Zobrazeno 1 - 10
of 83
pro vyhledávání: '"E. DeMet"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Three allosteric glycolytic enzymes, phosphofructokinase, glyceraldehyde-3 phosphate dehydrogenase and pyruvate kinase, associated with bacterial, parasitic and human species, were explored to identify potential allosteric sites that would be used as
Externí odkaz:
https://doaj.org/article/0761870798c449fab3b165fb0cecb176
Autor:
Akbaş, E. Demet1 edemetakbas@gmail.com, Yüreğir, Ö. Özalp2, Anlaş, Ö.2, Özçelik, Z.3, Tolunay, O. Zerrin1
Publikováno v:
Acta Endocrinologica (1841-0987). Jul-Sep2021, Vol. 17 Issue 3, p399-401. 3p.
Akademický článek
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Autor:
E. Demet Akten, Nuray Sogunmez
Publikováno v:
The Journal of Physical Chemistry B. 123:3630-3642
The alternative inactive state of the human β2-adrenergic receptor originally exposed in molecular dynamics simulations was investigated using various analysis tools to evaluate causality between correlated residue-pair fluctuations and suggest allo
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
Three allosteric glycolytic enzymes, phosphofructokinase, glyceraldehyde-3 phosphate dehydrogenase and pyruvate kinase, associated with bacterial, parasitic and human species, were explored to identify potential allosteric sites that would be used as
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Nuray, Sogunmez, E Demet, Akten
Publikováno v:
The journal of physical chemistry. B. 123(17)
The alternative inactive state of the human β
Autor:
Sogunmez, Nuray, Akten, E. Demet
The alternative inactive state of the human beta(2)-adrenergic receptor originally exposed in molecular dynamics simulations was investigated using various analysis tools to evaluate causality between correlated residue-pair fluctuations and suggest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=r39c86a4b39b::e5abcfc8059922b449b3132001204ccc
https://aperta.ulakbim.gov.tr/record/73075
https://aperta.ulakbim.gov.tr/record/73075
In a first step in the discovery of novel potent inhibitor structures for the PDE4B family with limited side effects, we present a protocol to rank newly designed molecules through the estimation of their IC[Formula: see text] values. Our protocol is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e04e237b1af64ee8a52ed39ee44b7fbe
https://hdl.handle.net/20.500.12469/341
https://hdl.handle.net/20.500.12469/341