People

Eduardo de Mattos
+31 30 253 ….
e.demattos@uu.nl
Office: O.707

I investigate how folding intermediates of CFTR and their interaction with cellular protein quality control mechanisms modulates CFTR structure and function.

Françoise Dekker
+31 30 253 ….
f.a.dekker@uu.nl
Office: O.707

I work on developing other strategies for protein folding diseases, exploiting our knowledge on protein folding, molecular chaperones and fibril structures.

Júlia Aragones Pedrola
+31 30 253 ….
j.aragonespedrola@uu.nl
Office: O.710

Development of a strategy to target protein aggregation diseases, based on mimicking the role of molecular chaperones in the protein quality control.

Tamara Hillenaar
+31 30 253 ….
m.j.h.hillenaar@uu.nl
Office: O.706

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.

Jisu Im
+31 30 253 ….
j.im@uu.nl
Office: O.709

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.

Laura Tadé
+31 30 253 ….
l.tade@uu.nl
Office: DDW

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.

Magdalena Wawrzyniuk
+31 30 253 ….
m.wawrzynuik

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.

Guus van Zadelhoff
+31 30 253 3752
g.vanzadelhoff@uu.nl
Office: O.709

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.

Senna Hiensch
+31 30 253 3841
s.hiensch@uu.nl
Office: O.706

My research is about comparing genetic disease causing protein mutants to their wildtype variant by limited proteolysis and see if chaperones are able to stabilize these mutants.

Danny Schildknegt
+31 30 253 3841
d.schildknegt@uu.nl
Office: O.710

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.