PD Dr. Susanne Eschenburg participates in RESIST research project B4.
| My Research Interest in RESIST |
We work on the elucidation of the molecular mechanism of innate immune receptors of the NLRP family. These immune receptors constitute a first line of defense against invading pathogens. We combine a wide range of structural and cell biological methods to understand, how NLRPs function and how their function can be modulated.
In particular we will analyse the interactions of pathogen- derived proteins with NLRPs and of small-molecule compounds that are known to inhibit selected NLRPs. Among our long-term goals is the structure-based development of lead compounds for the therapeutic modulation of the function of selected NLRPs.
PD Dr. Eschenburg about her scientific work
PD Dr. Susanne Eschenburg – Curriculum Vitae
Current Position
Since 2000 Head of the research group „Structural and Functional Analysis of Disease Relevant Proteins“, Institute for Biophysical Chemistry, MHH
Undergraduate and Postgraduate Training
1982 – 1989 Study of Physics, University of Tübingen and University of Hamburg, Germany
1991 Diploma in Physics, University of Hamburg, Germany
1991 – 1996 Predoctoral fellow, EMBL Outstation Hamburg, Germany
1996 Doctoral degree (Dr. rer. nat.) University of Hamburg
2017 Habilitation in Biochemistry, MHH
Academic and Research Posts
1996 – 1999 Postdoc, Institute of Physiological Chemistry, University of Hamburg, Germany
1999 – 2004 Scientist, Max-Planck Institute for Medical Research,Heidelberg, Germany
2004 – 2010 Group Leader, Max-Planck Institute for Molecular Physiology, Dortmund, Germany
Since 2010 Group Leader, Institute for Biophysical Chemistry
Awards and Prizes
2014 Participant in the Ellen Schmidt program of the Hannover Medical School
10 Selected Publications (of > 225 original publications)
Duong M, Yu X, Teng B, Schroder P, Haller H, Eschenburg S, and Schiffer, M. Protein kinase C regulates stabilization of -catenin and its subcellular localization in podocytes. J. Biol. Chem. 2017, 292: 12100-12110.
Zumbrägel FK, Machtens DA, Curth U, Lüder CG, Reubold TF, and Eschenburg S. Survivin does not influence the anti-apoptotic action of XIAP on caspase-9. Biochem. Biophys. Res. Commun. 2017, 482: 530-535.
Reubold TF, Faelber K, Plattner N, Posor Y, Ketel K, Curth U, Schlegel J, Anand R, Manstein DJ, Noe F, Haucke V, Daumke O, Eschenburg S. Crystal structure of the dynamin tetramer. Nature 2015, 525:404-408.
Reubold TF, Hahne G, Wohlgemuth, Eschenburg S. Crystal structure of the leucine-rich repeat domain of the NOD-like receptor NLRP1: implications for binding of muramyl dipeptide. FEBS Lett 2014, 588:3327-3332.
Reubold TF, Wohlgemuth, Eschenburg S. Crystal structure of full-length Apaf-1: how the death signal is relayed in the mitochondrial pathway of apoptosis. Structure 2011,19:1074-1083.
Reubold TF, Wohlgemuth, Eschenburg S. A new model for the transition of APAF-1 from inactive monomer to caspase-activating apoptosome. J Biol Chem 2009, 284:32717-32724.
Reubold TF, Eschenburg S, Becker A, Leonard M, Schmid SL, Vallee RB, Kull FJ; Manstein DJ. Crystal structure of the GTPase domain of rat dynamin 1. Proc Natl Acad Sci U S A 2005, 102:13093-13098.
Reubold TF, Eschenburg S, Becker A, Kull FJ, Manstein DJ. A structural model for actin-induced nucleotide release in myosin. Nat Struct Biol 2003, 10:826-830.
Schonbrunn E1 , Eschenburg S1 , Shuttleworth WA, Schloss JV, Amrhein N, Evans JN, Kabsch W. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A 2001, 98:1376-1380. 1 Equal contribution
Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N. Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc Natl Acad Sci U S A, 2000, 97:6345-6349.
