Hartmut Oschkinat

Collective exchange processes reveal an active site proton cage in bacteriorhodopsin

• Friedrich, D.
• Brünig, F. N.
• Nieuwkoop, A. J.
• Netz, R. R.
• Hegemann, P., &
• Oschkinat, H.

Communications Biology 2020, 3, 4

Crystal structure of Q4D6Q6, a conserved kinetoplastid-specific protein from Trypanosoma cruzi

• D'Andrea, E. D.
• Roske, Y.
• Oliveira, G. A. P.
• Cremer, N.
• Diehl, A.
• Schmieder, P.
• Heinemann, U.
• Oschkinat, H., &
• Pires, J. R.

Journal of Structural Biology 2020, 211, 107536

Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells

• Barone, M.
• Müller, M.
• Chiha, S.
• Ren, J.
• Albat, D.
• Soicke, A.
• Dohmen, S.
• Klein, M.
• Bruns, J.
• Dinther, M.
• Opitz, R.
• Lindemann, P.
• Beerbaum, M.
• Motzny, K.
• Roske, Y.
• Schmieder, P.
• Volkmer, R.
• Nazare, M.
• Heinemann, U.
• Oschkinat, H.
• Ten Dijke, P.
• Schmalz, H. G., &
• Kühne, R.

Proceedings of the National Academy of Sciences of the United States of America 2020, 117, 29684-29690

MAS NMR detection of hydrogen bonds for protein secondary structure characterization

• Friedrich, D.
• Perodeau, J.
• Nieuwkoop, A. J., &
• Oschkinat, H.

Journal of Biomolecular NMR 2020, 74, 247-256

NMR quality control of fragment libraries for screening

• Sreeramulu, S.
• Richter, C.
• Kuehn, T.
• Azzaoui, K.
• Blommers, M. J. J.
• Del Conte, R.
• Fragai, M.
• Trieloff, N.
• Schmieder, P.
• Nazare, M.
• Specker, E.
• Ivanov, V.
• Oschkinat, H.
• Banci, L., &
• Schwalbe, H.

Journal of Biomolecular NMR 2020, 74, 555-563

pH-Dependent Protonation of Surface Carboxylate Groups in PsbO Enables Local Buffering and Triggers Structural Changes

• Gerland, L.
• Friedrich, D.
• Hopf, L.
• Donovan, E. J.
• Wallmann, A.
• Erdmann, N.
• Diehl, A.
• Bommer, M.
• Buzar, K.
• Ibrahim, M.
• Schmieder, P.
• Dobbek, H.
• Zouni, A.
• Bondar, A. N.
• Dau, H., &
• Oschkinat, H.

ChemBioChem 2020, 21, 1597-1604

Pigmentation Chemistry and Radical-Based Collagen Degradation in Alkaptonuria and Osteoarthritic Cartilage

• Chow, W. Y.
• Norman, B. P.
• Roberts, N. B.
• Ranganath, L. R.
• Teutloff, C.
• Bittl, R.
• Duer, M. J.
• Gallagher, J. A., &
• Oschkinat, H.

Angewandte Chemie-International Edition 2020, 59, 11937-11942

Protein resonance assignment by BSH-CP based 3D solid-state NMR experiments: A practical guide

• Hoffmann, J.
• Ruta, J.
• Shi, C.
• Hendriks, K.
• Chevelkov, V.
• Franks, W. T.
• Oschkinat, H.
• Giller, K.
• Becker, S., &
• Lange, A.

Magnetic Resonance in Chemistry 2020, 58, 445-465

Detection of nucleic acids and other low abundance components in native bone and osteosarcoma extracellular matrix by isotope enrichment and DNP-enhanced NMR

• Goldberga, I.
• Li, R.
• Chow, W. Y.
• Reid, D. G.
• Bashtanova, U.
• Rajan, R.
• Puszkarska, A.
• Oschkinat, H., &
• Duer, M. J.

RSC Advances 2019, 9, 26686-26690

DNP NMR of biomolecular assemblies

• Jaudzems, K.
• Polenova, T.
• Pintacuda, G.
• Oschkinat, H., &
• Lesage, A.

Journal of Structural Biology 2019, 206, 90-98

Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies

• Gupta, R.
• Zhang, H. L.
• Lu, M. M.
• Hou, G. J.
• Caporini, M.
• Rosay, M.
• Maas, W.
• Struppe, J.
• Ahn, J.
• Byeon, I. J. L.
• Oschkinat, H.
• Jaudzems, K.
• Barbet-Massin, E.
• Emsley, L.
• Pintacuda, G.
• Lesage, A.
• Gronenborn, A. M., &
• Polenova, T.

Journal of Physical Chemistry B 2019, 123, 5048-5058

Host monitoring of quorum sensing during Pseudomonas aeruginosa infection

• Moura-Alves, P.
• Puyskens, A.
• Stinn, A.
• Klemm, M.
• Guhlich-Bornhof, U.
• Dorhoi, A.
• Furkert, J.
• Kreuchwig, A.
• Protze, J.
• Lozza, L.
• Pei, G.
• Saikali, P.
• Perdomo, C.
• Mollenkopf, H. J.
• Hurwitz, R.
• Kirschhoefer, F.
• Brenner-Weiss, G.
• Weiner, 3.
• Oschkinat, H.
• Kolbe, M.
• Krause, G., &
• Kaufmann, S. H. E.

Science 2019, 366, eaaw1629

Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization

• Müller, K. H.
• Hayward, R.
• Rajan, R.
• Whitehead, M.
• Cobb, A. M.
• Ahmad, S.
• Sun, M. X.
• Goldberga, I.
• Li, R.
• Bashtanova, U.
• Puszkarska, A. M.
• Reid, D. G.
• Brooks, R. A.
• Skepper, J. N.
• Bordoloi, J.
• Chow, W. Y.
• Oschkinat, H.
• Groombridge, A.
• Scherman, O. A.
• Harrison, J. A.
• Verhulst, A.
• D'Haese, P. C.
• Neven, E.
• Needham, L. M.
• Lee, S. F.
• Shanahan, C. M., &
• Duer, M. J.

Cell Reports 2019, 27, 3124-3138

The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants

• Kesten, C.
• Wallmann, A.
• Schneider, R.
• McFarlane, H. E.
• Diehl, A.
• Khan, G. A.
• Rossum, B. J.
• Lampugnani, E. R.
• Szymanski, W. G.
• Cremer, N.
• Schmieder, P.
• Ford, K. L.
• Seiter, F.
• Heazlewood, J. L.
• Sanchez-Rodriguez, C.
• Oschkinat, H., &
• Persson, S.

Nature Communications 2019, 10, 857