Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Tetsuhiro Kawabe"'
Publikováno v:
Biochemistry. 61:1548-1553
Publikováno v:
Biochemistry. 61(15)
NADP
Autor:
Kazuhiro Tetsuka, Laura M Tool, Fumiko Kiyonaga, Marianne K. Vormann, Akira Fujimori, Masato Ohbuchi, Paul Vulto, Thomas Hankemeier, Takayuki Goto, Remko van Vught, Linda Gijzen, Henriëtte L. Lanz, Tetsuhiro Kawabe
Publikováno v:
Kidney360
Background: Renal ischemia/reperfusion injury (rIRI) is one of the major causes of acute kidney injury (AKI). While animal models are suitable for investigating systemic symptoms of AKI they are limited in translatability. Human in vitro models are c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13dda44bc10390b4a5e7a95719ab5001
https://europepmc.org/articles/PMC8967632/
https://europepmc.org/articles/PMC8967632/
Autor:
Masato Ohbuchi, Kaori Takama, Shunji Yamazaki, Akira Fujimori, Kazuhiro Tetsuka, Takayuki Goto, Fumiko Kiyonaga, Tetsuhiro Kawabe
Publikováno v:
Biologicalpharmaceutical bulletin. 43(3)
Recent progress in the fields of tissue engineering, micro-electro mechanical systems, and materials science have greatly improved cell culture systems, which were traditionally performed in a static two-dimensional manner. This progress has led to a
Publikováno v:
Biochemistry. 37:5475-5480
Seven arginine residues are conserved in all the tetracycline/H+ antiporters of Gram-negative bacteria. Four (Arg67, -70, -71, and -127) of them are located in the putative cytoplasmic loop regions and three (Arg31, -101, and -238) in the putative pe
Publikováno v:
The Journal of biological chemistry. 275(50)
Multidrurg resistance-associated protein 2 (MRP2)/canalicular multispecific organic anion transporter (cMOAT) is involved in the ATP-dependent export of organic anions across the bile canalicular membrane. To identify functional amino acid residues t
Publikováno v:
Journal of biochemistry. 128(2)
The AcrAB system of Escherichia coli is an intrinsic efflux protein with a broad substrate specificity. AcrA was thought to be localized in the periplasmic space, and to be linked to AcrB and TolC. The AcrAB-TolC system directly exports diverse subst
Publikováno v:
The Journal of biological chemistry. 275(8)
Our previous study on second-site suppressor mutations of the Tn10-encoded metal-tetracycline/H(+) antiporter suggested that Leu(30) and Ala(354), located in periplasmic loop 1-2 and 11-12, respectively, are conformationally linked to each other (Kaw
Autor:
Akihito Yamaguchi, Tetsuhiro Kawabe
Publikováno v:
FEBS Letters. (1):169-173
Gly-332 is a conformationally important residue of the Tn 10 -encoded metal-tetracycline/H + antiporter (TetA(B)), which was found by random mutagenesis and confirmed by site-directed mutagenesis. A bulky side chain at position 332 is deleterious to