Wiktor Koźmiński's NMR group

orcid.org/0000-0002-1356-0301

List of publications:

• Fast evaluation of protein dynamics from deficient 15N relaxation data, Ł. Jaremko, M. Jaremko, A. Ejchart, M. Nowakowski, Journal of Biomolecular NMR (2018), 70, 219, DOI:10.1007/s10858-018-0176-3
• Spatial attributes of the four-helix bundle group of bacteriocins – The high-resolution structure of BacSp222 in solution, M. Nowakowski, L. Jaremko, B. Wladyka, G. Dubin, A. Ejchart, P. Mak, International Journal of biological macromolecules (2018), 107, 2715, DOI:10.1016/J.ijbiomac.2017.10.158
• Size makes a difference: Chiral recognition in complexes of fenchone with cyclodetrins studied by means of NMR titration, K. Dudzik, J. Wojcik, A. Ejchart, M. Nowakowski, Chirality (2017), 29, 747, DOI:10.1002/chir.22747
• Pitfalls in compressed sensing reconstruction and how to avoid them, A. Shchukina, P. Kasprzak, R. Dass, M. Nowakowski, K. Kazimierczuk, Journal of Biomolecular NMR (2017), 68, 79, DOI: 10.1007/s10858-016-0068-3
• Joint non-uniform sampling of all incremented time delays for quicker acquisition in protein relaxation studies, M. Urbanczyk, M. Nowakowski, W. Koźmiński, K. Kazimierczuk, Journal of Biomolecular NMR (2017), 68, 155, DOI:10.1007/s10858-017-0115-8
• Fast 2D NMR Spectroscopy for In vivo Monitoring of Bacterial Metabolism in Complex Mixtures, R. Dass, K. Grudziaz, T. Ishikawa, M. Nowakowski, R. Debowska, K. Kazimierczuk, Frontiers in Microbiology (2017), 8, DOI:10.3389/fmicb.201701306
• The Impact of beta-azido(or-piperidinyl)methylamino acids in position 2 or 3 on biological activity and conformation of dermorphin analogues, M. Maciejczyk, A. Lasota, O. Fraczak, P. Kosson, A. Misicka, M. Nowakowski, A. Ejchart, A. Olma, Journal of Peptide Science (2016), 22, 545, DOI:10.1002/psc.2903
• Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly, T. Kochanczyk, M. Nowakowski, D. Wojewska, A. Kocyla, A. Ejchart, W. Kozminski, A. Krezel, Scientific Reports (2016), 6, DOI:10.1038/srep36346
• Synthesis, biological activity and NMR-based structural studies of deltorphin I analogues modified in message domain with a niew α,α-disubstituted glycines, A. Lasota, O. Frączak, A. Muchowska, M. Nowakoski, M. Maciejczyk, A. Ejchart, A. Olma, Chemical Biology & Drug Design (2016), DOI:10.1111.cbdd.12730
• Backbone assignment of the MALT1 Paracaspase by Solution NMR, S. Unnerstale, M. Nowakowski, V. Brazenok, G. Stenberg, J. Lindberg, M. Mayzel, V. Orekhov, T. Agback, PloS one (2016), 11, e0146496, DOI:10.1371/journal.pone.0146496
• Applications of high dimensionality experiments to biomolecular NMR, M. Nowakowski, S. Saxena, J. Stanek, W. Koźmiński, Progress in Nuclear Magnetic Resonance Spectroscopy (2015), 90-91, 49, DOI:10.1016/J.pnmrs.2015.07.001
• Analogues of deltorphin I containing conformationally restricted amino acids in position 2: structure and opioid activity, A. Lasota, O. Frączak, A. Leśniak, A. Muchowska, A. W. Lipkowski, M. Nowakowski, A. Ejchart, A. Olma, Journal of Peptide Science (2015), 21, 120, DOI:10.1002/psc.2738
• The solution structure of the MANEC-type domain from Hepatocyte Growth Factor Activator Inhibitor 1 reveals an unexpected PAN/apple domain-type fold, Z. Hong, M. Nowakowski, C. Spronk, S. V. Petersen, P. A. Andreasen, W. Koźmiński, F. A. A. Mulder, J. Jensen Biochemical Journal (2015), 466, 299, DOI:10.1042/BJ20141236
• Complex formation of fenchone with a-cyclodextrin: NMR titrations, M. Nowakowski, A. Ejchart, Journal of Inclusion Phenomena and Macrocyclic Chemistry, (2014), 79, 337, DOI:10.1007/s10847-013-0356-4
• NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme, M. Jaremko, Ł. Jaremko, M. Nowakowski, M. Wojciechowski, R. H. Szczepanowski, R. Panecka, I. Zhukov, M. Bochtlerd, A. Ejchart, Journal of Structural Biology (2014), 185, 69, DOI:10.1016/J.jsb.2013.10.020
• Selective diagonal-free ¹³C,¹³C-edited aliphatic-aromatic NOESY experiment with non-uniform sampling, J. Stanek, M. Nowakowski, S. Saxena, K. Ruszczyńska-Bartnik, A. Ejchart and W. Koźmiński, Journal of Biomol. NMR (2013),  DOI:10.1007/s10858-013-9739-5
• Sialorphin and its analog as ligands for copper(II) ions, Elżbieta Kamysz, Aleksandra Kotynia, Żaneta Czyżnikowska, Mariusz Jaremko, Łukasz Jaremko, Michał Nowakowski, Justyna Brasun, Polyhedron (2013), 55,  216–224, DOI:10.1016/j.poly.2012.10.055
• Impact of calcium binding and thionylation of S100A1 protein on its NMR derived structure and backbone dynamics, M. Nowakowski, K. Ruszczyńska-Bartnik, M. Budzińska, Ł. Jaremko, M. Jaremko, K. Zdanowski, A. Bierzyński, and A. Ejchart, Biochemistry (2013), 52, 1149-1159, DOI:10.1021/bi3015407
• Solution NMR structure and dynamics of human apo-S100A1 protein, M. Nowakowski, Ł. Jaremko, M. Jaremko, I. Zhukov, A. Belczyk, A. Bierzyński, A. Ejchart, Journal of Structural Biology (2011), 174, 391, DOI:10.1016/j.jsb.2011.01.011
• Complexation of aminoglutethimide with native and modified cyclodextrins, M. Nowakowski, M. Długosz, J. Taraszewska, J. Wójcik, Journal of Physical Organic Chemistry (2009), 22, 948, DOI:10.1002/poc.1544
• N-(ureidoethyl)amides of cyclic enkephalin analogs, M. Ciszewska, M. Kwasiborska, M. Nowakowski, M. Oleszczuk, J. Wójcik, N. N. Chung, P. W. Schiller, J. Izdebski, Journal of Peptide Science (2009), 15, 312, DOI:10.1002/psc.1118
• New analogues of the Potent Cytotoxic Saponin OSW-1, A. Wojtkielewicz, M. Długosz, J. Maj, J. W. Morzycki, M. Nowakowski, J. Renkiewicz, M. Strnad, J. Swaczynova, A. Z. Wilczewska, J.Wójcik, Journal of Medicinal Chemistry (2007), 50, 3667-3673, DOI:10.1021/jm0613572
• Ureido group containing cyclic dermorphin (1 to 7) analogues: synthesis, biology and conphormation. E. Witkowska, M. Nowakowski, M. Oleszczuk, K. Filip, M. Ciszewska, N. N. Chung, P. W. Schiller, J. Wójcik, J. Izdebski, Journal of Peptide Science (2007), 13, 519, DOI:10.1002/psc.877
• Determination of association constats at moderately fast chemical exchange. Complexation of camphor enantiomers by α – cyclodextrin. P. Bernatowicz, M. Nowakowski, H. Dodziuk, A. Ejchart, Journal of Magnetic Resonanse (2006), 181, 304, DOI:10.1016/J.jmr.2006.06.001