✦ LIBER ✦

Modulation of Na,K-ATPase by Associated Small Transmembrane Regulatory Proteins and by Lipids

✍ Scribed by Flemming Cornelius; Yasser A. Mahmmoud; Hanne R. Z. Christensen

Book ID: 110294203
Publisher: Springer US
Year: 2001
Tongue: English
Weight: 206 KB
Volume: 33
Category: Article
ISSN: 0145-479X
DOI: 10.1023/a:1010671607911

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Modulation of cardiac glycoside inhibiti

Modulation of cardiac glycoside inhibition of (Na+ + K+)-ATPase by membrane lipids. Difference between species

✍ Mahinda Y. Abeywardena; John S. Charnock 📂 Article 📅 1983 🏛 Elsevier Science 🌐 English ⚖ 737 KB

Modulation of Na,K-ATPase and Na-ATPase

Modulation of Na,K-ATPase and Na-ATPase Activity by Phospholipids and Cholesterol. I. Steady-State Kinetics †

✍ Cornelius, Flemming 📂 Article 📅 2001 🏛 American Chemical Society 🌐 English ⚖ 133 KB

Modulation of FXYD Interaction with Na,K

Modulation of FXYD Interaction with Na,K-ATPase by Anionic Phospholipids and Protein Kinase Phosphorylation †

✍ Cornelius, Flemming; Mahmmoud, Yasser A. 📂 Article 📅 2007 🏛 American Chemical Society 🌐 English ⚖ 210 KB

Selectivity of lipid–protein interaction

Selectivity of lipid–protein interactions with trypsinized Na,K-ATPase studied by spin-label EPR

✍ Ashish Arora; Mikael Esmann; Derek Marsh 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 195 KB

The γ subunit of Na+, K+-ATPase: Role on

The γ subunit of Na+, K+-ATPase: Role on ATPase activity and regulatory phosphorylation by PKA

✍ Vanessa Faria Cortes; Fabio Eduardo Veiga-Lopes; Hector Barrabin; Marcelo Alves- 📂 Article 📅 2006 🏛 Elsevier Science 🌐 English ⚖ 360 KB

Membrane orientation of the Na,K-ATPase

Membrane orientation of the Na,K-ATPase regulatory membrane protein CHIF determined by solid-state NMR

✍ Carla M. Franzin; Peter Teriete; Francesca M. Marassi 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 460 KB

Corticosteroid hormone-induced factor (CHIF) is a major regulatory subunit of the Na,K-ATPase, and a member of an evolutionarily conserved family of membrane proteins that regulate the function of the enzyme complex in a tissue-specific and physiological-state-specific manner. Here we present the st