Persönlicher Status und Werkzeuge

Prof. Dr. Aymelt Itzen

Specific field

Protein Chemistry

Department

Chemistry

Contact Details

Business card at TUMonline

Academic Career and Research Areas

Prof. Itzen (*1977) investigates the regulation of intracellular transport processes from a biochemical point of view. In doing so, he especially exploits proteins originating from Legionella bacteria in order to elucidate the activities of human proteins. The objective of his research is to gain a more profound understanding of intracellular transport processes by using methods of biochemistry and protein chemistry.

After receiving his diploma (2003) in biochemistry at the University of Hannover, he finished his PhD at the Max Planck Institute of Molecular Physiology in Dortmund. After working as a PostDoc at the same institute for a short period of time, he was promoted to manager of a project group (2009). In 2011 he was appointed assistant professor at the Technische Universität München in the subject of protein chemistry.

Key Publications (all publications)

Schoebel S, Cichy AL, Goody RS, Itzen A: “Protein LidA from Legionella is a Rab GTPase supereffector”. Proc. Natl. Acad. Sci. USA. 2011; 108(44), 17945-17950.

Abstract

Hou XM, Hagemann N, Schoebel S, Blankenfeldt W, Goody RS, Erdmann KS, Itzen A: „A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1”. EMBO J. 2011; 30(8), 1659-1670.

Abstract

Müller MP, Peters H, Blumer J, Blankenfeldt W, Goody RS, Itzen A: „The Legionella Effector Protein DrrA AMPylates the Membrane Traffic Regulator Rab1b”. Science. 2010; 329(5994), 946-949.

Abstract

Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A.: “RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity”. Mol. Cell. 2009; 36(6), 1060-1072. 

Abstract

Itzen A, Pylypenko O, Goody RS, Alexandrov K, Rak A.: “Nucleotide exchange via local protein unfolding-structure of Rab8 in complex with MSS4”. EMBO J. 2006; 25(7):1445-55.

Abstract