Scientific Staff
Adabella van der Zand
Support
Postdoctoral researchers
I aim to discover the mode of action of novel corrector drugs developed to rescue cell surface function of CFTR and gain more insight into how mutations and cellular factors affect protein folding.
CFTR folds in the ER and requires an orchestrated action of chaperone networks in the ER lumen, the ER membrane, and cytosol. I am interested in understanding how this cellular machinery assists CFTR folding, with focus on NBD1 domain, where the most common disease-causing mutation resides.
My project aims to identify the key players in the transport and recycling of CFTR protein at the plasma membrane by employing biochemical and fluorescence (immune) imaging techniques.
I am investigating how does the regulation of translation processes (e.g. RNA motifs, translation speed control) influence CFTR folding and, consequently, CFTR functioning.
PhD candidates
My aim is to identify intramembrane interaction partners of CFTR and how these are involved in chaperoning and quality control of folding of the transmembrane region of CFTR.
Laura Tadé
+31 30 253 3752
l.tade@uu.nl
Office: O.709
I want to know whether CFTR is only active at the cell surface or also in other cell compartments and when/where it acquires the structure that allows its function.
Marcel van Willigen
+31 30 253 4105
m.vanwilligen@uu.nl
Office: O.707
My research focuses on investigating CFTR folding using Cystic Fibrosis patient mutations, providing insights into how wild-type protein folds and how the respective patient mutants misfold.
I focus on aggregation-prone proteins linked to neurodegeneration. I am especially interested in understanding how Hsp90 can modulate Tau aggregation and its associated interactome.
My research focuses on the interplay between the chaperones Hsp70 and Hsp90, with emphasis on the purpose of Hsp90 and the function of the Hsp70/Hsp90 folding cascade.
I focus on the role of molecular chaperones – such as Hsp70 and Hsp90 – and their role in the aggregation process of Tau, a protein involved in Alzheimer’s Disease.
My research focuses on how Hsp90 selects its client proteins, as known Hsp90 binding partners recruit from various protein families and do not share functional or structural similarities.
The aim of my research is to determine for each CFTR2 disease-causing mutant to which available (pre)clinical drugs they respond at the CFTR protein level.
My project investigates how CFTR transmembrane domains assemble, and see how chaperones help with the assembly of these transmembrane domains with each other and nucleotide binding domains.
Technicians
I work on elucidating the mode of action of compounds that affect CFTR folding, to understand mechanisms of these compounds and their potential benefits for Cystic Fibrosis patients.
I am interested in a set of small endoplasmic reticulum localized chaperones, called the canopy family and their role in proteins folding, B cell differentiation and antibody secretion.
I develop/modify analysis techniques to study protein folding of model oxidative proteins and folding factors, in vivo and in vitro by short and long radioactive metabolic labelling.
My project aims to investigate the correlation between translation rate and CFTR folding
My aim is to develop a method to see CFTR at the plasma membrane of living cells using fluorescence microscopy. This method will then be used to identify key players in the transport and recycling of CFTR.
Students
Guests
Maarten Egmond