Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Mikio, Tanabe"'
Autor:
Kumar Nagarathinam, Yoshiko Nakada-Nakura, Christoph Parthier, Tohru Terada, Narinobu Juge, Frank Jaenecke, Kehong Liu, Yunhon Hotta, Takaaki Miyaji, Hiroshi Omote, So Iwata, Norimichi Nomura, Milton T. Stubbs, Mikio Tanabe
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
The multidrug resistance transporter mediated efflux of antibiotics from the bacterial cytoplasm represents a major challenge to medicine. Here authors solve the X-ray crystallographic structure of the drug/H+ antiporter MdfA from Escherichia coli an
Externí odkaz:
https://doaj.org/article/9c31b685bee4442382a7b84e7402aa22
Myelin protein zero (MPZ or P0) is a major transmembrane protein expressed in peripheral compact myelin and functions to glue membranes to form multiple layered membranes characteristic of myelin. Intermembrane adhesion is mediated by homophilic inte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5072acbd0e79fc037160c299525b372b
https://doi.org/10.1101/2023.04.12.536520
https://doi.org/10.1101/2023.04.12.536520
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2524
Cell-free bioassays (CFBs) provide their own distinctive merits over cell-based bioassays (CBBs) including (i) rapid and on-site applicability, (ii) long-term utility, and (iii) bioanalytical versatility. The authors previously introduced a unique bi
Publikováno v:
Chemical Reviews
The major facilitator superfamily (MFS) is the largest known superfamily of secondary active transporters. MFS transporters are responsible for transporting a broad spectrum of substrates, either down their concentration gradient or uphill using the
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
An improved, fully automated protein crystallization and monitoring system, PXS2, can perform crystallization using smaller protein samples than the previous version. In addition, PXS2 can be used for membrane-protein crystallization using the bicell
Publikováno v:
Bioluminescence ISBN: 9781071624524
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ace3261f95905fdb15be491116837efe
https://doi.org/10.1007/978-1-0716-2453-1_7
https://doi.org/10.1007/978-1-0716-2453-1_7
Protein complexes exert various functions through allosterically controlled cooperative work. De novo design of allosteric control into protein complexes provides understanding of their working principles and potential tools for synthetic biology. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8834d29c0486d1a75cddb8804229cc6
https://doi.org/10.1101/2020.09.09.288571
https://doi.org/10.1101/2020.09.09.288571
Autor:
Takeshi Murata, Ryuichi Kato, Mikio Tanabe, Tomoki Akiyama, Tomohiko Hayashi, Toshiya Senda, Kano Suzuki, Yuki Sudo, Masahiro Kinoshita, Satoshi Yasuda, Kanae Kanehara, Keiichi Kojima
Publikováno v:
The journal of physical chemistry. B. 124(6)
We often encounter a case where two proteins, whose amino-acid sequences are similar, are quite different with regard to the thermostability. As a striking example, we consider the two seven-transmembrane proteins: recently discovered Rubrobacter xyl
Autor:
Axel Munk, Mikio Tanabe, Annika Bartsch, Christof Kattner, Salomé Llabrés, Florian Pein, Ulrich Zachariae, Manuel Diehn, Callum M. Ives, Claudia Steinem
Publikováno v:
Biochimica et Biophysica Acta. Biomembranes
Gram-negative bacteria cause the majority of highly drug-resistant bacterial infections. To cross the outer membrane of the complex Gram-negative cell envelope, antibiotics permeate through porins, trimeric channel proteins that enable the exchange o
Autor:
So Iwata, Norimichi Nomura, Milton T. Stubbs, Yunhon Hotta, Yoshiko Nakada-Nakura, Kumar Nagarathinam, Kehong Liu, Frank Jaenecke, Mikio Tanabe
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 73:423-430
The active efflux of antibiotics by multidrug-resistance (MDR) transporters is a major pathway of drug resistance and complicates the clinical treatment of bacterial infections. MdfA is a member of the major facilitator superfamily (MFS) fromEscheric