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Adabella van der Zand
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.
I want to identify molecular chaperones that are involved in folding of CFTR’s NBD1 domain, the location of the most common disease-causing mutation (F508del), and how they assist with NBD1 folding.
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.
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.
I study the folding and misfolding of CFTR and the effects of potential therapeutics on its folding/misfolding to aid in the development of transformative therapies.
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
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.
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.