[Translate to Deutsch:] Portrait

Prof. Dr.

Hartmut Oschkinat

Leitung Oschkinat Gruppe

 +49 30 94793 160

 oschkinat@fmp-berlin.de

Hartmut Oschinat ist der Gruppenleiter und NMR- Experte.
Er studierte in Göttingen und Heidelberg und so weiter


Strukturbiologie


Oschkinat Gruppe


FMP
FU Berlin

Publikationen

von 8

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

online lesen

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

online lesen

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

online lesen

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

online lesen

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

online lesen

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

online lesen

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

online lesen

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

online lesen

Publikationen

von 6

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

online lesen

DNP NMR of biomolecular assemblies

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

Journal of Structural Biology 2019, 206, 90-98

online lesen

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

online lesen

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

online lesen

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

online lesen

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

online lesen