Education

Ph.D. in Biotechnology, Department of Physics, Chemistry and Biology, Linköping University, Linköping, Sweden, 2009

Current position

Group leader at the Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany

Publications (since 2005)

1. Carlon, A., Ravera, E., Hennig, J., Parigi, G., Sattler, M. and Luchinat, C. (2016). Improved Accuracy from Joint X-ray and NMR Refinement of a Protein-RNA Complex Structure. J Am Chem Soc 138(5): 1601-1610.

2. Horn, A., Hennig, J., Ahmed, Y. L., Stier, G., Wild, K., Sattler, M. and Sinning, I. (2015). Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction. Nat Commun 6: 8875.

3. Loedige, I., Jakob, L., Treiber, T., Ray, D., Stotz, M., Treiber, N., Hennig, J., Cook, K. B., Morris, Q., Hughes, T. R., Engelmann, J. C., Krahn, M. P. and Meister, G. (2015). The Crystal Structure of the NHL Domain in Complex with RNA Reveals the Molecular Basis of Drosophila Brain-Tumor-Mediated Gene Regulation. Cell Rep 13(6): 1206-1220.

4. Freiburger, L., Sonntag, M., Hennig, J., Li, J., Zou, P. and Sattler, M. (2015). Efficient segmental isotope labeling of multi-domain proteins using Sortase A. J Biomol NMR 63(1): 1-8.

5. Hennig, J., Warner, L. R., Simon, B., Geerlof, A., Mackereth, C. D. and Sattler, M. (2015). Structural Analysis of Protein-RNA Complexes in Solution Using NMR Paramagnetic Relaxation Enhancements. Methods Enzymol 558: 333-362.

6. Hennig, J. and Sattler, M. (2015). Deciphering the protein-RNA recognition code: combining large-scale quantitative methods with structural biology. Bioessays 37(8): 899-908.

7. Friberg, A., Thumann, S., Hennig, J., Zou, P., Nossner, E., Ling, P. D., Sattler, M. and Kempkes, B. (2015). The EBNA-2 N-Terminal Transactivation Domain Folds into a Dimeric Structure Required for Target Gene Activation. PLoS Pathog 11(5): e1004910.

8. Hennig, J., Andresen, C., Museth, A. K., Lundstrom, P., Tibell, L. A. and Jonsson, B. H. (2015). Local destabilization of the metal-binding region in human copper-zinc superoxide dismutase by remote mutations is a possible determinant for progression of ALS. Biochemistry 54(2): 323-333.

9. Hennig, J., Gebauer, F. and Sattler, M. (2014). Breaking the protein-RNA recognition code. Cell Cycle 13(23): 3619-3620.

10. Hennig, J., Militti, C., Popowicz, G. M., Wang, I., Sonntag, M., Geerlof, A., Gabel, F., Gebauer, F. and Sattler, M. (2014). Structural basis for the assembly of the Sxl-Unr translation regulatory complex. Nature 515(7526): 287-290.

11. Feige, M. J., Grawert, M. A., Marcinowski, M., Hennig, J., Behnke, J., Auslander, D., Herold, E. M., Peschek, J., Castro, C. D., Flajnik, M., Hendershot, L. M., Sattler, M., Groll, M. and Buchner, J. (2014). The structural analysis of shark IgNAR antibodies reveals evolutionary principles of immunoglobulins. Proc Natl Acad Sci U S A 111(22): 8155-8160.

12. Loedige, I., Stotz, M., Qamar, S., Kramer, K., Hennig, J., Schubert, T., Loffler, P., Langst, G., Merkl, R., Urlaub, H. and Meister, G. (2014). The NHL domain of BRAT is an RNA-binding domain that directly contacts the hunchback mRNA for regulation. Genes Dev 28(7): 749-764.

13. Hennig, J. and Sattler, M. (2014). The dynamic duo: combining NMR and small angle scattering in structural biology. Protein Sci 23(6): 669-682.

14. Wang, I., Hennig, J., Jagtap, P. K., Sonntag, M., Valcarcel, J. and Sattler, M. (2014). Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1. Nucleic Acids Res 42(9): 5949-5966.

15. Pfaff, J., Hennig, J., Herzog, F., Aebersold, R., Sattler, M., Niessing, D. and Meister, G. (2013). Structural features of Argonaute-GW182 protein interactions. Proc Natl Acad Sci U S A 110(40): E3770-3779.

16. Weininger, U., Blissing, A. T., Hennig, J., Ahlner, A., Liu, Z., Vogel, H. J., Akke, M. and Lundstrom, P. (2013). Protein conformational exchange measured by 1H R1rho relaxation dispersion of methyl groups. J Biomol NMR 57(1): 47-55.

17. Weininger, U., Blissing, A. T., Hennig, J., Ahlner, A., Liu, Z., Vogel, H. J., Akke, M. and Lundstrom, P. (2013). Protein conformational exchange measured by 1H R1rho relaxation dispersion of methyl groups. J Biomol NMR 57(1): 47-55.

18. Hennig, J., de Vries, S. J., Hennig, K. D., Randles, L., Walters, K. J., Sunnerhagen, M. and Bonvin, A. M. (2012). MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry. BMC Struct Biol 12: 29.

19. Wennerstrand, P., Dametto, P., Hennig, J., Klingstedt, T., Skoglund, K., Appell, M. L. and Martensson, L. G. (2012). Structural characteristics determine the cause of the low enzyme activity of two thiopurine S-methyltransferase allelic variants: a biophysical characterization of TPMT*2 and TPMT*5. Biochemistry 51(30): 5912-5920.

20. Espinosa, A., Hennig, J., Ambrosi, A., Anandapadmanaban, M., Abelius, M. S., Sheng, Y., Nyberg, F., Arrowsmith, C. H., Sunnerhagen, M. and Wahren-Herlenius, M. (2011). Anti-Ro52 autoantibodies from patients with Sjogren's syndrome inhibit the Ro52 E3 ligase activity by blocking the E3/E2 interface. J Biol Chem 286(42): 36478-36491.

21. Hennig, J., Hennig, K. D. and Sunnerhagen, M. (2008). MTMDAT: Automated analysis and visualization of mass spectrometry data for tertiary and quaternary structure probing of proteins. Bioinformatics 24(10): 1310-1312.

22. Hennig, J., Bresell, A., Sandberg, M., Hennig, K. D., Wahren-Herlenius, M., Persson, B. and Sunnerhagen, M. (2008). The fellowship of the RING: the RING-B-box linker region interacts with the RING in TRIM21/Ro52, contains a native autoantigenic epitope in Sjogren syndrome, and is an integral and conserved region in TRIM proteins. J Mol Biol 377(2): 431-449.

23. Ottosson, L., Hennig, J., Espinosa, A., Brauner, S., Wahren-Herlenius, M. and Sunnerhagen, M. (2006). Structural, functional and immunologic characterization of folded subdomains in the Ro52 protein targeted in Sjogren's syndrome. Mol Immunol 43(6): 588-598.

24. Hennig, J., Ottosson, L., Andresen, C., Horvath, L., Kuchroo, V. K., Broo, K., Wahren-Herlenius, M. and Sunnerhagen, M. (2005). Structural organization and Zn2+-dependent subdomain interactions involving autoantigenic epitopes in the Ring-B-box-coiled-coil (RBCC) region of Ro52. J Biol Chem 280(39): 33250-33261.

25. Ottosson, L., Salomonsson, S., Hennig, J., Sonesson, S. E., Dorner, T., Raats, J., Kuchroo, V. K., Sunnerhagen, M. and Wahren-Herlenius, M. (2005). Structurally derived mutations define congenital heart block-related epitopes within the 200-239 amino acid stretch of the Ro52 protein. Scand J Immunol 61(2): 109-118.