by pairs of DNA oligonucleotide-modified affinity reagents. In Paper I, a robust protocol was set up for PLA on paramagnetic microparticles, and we demonstrated that this solid phase PLA had superior performance for detecting nine candidate cancer biomarkers compared to other immunoassays. Based on the protocol described in Paper I I then developed further variants of PLA that allows detection of protein aggregates and protein interactions. I sensitively detected aggregated amyloid protofibrils of prion proteins in paper II, and in paper III I studied binary interactions between several proteins of the NFκB family. For all immunoassays the selection of high quality affinity binders represents a major challenge. I have therefore established a protocol where a large set of protein binders can be simultaneously validated to identify optimal pairs for dual recognition immunoassays (Paper IV).  

sted, utgiver, år, opplag, sider
Uppsala: Acta Universitatis Upsaliensis, 2013. s. 43
Serie
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Medicine, ISSN 1651-6206 ; 923
Emneord
Proximity ligation assay, Protein complexes, Protein interactions, Biomarkers, Prions, Antibodies
HSV kategori
Forskningsprogram
Medicinsk vetenskap
Identifikatorer
urn:nbn:se:uu:diva-204861 (URN)978-91-554-8718-8 (ISBN)
Disputas
2013-09-27, Rudbecksalen, Rudbeck Laboratory, Uppsala, 13:00 (engelsk)
Opponent
Veileder
Tilgjengelig fra: 2013-09-06 Laget: 2013-08-12 Sist oppdatert: 2014-01-08

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