Institut for Molekylærbiologi og Genetik

Aarhus Universitets segl

Jan J. Enghild

Jan J. Enghild

Professor
M
H 1874, 261
P +4587155449

Research project: Proteome analysis and protein characterization

The laboratory seeks to describe the "structure–activity–function" algorithm of proteins. Our research is located at the interface between other structure analyses methods (NMR and X-ray crystallography) and we use a combination of protein chemistry, proteomics, enzymology, and recombinant DNA techniques.


We are interested in extracellular matrix (ECM) homeostasis and the identification and characterization of post-translational modifications. Available structural and functional information concerning ECM proteins is limited due to the inherent insolubility.

Granular corneal dystrophy, Type I. 

A superposition of the crystal structures of bovine TAFI (green) and porcine carboxypeptidase B (purple). Read more.

Protein Characterization

Our research is located at the interface between other structure analyses methods (NMR and X-ray crystallography) and we use a combination of protein chemistry, proteomics, enzymology, and recombinant DNA techniques.

  • Bikunin Proteins
  • Extracellular superoxide dismutase (EC-SOD)
  • Matrix metalloproteinase (MMP)
  • Novel proteolytic enzymes
  • Pigment epithelium-derived factor (PEDF)
  • Thrombin Activatable Fibrinolysis inhibitor (TAFI)
  • Transforming growth factor beta induced protein (TGFBIP) and cornea dystrophies
  • Transglutaminase

Peer-reviewed articles

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Jensen, K. T., Viana de Almeida, A. C., Rönning, S., Karlander, M., Nielsen, N. S., Thøgersen, I., Malm, M., Andersen, G. R., Enghild, J. J., Rockberg, J. & Harwood, S. L. (2026). Antagonist nanobodies prevent protease inhibition by CD109. Journal of Biological Chemistry, 302(3), Artikel 111187. https://doi.org/10.1016/j.jbc.2026.111187
Winther, K. G., Schneider, J., Haas, G., Christensen, A. H., Goyal, S., Luo, W., Wei, Z., Liu, J., Kjøge, K., Enghild, J. J., Meignin, C., Silverman, N., Cai, H., Imler, J. L. & Hartmann, R. (2026). FADD is recruited to activated STING oligomers to initiate caspase-mediated NF-κB activation in Drosophila melanogaster. EMBO Journal. Advance online publication. https://doi.org/10.1038/s44318-026-00761-9
Chrenková, A., Nashier, P., Madsen, C. L., Singh, M., Nielsen, J., Otzen, D. E., Enghild, J. J., Macek, B., Skjerning, R. B. & Brodersen, D. E. (2026). Homologous HipA-like kinases are controlled by internal translational initiation and genetic organisation. FEBS Letters, 600(3), 356-369. https://doi.org/10.1002/1873-3468.70234
Gadeberg, T. A. F., Jørgensen, M. H., Olesen, H. G., Lorentzen, J., Harwood, S. L., Almeida, A. V., Fruergaard, M. U., Jensen, R. K., Kanis, P., Pedersen, H., Tranchant, E., Petersen, S. V., Thøgersen, I. B., Kragelund, B. B., Lyons, J. A., Enghild, J. J. & Andersen, G. R. (2025). Cryo-EM analysis of complement C3 reveals a reversible major opening of the macroglobulin ring. Nature Structural and Molecular Biology, 32(5), 884-895. Artikel 872536. https://doi.org/10.1038/s41594-024-01467-4
Bryzek, D., Gasiorek, A., Kowalczyk, D., Santocki, M., Ciaston, I., Dobosz, E., Kolaczkowska, E., Kjøge, K., Kantyka, T., Lech, M., Potempa, B., Enghild, J. J., Potempa, J. & Koziel, J. (2025). Non-classical neutrophil extracellular traps induced by PAR2-signaling proteases. Cell Death & Disease, 16(1), Artikel 109. https://doi.org/10.1038/s41419-025-07428-z
Waligórska, I., Żak, K. M., Mikrut, N., Budziaszek, J., Medviediev, V., Bielecka, E., Kantyka, T., Kozieł, J., Thøgersen, I. B., Enghild, J. J., Grudnik, P., Potempa, J. & Książek, M. (2025). Periodontopathogens degrade angiotensin I from the human renin-angiotensin system through surface-attached proteases. Scientific Reports, 15(1), Artikel 43309. https://doi.org/10.1038/s41598-025-27891-0
Silale, A., Madej, M., Mikruta, K., Frey, A. M., Hart, A. J., Baslé, A., Scavenius, C., Enghild, J. J., Trost, M., Hirt, R. P. & van den Berg, B. (2025). Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota. Nature Microbiology, 10(11), 2845-2859. https://doi.org/10.1038/s41564-025-02132-2
McLain, A., Kowalczyk, A., Baran-Rachwalska, P., Sutera, F. M., Robertson, L. J., Nielsen, N. S., Enghild, J. J., Cobice, D., Bonelli, F., Barbaro, V., Ferrari, S., Patterson, B., Moore, L., Marshall, J., Nesbit, M. A. & Moore, T. (2025). TGFBI R124H mutant allele silencing in granular corneal dystrophy type 2 using topical siRNA delivery. Journal of Controlled Release, 382, Artikel 113681. https://doi.org/10.1016/j.jconrel.2025.113681
Poulsen, E. T., Nielsen, N. S. & Enghild, J. J. (2025). The role of the extracellular matrix in TGFBI-related corneal dystrophy development. I E. K. Kim & R. D. Stulting (red.), TGFBI-related Corneal Dystrophies: Clinical Findings, Cell Biology, and Genetics (s. 77-94). Springer. https://doi.org/10.1007/978-981-96-0131-8_9
Shah, A., Zhang, X., Snee, M., Lockhart-Cairns, M. P., Levy, C. W., Jowitt, T. A., Birchenough, H. L., Dean, L., Collins, R., Dodd, R. J., Roberts, A. R. E., Enghild, J. J., Mantovani, A., Fontana, J., Baldock, C., Inforzato, A., Richter, R. P. & Day, A. J. (2025). The structural organisation of pentraxin-3 and its interactions with heavy chains of inter-α-inhibitor regulate crosslinking of the hyaluronan matrix. Matrix biology : journal of the International Society for Matrix Biology, 136, 52-68. https://doi.org/10.1016/j.matbio.2025.01.002

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Revideret 15.08.2023
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