Kiel Group


Group Members

Christina Kiel
Associate Professor
Simona Catozzi
Postdoctoral Researcher, Kiel Group
Cian D'Arcy
Ph.D. Student, Kiel Group
Philipp Junk
Ph.D. Student, Kiel Group
Thomas Sevrin
Postdoctoral Researcher, Kiel Group
Camille Ternet
Ph.D. Student, Kiel Group

About the Group

What we do 

Proteins are the key molecules in cells and tissues. Their levels, activities and interactions with other molecules (into networks) ensures that normal developmental and cellular/tissue homeostasis processes take place. Consequently, network-centric approaches to molecular medicine consider human diseases as the consequence of perturbations of these protein (and ultimately signalling, transcriptional, and metabolic) networks. Dr Kiel’s research takes proteins to the centre stage. The focus lies on understanding - in a systems and quantitative fashion - how missense disease mutations affect protein abundances, catalytic activities, and their interaction with partner proteins and other molecules. Combined complementary computational and experimental approaches are used in the different research projects.  


Recent publications 

From oncogenic mutation to dynamic code.
Kolch W, Kiel C. 
Science 361(6405):844-845 (2018). 

Systems level expression correlation of Ras GTPase regulators.  
Besray Unal E, Kiel C, Benisty H, Campbell A, Pickering K, Blüthgen N, Sansom OJ, Serrano L. 
Cell Commun Signal. 16(1):46 (2018). 

Opportunities and Challenges of Whole-Cell and -Tissue Simulations of the Outer Retina in Health and Disease.  
Luthert PJ, Serrano L, Kiel C. 
Annual Review of Biomedical Data Science 1,131-152 (2018). 

Interaction dynamics determine signaling and output pathway responses.  
Stojanovski K, Ferrar T, Benisty H, Uschner F, Delgado J, Jimenez J, Solé C, de Nadal E, Klipp E, Posas F, Serrano L, Kiel C.  
Cell. Rep. 19, 136-149 (2017). 
Simple and complex retinal dystrophies are associated with profoundly different disease networks.  
Kiel C, Lastrucci C, Luthert PJ, Serrano L.  
Sci. Rep. 7, 41835 (2017). 
The yin-yang of kinase activation and unfolding explains the peculiarity of Val600 in the activation segment of BRAF. 
Kiel C, Benisty H, Lloréns-Rico V, Serrano L.   
Elife 5, pii, e12814 (2016).