Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Björn Claussen"'
Autor:
Lena Schleicher, Valentin Muras, Björn Claussen, Jens Pfannstiel, Bastian Blombach, Pavel Dibrov, Günter Fritz, Julia Steuber
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Escherichia coli is a convenient host for the expression of proteins, but the heterologous production of large membrane protein complexes often is hampered by the lack of specific accessory genes required for membrane insertion or cofactor assembly.
Externí odkaz:
https://doaj.org/article/16bdcd40b5a2492fb9201bbb741b2c99
Autor:
Olaf Voolstra, Philipp Spät, Claudia Oberegelsbacher, Björn Claussen, Jens Pfannstiel, Armin Huber
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0122039 (2015)
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein that tethers components of the phototransduction cascade to form a supramolecular signaling complex. Here, we report the identification of eight INAD ph
Externí odkaz:
https://doaj.org/article/f4c8879eeddc43b29e62d85a696c3aad
Publikováno v:
Analytical Biochemistry. 537:56-59
We demonstrate the miniaturization of an enzymatic assay for the determination of NADH oxidation and quinone reduction by the Na+ -translocating NADH quinone oxidoreductase (NQR) in the 96-well plate format. The assay is based on the spectrophotometr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f50bea22017b605239fc6313c65a735c
https://doi.org/10.1016/j.ab.2017.08.025
https://doi.org/10.1016/j.ab.2017.08.025
Publikováno v:
Analytical biochemistry. 537
We demonstrate the miniaturization of an enzymatic assay for the determination of NADH oxidation and quinone reduction by the Na
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::87dbee0dca060525a2867570290428ef
https://pubmed.ncbi.nlm.nih.gov/28870828
https://pubmed.ncbi.nlm.nih.gov/28870828
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
Publikováno v:
Biological chemistry. 398(2)
The Na+-translocating NADH:quinone oxidoreductase (NQR) is the entry site for electrons into the respiratory chain of Vibrio cholerae, the causative agent of cholera disease. NQR couples the electron transfer from NADH to ubiquinone to the translocat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87109349ee83fcbbcbed85199740587d
https://pubmed.ncbi.nlm.nih.gov/27639271
https://pubmed.ncbi.nlm.nih.gov/27639271
Autor:
Björn Claussen, Armin Huber, Jens Pfannstiel, Olaf Voolstra, Philipp Spät, Claudia Oberegelsbacher
Publikováno v:
PLoS ONE, Vol 10, Iss 3, p e0122039 (2015)
PLoS ONE
PLoS ONE
Drosophila inactivation no afterpotential D (INAD) is a PDZ domain-containing scaffolding protein that tethers components of the phototransduction cascade to form a supramolecular signaling complex. Here, we report the identification of eight INAD ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e1bd9bff301b050b43d3b2be0875fb9
http://europepmc.org/articles/PMC4370639?pdf=render
http://europepmc.org/articles/PMC4370639?pdf=render