Structural and biophysical investigations of Rab GTPase interacting proteins
Citation:
Carmen Dregger, 'Structural and biophysical investigations of Rab GTPase interacting proteins', [thesis], Trinity College (Dublin, Ireland). School of Biochemistry and Immunology, 2011, pp 197Download Item:
Dregger TCD THESIS 9779 Structural and.pdf (PDF) 78.64Mb
Abstract:
Summary: Rab GTPases are important regulators of cell trafficking steps such as vesicle
fusion, budding and motility. They are often described as 'on/off' switches, interacting
with specific effectors when bound to GTP. Although their secondary and tertiary
structures are largely conserved they bind sometimes very diverse effectors sharing little or
no homology. A similar but less prodigious situation is evident with guanosine nucleotide
exchange factors, proteins that interact with Rab GTPases in order to facilitate the
nucleotide exchange during the Rab GTPase cycling.
Author: Dregger, Carmen
Advisor:
Khan, AmirQualification name:
Doctor of Philosophy (Ph.D.)Publisher:
Trinity College (Dublin, Ireland). School of Biochemistry and ImmunologyNote:
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Biochemistry, Ph.D., Ph.D. Trinity College Dublin.Licences: