Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Krzysztof M, Zak"'
Autor:
Lena Münzker, Serah W. Kimani, Milan M. Fowkes, Aiping Dong, Hong Zheng, Yanjun Li, Morgan Dasovich, Krzysztof M. Zak, Anthony K. L. Leung, Jonathan M. Elkins, Dirk Kessler, Cheryl H. Arrowsmith, Levon Halabelian, Jark Böttcher
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-15 (2024)
Abstract The WWE domain is a relatively under-researched domain found in twelve human proteins and characterized by a conserved tryptophan-tryptophan-glutamate (WWE) sequence motif. Six of these WWE domain-containing proteins also contain domains wit
Externí odkaz:
https://doaj.org/article/d563b7d731e84d30bedff15301871bf2
Autor:
Stefan Gaussmann, Rebecca Peschel, Julia Ott, Krzysztof M. Zak, Judit Sastre, Florent Delhommel, Grzegorz M. Popowicz, Job Boekhoven, Wolfgang Schliebs, Ralf Erdmann, Michael Sattler
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-17 (2024)
Abstract Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. By combining biochemical methods and structural biology, we show that the C-terminal SH3 domain of PEX13 mediates intramolecular interactions with a proximal FxxxF motif.
Externí odkaz:
https://doaj.org/article/89d258036d6146bbb1acbb853157ad7f
Autor:
Elżbieta Wątor, Piotr Wilk, Artur Biela, Michał Rawski, Krzysztof M. Zak, Wieland Steinchen, Gert Bange, Sebastian Glatt, Przemysław Grudnik
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-14 (2023)
eIF5A is the only protein known to contain hypusine. Here, the authors present the cryoEM structure of the eIF5A-DHS complex and provide mechanistic insights to understand the deoxyhypusination reaction and hypusination-related neurodegeneration.
Externí odkaz:
https://doaj.org/article/e4e3adc8dd2e42ca879034e54b682cda
Autor:
Krzysztof M. Zak, Mark J. Bostock, Irena Waligorska, Ida B. Thøgersen, Jan J. Enghild, Grzegorz M. Popowicz, Przemyslaw Grudnik, Jan Potempa, Miroslaw Ksiazek
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 1267-1281 (2021)
Mirolysin is a secretory protease of Tannerella forsythia, a member of the dysbiotic oral microbiota responsible for periodontitis. In this study, we show that mirolysin latency is achieved by a “cysteine-switch” mechanism exerted by Cys23 in the
Externí odkaz:
https://doaj.org/article/facc41ee0c7f40019822708c69e05cfb
Autor:
Stefan Gaussmann, Julia Ott, Krzysztof M. Zak, Florent Delhommel, Grzegorz M. Popowicz, Wolfgang Schliebs, Ralf Erdmann, Michael Sattler
Targeting and import of peroxisomal proteins depends on PEX5, PEX14 and PEX13. We present a biochemical and structural characterization of the PEX13 C-terminal region. By combining NMR spectroscopy, X-ray crystallography and biochemical methods, we s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::549f3d0547a0d835e68046535dc56890
https://doi.org/10.1101/2022.12.19.520972
https://doi.org/10.1101/2022.12.19.520972
Autor:
Krzysztof M. Zak, Magdalena Kalińska, Elżbieta Wątor, Katarzyna Kuśka, Rościsław Krutyhołowa, Grzegorz Dubin, Grzegorz M. Popowicz, Przemysław Grudnik
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 19, p 4821 (2019)
Glucose phosphorylating enzymes are crucial in the regulation of basic cellular processes, including metabolism and gene expression. Glucokinases and hexokinases provide a pool of phosphorylated glucose in an adenosine diphosphate (ADP)- and ATP-depe
Externí odkaz:
https://doaj.org/article/bd596ffac00d4773afbf45c1807e58b7
Autor:
Maximilian M. Biebl, Florent Delhommel, Ofrah Faust, Krzysztof M. Zak, Ganesh Agam, Xiaoyan Guo, Moritz Mühlhofer, Vinay Dahiya, Daniela Hillebrand, Grzegorz M. Popowicz, Martin Kampmann, Don C. Lamb, Rina Rosenzweig, Michael Sattler, Johannes Buchner
Publikováno v:
Mol. Cell 82, 555-569.e7 (2022)
Molecular Cell
Molecular Cell
In the eukaryotic cytosol, the Hsp70 and the Hsp90 chaperone machines work in tandem with the maturation of a diverse array of client proteins. The transfer of nonnative clients between these systems is essential to the chaperoning process, but how i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d06ad9f467968faed6ec9051da167d1
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=64217
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=64217
Autor:
Ida B. Thøgersen, Krzysztof M. Zak, Mark J Bostock, Jan Potempa, Irena Waligorska, Jan J. Enghild, Grzegorz M Popowicz, Przemyslaw Grudnik, Miroslaw Ksiazek
Publikováno v:
Zak, K M, Bostock, M J, Waligorska, I, Thøgersen, I B, Enghild, J J, Popowicz, G M, Grudnik, P, Potempa, J & Ksiazek, M 2021, ' Latency, thermal stability, and identification of an inhibitory compound of mirolysin, a secretory protease of the human periodontopathogen Tannerella forsythia ', Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 36, no. 1, pp. 1267-1281 . https://doi.org/10.1080/14756366.2021.1937619
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 1267-1281 (2021)
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 1267-1281 (2021)
Mirolysin is a secretory protease of Tannerella forsythia, a member of the dysbiotic oral microbiota responsible for periodontitis. In this study, we show that mirolysin latency is achieved by a “cysteine-switch” mechanism exerted by Cys23 in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfe83f78b12e748673165bea71b66b00
Autor:
Hans Zischka, Thomas Damgaard Sandahl, Andrew H Coles, Ruth Viana, Sabine Borchard, Sandra M. Müller, Thomas Plitz, Carola Eberhagen, Krzysztof M. Zak, Josef Lichtmannegger, Claudia Einer, Tanja Schwerdtle, Tamara Rieder, Grzegorz M Popowicz, Albrecht Wieser, Martin Klingenspor, Stefanie Raschke, Jerzy Adamski, Elisabeth Weber, Mikkel H. Vendelbo, Bernhard Michalke
Publikováno v:
Life Science Alliance
'Life Science Alliance ', vol: 5, pages: e202101164-1-e202101164-16 (2022)
Borchard, S, Raschke, S, Zak, K M, Eberhagen, C, Einer, C, Weber, E, Müller, S M, Michalke, B, Lichtmannegger, J, Wieser, A, Rieder, T, Popowicz, G M, Adamski, J, Klingenspor, M, Coles, A H, Viana, R, Vendelbo, M H, Sandahl, T D, Schwerdtle, T, Plitz, T & Zischka, H 2021, ' Bis-choline tetrathiomolybdate prevents copper-induced blood-brain barrier damage ', Life science alliance, vol. 5, no. 3, e202101164 . https://doi.org/10.26508/lsa.202101164
'Life Science Alliance ', vol: 5, pages: e202101164-1-e202101164-16 (2022)
Borchard, S, Raschke, S, Zak, K M, Eberhagen, C, Einer, C, Weber, E, Müller, S M, Michalke, B, Lichtmannegger, J, Wieser, A, Rieder, T, Popowicz, G M, Adamski, J, Klingenspor, M, Coles, A H, Viana, R, Vendelbo, M H, Sandahl, T D, Schwerdtle, T, Plitz, T & Zischka, H 2021, ' Bis-choline tetrathiomolybdate prevents copper-induced blood-brain barrier damage ', Life science alliance, vol. 5, no. 3, e202101164 . https://doi.org/10.26508/lsa.202101164
The blood–brain barrier endothelial cell monolayer becomes permeable to elevated copper loosely bound to albumin, which can be avoided by a high-affinity copper chelator but not by D-penicillamine.
In Wilson disease, excessive copper accumulat
In Wilson disease, excessive copper accumulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a65c0b7183eb41717035aca40864783
https://mediatum.ub.tum.de/doc/1689921/document.pdf
https://mediatum.ub.tum.de/doc/1689921/document.pdf
Autor:
Michael Sattler, Grzegorz M Popowicz, Ramona Mejdi-Nitiu, Marta Kolonko, Mark J Bostock, Richard Xu Zhou, Roberto Fino, Charlotte A Softley, Krzysztof M. Zak, Hannelore Meyer
Publikováno v:
Antimicrobial Agents and Chemotherapy
Multidrug resistance among Gram-negative bacteria is a major global public health threat. Metallo-β-lactamases (MBLs) target the most widely used antibiotic class, the β-lactams, including the most recent generation of carbapenems. Interspecies spr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c053c3979aad5f801b24c574760a9cd5
https://pubmed.ncbi.nlm.nih.gov/32205343
https://pubmed.ncbi.nlm.nih.gov/32205343