Publication

Genetic factors and analysis of protein misfolding in vivo

Holmberg, M., 2015, [Groningen]: University of Groningen. 199 p.

Research output: ThesisThesis fully internal (DIV)Academic

Copy link to clipboard

Documents

  • Title_and_contents

    Final publisher's version, 121 KB, PDF document

  • Chapter_1

    Final publisher's version, 734 KB, PDF document

  • Chapter_2

    Final publisher's version, 1 MB, PDF document

  • Chapter_3

    Final publisher's version, 146 KB, PDF document

  • Chapter_4

    Final publisher's version, 608 KB, PDF document

  • Chapter_5

    Final publisher's version, 73 KB, PDF document

  • Summary

    Final publisher's version, 35 KB, PDF document

  • Samenvatting

    Final publisher's version, 30 KB, PDF document

  • Acknowledgements

    Final publisher's version, 28 KB, PDF document

  • List_of_abbreviations

    Final publisher's version, 23 KB, PDF document

  • Complete_thesis

    Final publisher's version, 2 MB, PDF document

  • Propositions

    Final publisher's version, 23 KB, PDF document

  • Mats Holmberg
Alzheimer’s, Huntington’s and Parkinson’s disease belong to a group of disorders caused by misfolded proteins that are known to stick together in a specific manner forming long fibrils made up of thousands of individual proteins. These fibrils are known as amyloids. It is still unclear which part of the process of aggregation is harmful, and it is even possible that the amyloid is beneficial to the cell because it hides these proteins. In this thesis we identify a protein we have called Modifier of aggregation 4 (MOAG-4), which strongly promotes the formation of these protein aggregates. It affects several amyloid forming proteins but does not appear to act on other proteins that form aggregates in a more disordered fashion. MOAG-4 appears to work independently of other processes that protect cells against protein misfolding. MOAG-4 may help to answer questions about amyloid formation in the cell or can be further explored as a target for therapeutic intervention in neurodegenerative disorders. This thesis also describes two methods useful in the field of protein misfolding. The first one describes an efficient way to screen for protein modification and aggregation. The second method deals with the production of purified proteins which can be used to analyse the behaviour of proteins outside the cell. The strength of both methods lies in their speed and effectiveness.
Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
Supervisors/Advisors
Award date9-Sep-2015
Place of Publication[Groningen]
Publisher
Print ISBNs978-90-367-8035-3
Electronic ISBNs978-90-367-8034-6
Publication statusPublished - 2015

Download statistics

No data available

ID: 23436926