Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Bosmat Refaeli"'
Autor:
Khiem Nguyen, Tali Strauss, Bosmat Refaeli, Reuben Hiller, Olga Vinogradova, Daniel Khananshvili
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 13, p 6909 (2024)
Consecutive interactions of 3Na+ or 1Ca2+ with the Na+/Ca2+ exchanger (NCX) result in an alternative exposure (access) of the cytosolic and extracellular vestibules to opposite sides of the membrane, where ion-induced transitions between the outward-
Externí odkaz:
https://doaj.org/article/f0a76753fab442579d82f065f02b56ed
Autor:
Moshe Giladi, Sunayana Mitra, Luba Simhaev, Reuben Hiller, Bosmat Refaeli, Tali Strauss, Carlos R. Baiz, Daniel Khananshvili
Publikováno v:
Cell Calcium
The plasma membrane (NCX) and mitochondrial (NCLX) Na(+)/Ca(2+) exchangers are structurally related proteins, although they operate under strictly different ionic conditions and membrane potentials. In contrast with NCX, NCLX can transport either Li(
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f83185ac9383618f0f129844aee8121f
https://europepmc.org/articles/PMC10124574/
https://europepmc.org/articles/PMC10124574/
Autor:
Moshe Giladi, Reuben Hiller, Liat van Dijk, Mary Hongying Cheng, Daniel Khananshvili, Bosmat Refaeli, Ivet Bahar
Publikováno v:
Cell Calcium. 76:10-22
Prokaryotic and eukaryotic Na(+)/Ca(2+) exchangers (NCX) control Ca(2+) homeostasis. NCX orthologs exhibit up to 10(4)-fold differences in their turnover rates (k(cat)), whereas the ratios between the cytosolic (cyt) and extracellular (ext) K(m) valu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::485b2f48084a0273f72a918e296a3552
https://doi.org/10.1016/j.ceca.2018.09.004
https://doi.org/10.1016/j.ceca.2018.09.004
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1864:183792
The Na+/Ca2+ exchangers (NCXs) modulate the Ca2+ signaling and homeostasis in health and disease. The transport cycle turnover rates (kcat) and the kcat/Km values of eukaryotic NCXs are ~104-times higher than those of prokaryotic NCXs. Three ion-coor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68aecde13d4c59affcbd712612668873
https://doi.org/10.1016/j.bbamem.2021.183792
https://doi.org/10.1016/j.bbamem.2021.183792
Autor:
Stephanie Liu, Moshe Giladi, Reuben Hiller, Carlos R. Baiz, Bosmat Refaeli, Daniel Khananshvili
Publikováno v:
Cell Calcium
The cytosolic pH decline from 7.2 to 6.9 results in 90% inactivation of mammalian Na(+)/Ca(2+) exchangers (NCXs) due to protons interactions with regulatory and transport domains (“proton block”). Remarkably, the pH titration curves of mammalian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::806622648a63f97024aa4fa1e84ebdac
https://doi.org/10.1016/j.ceca.2021.102476
https://doi.org/10.1016/j.ceca.2021.102476
Autor:
Masayo, Iwaki, Bosmat, Refaeli, Liat, van Dijk, Reuben, Hiller, Moshe, Giladi, Hideki, Kandori, Daniel, Khananshvili
Publikováno v:
The FEBS journalReferences. 287(21)
Selective recognition and transport of Na
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d25e5939b749d5540617f3df1b3af589
https://pubmed.ncbi.nlm.nih.gov/32056381
https://pubmed.ncbi.nlm.nih.gov/32056381
Autor:
Moshe, Giladi, Su Youn, Lee, Bosmat, Refaeli, Reuben, Hiller, Ka Young, Chung, Daniel, Khananshvili
Publikováno v:
Biochimica et biophysica acta. Bioenergetics. 1860(3)
The cell membrane (NCX) and mitochondrial (NCLX) Na
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::32890c77f59911ced738f94feddc21ea
https://pubmed.ncbi.nlm.nih.gov/30414928
https://pubmed.ncbi.nlm.nih.gov/30414928
Autor:
Bosmat Refaeli, Petr Man, Liat van Dijk, Moshe Giladi, Eric Forest, Daniel Khananshvili, Lior Almagor, Reuben Hiller
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (29), pp.12311-12323. ⟨10.1074/jbc.M117.787168⟩
Journal of Biological Chemistry, 2017, 292 (29), pp.12311-12323. ⟨10.1074/jbc.M117.787168⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (29), pp.12311-12323. ⟨10.1074/jbc.M117.787168⟩
Journal of Biological Chemistry, 2017, 292 (29), pp.12311-12323. ⟨10.1074/jbc.M117.787168⟩
International audience; Na(+)/Ca(2+) exchanger (NCX) proteins operate through the alternating access mechanism, where the ion-binding pocket is exposed in succession either to the extracellular or the intracellular face of the membrane. The archaeal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db149f8e673c6fd57bdf26a6166aeece
https://hal.archives-ouvertes.fr/hal-01647025
https://hal.archives-ouvertes.fr/hal-01647025
Autor:
Moshe, Giladi, Liat, van Dijk, Bosmat, Refaeli, Lior, Almagor, Reuben, Hiller, Petr, Man, Eric, Forest, Daniel, Khananshvili
Publikováno v:
The Journal of biological chemistry. 292(29)
Na+/Ca2+ exchanger (NCX) proteins operate through the alternating access mechanism, where the ion-binding pocket is exposed in succession either to the extracellular or the intracellular face of the membrane. The archaeal NCX_Mj (Methanococcus jannas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a42ab9af1cc70303e0d1a5b3ce9221d0
https://pubmed.ncbi.nlm.nih.gov/28572509
https://pubmed.ncbi.nlm.nih.gov/28572509
Autor:
Polina Kornilov, Sun Choi, Moshe Rehavi, Netta Roz, Bernard Attali, Karam Son, Yoonji Lee, Jin Hee Lee, Asher Peretz, Bosmat Refaeli
Publikováno v:
The FASEB Journal. 28:2591-2602
Some of the fascinating features of voltage-sensing domains (VSDs) in voltage-gated cation channels (VGCCs) are their modular nature and adaptability. Here we examined the VSD sensitivity of different VGCCs to 2 structurally related nontoxin gating m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::501f38d53713571f65c7db2ca0b64542
https://doi.org/10.1096/fj.14-250647
https://doi.org/10.1096/fj.14-250647