Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Miyer Patiño-Ruiz"'
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:
International Journal of Molecular Sciences. 23(16)
Na+/H+ exchangers are essential for Na+ and pH homeostasis in all organisms. Human Na+/H+ exchangers are of high medical interest, and insights into their structure and function are aided by the investigation of prokaryotic homologues. Most prokaryot
Publikováno v:
International journal of molecular sciences. 23(16)
Na
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
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
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
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Bacterial NhaB Na+/H+ exchangers belonging to the Ion Transporter superfamily are poorly characterized in contrast to Na+/H+ exchangers of the Cation Proton Antiporter superfamily which have NhaA from Escherichia coli as a prominent member. For a mor
Autor:
Miyer, Patiño-Ruiz, Manish, Dwivedi, Octavian, Călinescu, Mehmet, Karabel, Etana, Padan, Klaus, Fendler
Publikováno v:
The Journal of biological chemistry. 294(1)
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 candid
Autor:
Jenifer Cuesta-Bernal, Luz-Mary Salazar, Miyer Patiño-Ruiz, Andrés León-Torres, Carlos-Yesid Soto, David Landsman, Leonardo Mariño-Ramírez, Lorena Novoa-Aponte
Publikováno v:
BMC Structural Biology, Vol 12, Iss 1, p 25 (2012)
BMC Structural Biology
BMC Structural Biology
Background P-type ATPases hydrolyze ATP and release energy that is used in the transport of ions against electrochemical gradients across plasma membranes, making these proteins essential for cell viability. Currently, the distribution and function o
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