Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Christoph Heinrich, Strunk"'
Autor:
Pablo Perez-Garcia, Stefanie Kobus, Christoph G. W. Gertzen, Astrid Hoeppner, Nicholas Holzscheck, Christoph Heinrich Strunk, Harald Huber, Karl-Erich Jaeger, Holger Gohlke, Filip Kovacic, Sander H. J. Smits, Wolfgang R. Streit, Jennifer Chow
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues. This structure provides insight as to the evolution of metallo-beta-lactamases and their
Externí odkaz:
https://doaj.org/article/882f23538291485d9a533860520c28aa
Autor:
Muttalip Caliskan, Gereon Poschmann, Mirja Gudzuhn, Daniel Waldera-Lupa, Rebecka Molitor, Christoph Heinrich Strunk, Wolfgang R. Streit, Karl-Erich Jaeger, Kai Stühler, Filip Kovacic
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 1868:159317
Autor:
Jennifer Chow, Christoph Heinrich Strunk, Astrid Hoeppner, Holger Gohlke, Filip Kovacic, Wolfgang R. Streit, Harald Huber, Karl-Erich Jaeger, Nicholas Holzscheck, Sander H. J. Smits, Pablo Pérez-García, Stefanie Kobus, Christoph G. W. Gertzen
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Communications biology 4(1), 132 (2021). doi:10.1038/s42003-021-01671-8
Communications Biology
'Communications Biology ', vol: 4, pages: 132-1-132-12 (2021)
Communications biology 4(1), 132 (2021). doi:10.1038/s42003-021-01671-8
Communications Biology
'Communications Biology ', vol: 4, pages: 132-1-132-12 (2021)
The metallo-β-lactamase fold is an ancient protein structure present in numerous enzyme families responsible for diverse biological processes. The crystal structure of the hyperthermostable crenarchaeal enzyme Igni18 from Ignicoccus hospitalis was s
Autor:
Sabahuddin, Ahmad, Christoph Heinrich, Strunk, Stephan N, Schott-Verdugo, Karl-Erich, Jaeger, Filip, Kovacic, Holger, Gohlke
Publikováno v:
Journal of chemical information and modeling. 61(11)
PlaF is a cytoplasmic membrane-bound phospholipase A
Autor:
Filip Kovacic, Christoph Heinrich Strunk, Stephan Schott-Verdugo, Sabahuddin Ahmad, Karl-Erich Jaeger, Holger Gohlke
PlaF is a cytoplasmic membrane-bound phospholipase A1 from Pseudomonas aeruginosa that alters the membrane glycerophospholipid (GPL) composition and fosters the virulence of this human pathogen. PlaF activity is regulated by a dimer-to-monomer transi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a842beb2e8f21621df869bfc5a63f089
https://doi.org/10.1101/2021.06.29.450291
https://doi.org/10.1101/2021.06.29.450291
Autor:
Stephan Schott-Verdugo, Christoph Heinrich Strunk, Sabahuddin Ahmad, Holger Gohlke, Filip Kovacic, Karl-Erich Jaeger
Publikováno v:
Journal of chemical information and modeling 61(11), 5626–5643 (2021). doi:10.1021/acs.jcim.1c00973
PlaF is a cytoplasmic membrane-bound phospholipase A1 from Pseudomonas aeruginosa that alters the membrane glycerophospholipid (GPL) composition and fosters the virulence of this human pathogen. PlaF activity is regulated by a dimer-to-monomer transi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc1f1c2f75e9dfc8d65b64986ad4fd9d
https://juser.fz-juelich.de/record/902474
https://juser.fz-juelich.de/record/902474