Addition of subunit γ, K+ ions, and lipid restores the thermal stability of solubilized Na,K-ATPase-Reference-Cited by-同舟云学术

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Addition of subunit γ, K+ ions, and lipid restores the thermal stability of solubilized Na,K-ATPase

Published:2013-02 Issue:2 Volume:530 Page:93-100
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

Yoneda Juliana Sakamoto,Rigos Carolina Fortes,Ciancaglini Pietro

Funder

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Fundação de Amparo à Pesquisa do Estado de São Paulo

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference51 articles.

1. The influence of some cations on an adenosine triphosphatase from peripheral nerves

2. Endogenous Cardiotonic Steroids: Physiology, Pharmacology, and Novel Therapeutic Targets

3. The Physiological Significance of the Cardiotonic Steroid/Ouabain-Binding Site of the Na,K-ATPase

4. A structural overview of the plasma membrane Na+,K+-ATPase and H+-ATPase ion pumps

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1. Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome;Photochemistry and Photobiology;2024-06-24

2. Overview on solubilization and lipid reconstitution of Na,K-ATPase: enzyme kinetic and biophysical characterization;Biophysical Reviews;2020-01-18

3. Topographical and mechanical properties of liposome surfaces harboring Na,K-ATPase by means of atomic force microscopy;Soft Matter;2019

4. Kinetic stability of membrane proteins;Biophysical Reviews;2017-09-18

5. Interactions and cooperativity between P-glycoprotein structural domains determined by thermal unfolding provides insights into its solution structure and function;Biochimica et Biophysica Acta (BBA) - Biomembranes;2017-01

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