Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Marco S. Casutt"'
Autor:
Günter Fritz, Marco S. Casutt, Georg Vohl, Julia Steuber, Heiko M. Möller, Kay Diederichs, Björn Claussen, Ruslan Nedielkov, Thomas Vorburger
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 70:987-992
The Na+-translocating NADH:ubiquinone oxidoreductase (Na+-NQR) fromVibrio choleraeis a membrane protein complex consisting of six different subunits NqrA–NqrF. The major domains of the NqrA and NqrC subunits were heterologously expressed inEscheric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce7cd5b3004e41bde279768f021692cf
https://doi.org/10.1107/s2053230x14009881
https://doi.org/10.1107/s2053230x14009881
Autor:
Anja Basters, Lars Ketscher, Eberhard Krause, Huib Ovaa, Paul P. Geurink, Farid El Oualid, Günter Fritz, Marco S. Casutt, Klaus-Peter Knobeloch
Publikováno v:
FEBS Journal. 281:1918-1928
Protein modification by interferon-stimulated gene 15 (ISG15), an ubiquitin-like modifier, affects multiple cellular functions and represents one of the major antiviral effector systems. Covalent linkage of ISG15 to proteins was previously reported t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56d5413fda7cfc2fce119e253c3e51f8
https://doi.org/10.1111/febs.12754
https://doi.org/10.1111/febs.12754
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:1817-1822
The Na + -translocating NADH:quinone oxidoreductase (Na + -NQR) is the prototype of a novel class of flavoproteins carrying a riboflavin phosphate bound to serine or threonine by a phosphodiester bond to the ribityl side chain. This membrane-bound, r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::240ce06dd00e8330c65efad82bfba106
https://doi.org/10.1016/j.bbabio.2012.02.012
https://doi.org/10.1016/j.bbabio.2012.02.012
Autor:
Julia Steuber, Christiane Schaffitzel, Vladimir Y. Lunin, N.L. Lunina, Marco S. Casutt, Manfred W. Baumstark, Günter Fritz, Kèvin Knoops
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 68:724-731
A low-resolution structure of the Na(+)-translocating NADH:ubiquinone oxidoreductase from the human pathogen Vibrio cholerae was determined by ab initio phasing and independently confirmed by electron microscopy. This multi-subunit membrane-protein c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2275bcfe7d3003cb660676f7628b620
https://doi.org/10.1107/s0907444912012012
https://doi.org/10.1107/s0907444912012012
Publikováno v:
Journal of Biological Chemistry. 285:27088-27099
The sodium ion-translocating NADH:quinone oxidoreductase (Na(+)-NQR) from the human pathogen Vibrio cholerae is a respiratory membrane protein complex that couples the oxidation of NADH to the transport of Na(+) across the bacterial membrane. The Na(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::716b77a2b529b343035d03b549344e1e
https://doi.org/10.1074/jbc.m109.071126
https://doi.org/10.1074/jbc.m109.071126
NADH oxidation in the respiratory chain is coupled to ion translocation across the membrane to build up an electrochemical gradient. The sodium-translocating NADH:quinone oxidoreductase (Na+-NQR), a membrane protein complex widespread among pathogeni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3117dc63d74265635f95964bcb6c2b27
Autor:
Uwe Gerken, Ruslan Nedielkov, Hideto Miyoshi, Severin Wendelspiess, Masatoshi Murai, Julia Steuber, Sara Vossler, Marco S. Casutt, Heiko M. Möller
Na(+) is the second major coupling ion at membranes after protons, and many pathogenic bacteria use the sodium-motive force to their advantage. A prominent example is Vibrio cholerae, which relies on the Na(+)-pumping NADH:quinone oxidoreductase (Na(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96d68d28133417b5dbea94e4ea1d23c1
The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae couples the exergonic oxidation of NADH by membrane-bound quinone to Na+ translocation across the membrane. Na+-NQR consists of six different subunits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c21253a44a1074d93d1eb3483862501a
https://doi.org/10.5167/uzh-43090
https://doi.org/10.5167/uzh-43090
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. (7-8):696-702
The Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) from the human pathogen Vibrio cholerae is a respiratory flavo-FeS complex composed of the six subunits NqrA-F. The Na(+)-NQR was produced as His(6)-tagged protein by homologous expressi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6ec45bb6c1628113ac4c2fa1523a36e
Autor:
Wojtek Steffen, Guenter Fritz, Georg Vohl, Valentin Muras, Thomas Vorburger, Marco S. Casutt, Julia Steuber
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. :S62
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d22d499d7b43eb0ab02103fd8ee73a51