Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Gvantsa Chkadua"'
Autor:
Marina Nikolaishvili, Zakaria Nanobashvili, Nodar Mitagvaria, Gvantsa Chkadua, Tea Museliani, Gogi Jikia, Irine Bilanishvili, Khatuna Dondoladze
Publikováno v:
Open Access Macedonian Journal of Medical Sciences. 10:2555-2565
Introduction: The elucidation of the mechanism of action of radon on antioxidant processes needs further research, however, based on the results of the experiment, it can be concluded that studies on experimental animals have shown that, while inhali
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8a595e1ae218f37e775cf7a4a7e232e7
https://doi.org/10.3889/oamjms.2022.10716
https://doi.org/10.3889/oamjms.2022.10716
Autor:
Gvantsa Chkadua, Eka Nozadze, Leila Tsakadze, Lia Shioshvili, Nana Arutinova, Marine Leladze, Sopio Dzneladze, Maia Javakhishvili
Publikováno v:
Journal of Bioenergetics and Biomembranes. 54:241-249
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c399ef92f982f37aa25d71840667e697
https://doi.org/10.1007/s10863-022-09948-1
https://doi.org/10.1007/s10863-022-09948-1
Autor:
Marine Nikolaishvili, Zaqaria Nanobashvili, Nodar Mitagvaria, Gvantsa Chkadua, Tea Museliani, Khatuna Dondoladze, Gogi Jikia
Publikováno v:
Journal of Biosciences and Medicines. 10:212-227
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0272c09e5d8e5c67242ec1a28149a27c
https://doi.org/10.4236/jbm.2022.103020
https://doi.org/10.4236/jbm.2022.103020
Autor:
Marine Nikolaishvili, Zaqaria Nanobashvili, Nodar Mitagvaria, Gvantsa Chkadua, Khatuna Dondoladze, Salome Omiadze, Sesili Beriashvili, Tamar Ordenidze, Mariam Nikuradze
Publikováno v:
Current Innovations in Medicine and Medical Science Vol. 6 ISBN: 9789355478979
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61a35334800117a0c8ea326ea3bdbe43
https://doi.org/10.9734/bpi/cimms/v6/3660b
https://doi.org/10.9734/bpi/cimms/v6/3660b
Autor:
Gvantsa, Chkadua, Eka, Nozadze, Leila, Tsakadze, Lia, Shioshvili, Nana, Arutinova, Marine, Leladze, Sopio, Dzneladze, Maia, Javakhishvili
Publikováno v:
Journal of bioenergetics and biomembranes. 54(5-6)
Na,K-ATPase is a member of the P-type ATPase family, which transforms the energy of ATP to the transmembrane Na/K gradient that is used to create membrane potential, support the excitability of neurons and myocytes, control pH, and transport substanc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::90a1cdef83059ba260a043d58fc21f26
https://pubmed.ncbi.nlm.nih.gov/36331672
https://pubmed.ncbi.nlm.nih.gov/36331672
Autor:
Nana Arutinova, Leila Tsakadze, Eka Nozadze, Sopio Dzneladze, Marina Leladze, Gvantsa Chkadua, Lia Shioshvili
Publikováno v:
The Journal of Membrane Biology. 248:53-58
The comparative analysis between two enzymes, Mg-dependent and Mg-independent HCO3 − ATPases, were studied in synaptosomal and microsomal membrane fractions of albino rat brain, using the method of kinetic analysis of the multi-sited enzyme systems
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e363f7f8017cae2031539bf425a7d6d
https://doi.org/10.1007/s00232-014-9739-8
https://doi.org/10.1007/s00232-014-9739-8
Autor:
Marina Leladze, Nana Arutinova, Sopio Dzneladze, Eka Nozadze, Leila Tsakadze, Gvantsa Chkadua, Lia Shioshvili
Publikováno v:
The Journal of membrane biology. 248(2)
Mg-ATPase is very important in living organisms. To better understand the molecular mechanism of Mg-ATPase activity, we applied the method of kinetic analysis of multi-sited enzyme systems; this is a suitable approach used for kinetic investigation o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6797e0286d45cd0ddfcf5e0d4392780
https://pubmed.ncbi.nlm.nih.gov/25567360
https://pubmed.ncbi.nlm.nih.gov/25567360
Publikováno v:
Biological trace element research. 144(1-3)
Mn(2+) stimulated change of Mg-ATPase activity has been found in the synaptic fraction of rat brain that was named Mn-ATPase. Investigation of the molecular mechanism has shown that Mn-ATPase is a multi-sited enzyme system whose minimum functional un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fd8d165be327905aa76569452f321fb
https://pubmed.ncbi.nlm.nih.gov/21559873
https://pubmed.ncbi.nlm.nih.gov/21559873