Výsledky vyhledávání - "Mikael Esmann"

Geometry and water accessibility of the inhibitor binding site of Na+-pump:Pulse- and CW-EPR study

Autor: Ren-Wang Jiang, Natalya U. Fedosova, Derek Marsh, Rosa Bartucci, Jin-Hua Guo, Erika Aloi, Lucy Kate Ladefoged, Mikael Esmann, Rita Guzzi

Publikováno v: Aloi, E, Guo, J H, Guzzi, R, Jiang, R W, Ladefoged, L K, Marsh, D, Esmann, M, Bartucci, R & Fedosova, N U 2021, ' Geometry and water accessibility of the inhibitor binding site of Na +-pump : Pulse-and CW-EPR study ', Biophysical Journal, vol. 120, no. 13, pp. 2679-2690 . https://doi.org/10.1016/j.bpj.2021.05.018

Spin labels based on cinobufagin, a specific inhibitor of the Na,K-ATPase, have proved valuable tools to characterize the binding site of cardiotonic steroids (CTSs), which also constitutes the extracellular cation pathway. Because existing literatur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::771be57af7ec0adefc2aecf64a629bb1
https://pure.au.dk/portal/da/publications/geometry-and-water-accessibility-of-the-inhibitor-binding-site-of-napump(62a38489-ca08-4e8b-a50b-3569b2d1d1a6).html

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Geometry and water accessibility of the inhibitor binding site of Na

Autor: Erika, Aloi, Jin-Hua, Guo, Rita, Guzzi, Ren-Wang, Jiang, Lucy Kate, Ladefoged, Derek, Marsh, Mikael, Esmann, Rosa, Bartucci, Natalya U, Fedosova

Publikováno v: Biophysical journal. 120(13)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::20df3bc45ef932e0d15cae17de3bf817
https://pubmed.ncbi.nlm.nih.gov/34087213

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Spin-labeled derivatives of cardiotonic steroids as tools for characterization of the extracellular entrance to the binding site on Na+,K+-ATPase

Autor: Natalya U. Fedosova, Jin-Hua Guo, Jacob Andersen, Mikael Esmann, Ren-Wang Jiang

Publikováno v: Guo, J-H, Jiang, R-W, Andersen, J L, Esmann, M & Fedosova, N 2018, ' Spin-labeled derivatives of cardiotonic steroids as tools for characterization of the extracellular entrance to the binding site on Na+,K+-ATPase ', F E B S Journal, vol. 285, no. 12, pp. 2292-2305 . https://doi.org/10.1111/febs.14480

The information obtained from crystallized complexes of the Na + ,K + -ATPase with cardiotonic steroids (CTS) is not sufficient to explain differences in the inhibitory properties of CTS such as stereoselectivity of CTS binding or effect of glycosyla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb096953d6a80c780074a3b97608eb06
https://pure.au.dk/portal/da/publications/spinlabeled-derivatives-of-cardiotonic-steroids-as-tools-for-characterization-of-the-extracellular-entrance-to-the-binding-site-on-nakatpase(193b3393-85f2-48f6-a624-f5d29bc06572).html

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Na,K-ATPase structure/function relationships probed by the denaturant urea

Autor: Natalya U. Fedosova, Claus Olesen, Mikael Esmann

Publikováno v: Esmann, M, Fedosova, N U & Olesen, C 2015, ' Na,K-ATPase structure/function relationships probed by the denaturant urea ', B B A-Biomembranes, vol. 1848, no. 5, pp. 1212-1223 . https://doi.org/10.1016/j.bbamem.2015.02.006

Urea interacts with the Na,K-ATPase, leading to reversible as well as irreversible inhibition of the hydrolytic activity. The enzyme purified from shark rectal glands is more sensitive to urea than Na,K-ATPase purified from pig kidney. An immediate a

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Water Penetration Profile at the Protein-Lipid Interface in Na,K-ATPase Membranes

Autor: Mikael Esmann, Rosa Bartucci, Rita Guzzi, Derek Marsh

Publikováno v: Bartucci, R, Guzzi, R, Esmann, M & Marsh, D 2014, ' Water penetration profile at the protein-lipid interface in Na,K-ATPase membranes ', Biophysical Journal, vol. 107, no. 6, pp. 1375-82 . https://doi.org/10.1016/j.bpj.2014.07.057
Biophysical Journal

The affinity of ionized fatty acids for the Na,K-ATPase is used to determine the transmembrane profile of water penetration at the protein-lipid interface. The standardized intensity of the electron spin echo envelope modulation (ESEEM) from (2)H-hyp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::061cece5a27d475c5b21b5bcd0367fd6
https://doi.org/10.1016/j.bpj.2014.07.057

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Structures, chemotaxonomic significance, cytotoxic and Na+,K+-ATPase inhibitory activities of new cardenolides from Asclepias curassavica

Autor: David A. Middleton, Mikael Esmann, Natalya U. Fedosova, Jason T.C. Tzen, Tse-Yu Chung, Hai-Yan Tian, Xiao-Hui Sun, Rong-Rong Zhang, Xue Xia, Ya-Fang Tan, Wen-Cai Ye, Ren-Wang Jiang

Publikováno v: Zhang, R-R, Tian, H-Y, Tan, Y-F, Chung, T-Y, Sun, X-H, Xia, X, Ye, W-C, Middleton, D A, Fedosova, N, Esmann, M, Tzen, J T C & Jiang, R-W 2014, ' Structures, chemotaxonomic significance, cytotoxic and Na(+),K(+)-ATPase inhibitory activities of new cardenolides from Asclepias curassavica ', Organic & Biomolecular Chemistry, vol. 12, no. 44, pp. 8919-29 . https://doi.org/10.1039/c4ob01545b

Five new cardenolide lactates (1–5) and one new dioxane double linked cardenolide glycoside (17) along with 15 known compounds (6–16 and 18–21) were isolated from the ornamental milkweed Asclepias curassavica. Their structures were elucidated b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8eaccf62e7febb5378d724064fc2ed9c
https://doi.org/10.1039/c4ob01545b

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Novel stereoselective bufadienolides reveal new insights into the requirements for Na(+), K(+)-ATPase inhibition by cardiotonic steroids

Autor: David A. Middleton, Li-Jun Ruan, Mikael Esmann, Hai-Yan Tian, Ren-Wang Jiang, Guang-Ping Liang, Jason T.C. Tzen, Tse-Yu Chung, Eleri Hughes, Wen-Cai Ye, Hong-Jin Tang, Natalya U. Fedosova

Publikováno v: Scientific Reports
Tang, H-J, Ruan, L-J, Tian, H-Y, Liang, G-P, Ye, W-C, Hughes, E, Esmann, M, Fedosova, N, Chung, T-Y, Tzen, J T C, Jiang, R-W & Middleton, D 2016, ' Novel stereoselective bufadienolides reveal new insights into the requirements for Na,K-ATPase inhibition by cardiotonic steroids ', Scientific Reports . https://doi.org/10.1038/srep29155

Cardiotonic steroids (CTS) are clinically important drugs for the treatment of heart failure owing to their potent inhibition of cardiac Na+, K+-ATPase (NKA). Bufadienolides constitute one of the two major classes of CTS, but little is known about ho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9399846798a9838a4bab2efcc09be12
https://pubmed.ncbi.nlm.nih.gov/27377465

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Long-range effects of Na+ binding in Na,K-ATPase reported by ATP

Autor: Natalya U. Fedosova, Mikael Esmann, David A. Middleton

This paper addresses the question of long-range interactions between the intramembranous cation binding sites and the cytoplasmic nucleotide binding site of the ubiquitous ion-transporting Na,K-ATPase using (13)C cross-polarization magic-angle spinni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feb1c99b7a03aa44f5185e19aeffffff
https://doi.org/10.1021/acs.biochem.5b00893

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A study of the membrane association and regulatory effect of the phospholemman cytoplasmic domain

Autor: Igor L. Barsukov, David A. Middleton, Christopher A. P. Whittaker, Eleri Hughes, Mikael Esmann

Publikováno v: Hughes, E, Whittaker, C A P, Barsukov, I L, Esmann, M & Middleton, D A 2011, ' A study of the membrane association and regulatory effect of the phospholemman cytoplasmic domain ', B B A-Biomembranes, vol. 1808, no. 4, pp. 1021-31 . https://doi.org/10.1016/j.bbamem.2010.11.024

Phospholemman (PLM) is a single-span transmembrane protein belonging to the FXYD family of proteins. PLM (or FXYD1) regulates the Na,K-ATPase (NKA) ion pump by altering its affinity for K(+) and Na(+) and by reducing its hydrolytic activity. Structur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2df2ca12c21d3bbcd20b89bc04e1934
https://doi.org/10.1016/j.bbamem.2010.11.024

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Conformational Heterogeneity and Spin-Labeled −SH Groups: Pulsed EPR of Na,K-ATPase

Autor: Rosa Bartucci, Derek Marsh, Mikael Esmann, Luigi Sportelli, Rita Guzzi

Publikováno v: Guzzi, R, Bartucci, R, Sportelli, L, Esmann, M & Marsh, D 2009, ' Conformational Heterogeneity and Spin-Labeled-SH Groups: Pulsed EPR of Na,K-ATPase ', Biochemistry, vol. 48, pp. 8343-8354 .

Membranous Na,K-ATPase from shark salt gland and from pig kidney was spin-labeled on class I -SH groups in the presence of glycerol, or on class II -SH groups in the absence of glycerol. The class I-labeled preparations retain full enzymatic activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73f3ab9a7e4ea52fc9ede10a582a69a2
https://doi.org/10.1021/bi900849z

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