Zobrazeno 1 - 10
of 151
pro vyhledávání: '"Klaus Fendler"'
Publikováno v:
PLoS ONE, Vol 12, Iss 7, p e0182293 (2017)
Na+/H+ exchange is essential for survival of all organisms, having a role in the regulation of the intracellular Na+ concentration, pH and cell volume. Furthermore, Na+/H+ exchangers were shown to be involved in the virulence of the bacterium Yersini
Externí odkaz:
https://doaj.org/article/318cdeed6d3944b387c7439ad247bdf2
Publikováno v:
PLoS ONE, Vol 11, Iss 5, p e0156392 (2016)
Bacterial sugar symporters in the Major Facilitator Superfamily (MFS) use the H+ (and in a few cases Na+) electrochemical gradients to achieve active transport of sugar into the cell. Because a number of structures of MFS sugar symporters have been s
Externí odkaz:
https://doaj.org/article/1931cb7e20264ad9bc8500f26913829f
Publikováno v:
The Journal of Biological Chemistry
Bacterial transporters are difficult to study using conventional electrophysiology because of their low transport rates and the small size of bacterial cells. Here, we applied solid-supported membrane–based electrophysiology to derive kinetic param
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::173ab5f163d13e9c80e23eacd2a83eef
http://europepmc.org/articles/PMC8784342
http://europepmc.org/articles/PMC8784342
Autor:
Natalie Kolesova, Marina Schrecker, Miyer Patiño-Ruiz, Vedrana Mikusevic, Klaus Fendler, Inga Hänelt
Publikováno v:
The Journal of General Physiology
KtrAB is a bacterial ion channel with a noncanonical selectivity filter. Consequently, it was assumed to be rather unselective for monovalent cations. Mikušević et al. show that in the presence of Na+, KtrAB very selectively translocates K+, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bdbd9d45944fc9a68ae2844791a800a
https://doi.org/10.1085/jgp.201912384
https://doi.org/10.1085/jgp.201912384
Autor:
Mehmet Karabel, Klaus Fendler, Miyer Patiño-Ruiz, Etana Padan, Octavian Călinescu, Manish Dwivedi
Publikováno v:
Journal of Biological Chemistry. 294:246-256
Much of the research on Na+/H+ exchange has been done in prokaryotic models, mainly on the NhaA Na+/H+-exchanger from Escherichia coli (EcNhaA). Two conserved aspartate residues, Asp-163 and Asp-164, are essential for transport and are candidates for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5618fb54d248c4269a46adac2b1a1898
https://doi.org/10.1074/jbc.ra118.004903
https://doi.org/10.1074/jbc.ra118.004903
Publikováno v:
PLoS ONE, Vol 9, Iss 7, p e101575 (2014)
Na+/H+ antiporters are integral membrane proteins that are present in almost every cell and in every kingdom of life. They are essential for the regulation of intracellular pH-value, Na+-concentration and cell volume. These secondary active transport
Externí odkaz:
https://doaj.org/article/c70f036df6274bf8b421154546e4d6ad
Autor:
Dudu Alkoby, Abraham Rimon, Maral Budak, Miyer Patino-Ruiz, Octavian Călinescu, Klaus Fendler, Etana Padan
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93200 (2014)
pH and Na+ homeostasis in all cells requires Na+/H+ antiporters. The crystal structure, obtained at pH 4, of NhaA, the main antiporter of Escherichia coli, has provided general insights into an antiporter mechanism and its unique pH regulation. Here,
Externí odkaz:
https://doaj.org/article/45fdba5362e94c6189d25e4480030d48
Publikováno v:
Biophysical Journal
The glucose transporter from Staphylococcus epidermidis, GlcPSe, is a homolog of the human GLUT sugar transporters of the major facilitator superfamily. Together with the xylose transporter from Escherichia coli, XylEEc, the other prominent prokaryot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d82add5d22a44f472c72489cdcbe5f44
http://europepmc.org/articles/PMC5770559
http://europepmc.org/articles/PMC5770559
Publikováno v:
PLoS ONE, Vol 5, Iss 9, p e12585 (2010)
BackgroundClC-7 is a ubiquitous transporter which is broadly expressed in mammalian tissues. It is implied in the pathogenesis of lysosomal storage disease and osteopetrosis. Because of its endosomal/lysosomal localization it is still poorly characte
Externí odkaz:
https://doaj.org/article/e46a718215eb4955be96d388cc537ab9
Publikováno v:
The Journal of Biological Chemistry
Na+/H+ antiporters are located in the cytoplasmic and intracellular membranes and play crucial roles in regulating intracellular pH, Na+, and volume. The NhaA antiporter of Escherichia coli is the best studied member of the Na+/H+ exchanger family an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cb9d08f9b0bf06b3ef9fa84f98c6367
http://europepmc.org/articles/PMC5427271
http://europepmc.org/articles/PMC5427271