Results 61 to 70 of about 363,756 (199)

Effect of Electroacupuncture of "Neiguan"(PC 6) on Na~+-K~+-ATPase Activity and Its Gene Expression in Cardiocyte Membrane in Rats with Myocardial Ischemia-reperfusion Injury

open access: yes针刺研究, 2007
Objective: To compare the effects of electroacupuncture(EA) of "Neiguan" and other acupoints on Na+-K+-ATPase activity and its gene expression in ischemic myocrardial cell membrane in rats.Methods: A total of 50 Wistar rats were randomly divided into ...
YAN Jie   +6 more
doaj   +2 more sources

Chemical genetic identification of GAK substrates reveals its role in regulating Na+/K+-ATPase

open access: yes, 2020
Cyclin G-associated kinase (GAK) is a ubiquitous serine/threonine kinase that facilitates clathrin uncoating during vesicle trafficking. GAK phosphorylates a coat adaptor component, AP2M1, to help achieve this function.
Irene Matucci (9291047)   +9 more
core  

Na+/K+-ATPase: ion pump, signal transducer, or cytoprotective protein, and novel biological functions

open access: yesNeural Regeneration Research
Na+/K+-ATPase is a transmembrane protein that has important roles in the maintenance of electrochemical gradients across cell membranes by transporting three Na+ out of and two K+ into cells.
Songqiang Huang   +3 more
doaj   +1 more source

Na/K Pump and Beyond: Na/K-ATPase as a Modulator of Apoptosis and Autophagy

open access: yesMolecules, 2017
Lung cancer is a leading cause of global cancer deaths. Na/K-ATPase has been studied as a target for cancer treatment. Cardiotonic steroids (CS) trigger intracellular signalling upon binding to Na/K-ATPase. Normal lung and tumour cells frequently express
Cassiano Felippe Gonçalves-de-Albuquerque   +4 more
doaj   +1 more source

Involvement of the alpha-subunit N-terminus in the mechanism of the Na+,K+-ATPase

open access: yes, 2023
Previous studies have shown that cytoplasmic K+ release and the associated E2 → E1 conformational change of the Na+,K+-ATPase is a major rate-determining step of the enzyme's ion pumping cycle and hence a prime site of acute regulatory intervention. From
C. Cranfield (20092251)   +5 more
core  

Vacuolar ATPase as a potential therapeutic target and mediator of treatment resistance in cancer

open access: yesCancer Medicine, 2018
Vacuolar ATPase (V‐ATPase) is an ATP‐dependent H+‐transporter that pumps protons across intracellular and plasma membranes. It consists of a large multi‐subunit protein complex and influences a wide range of cellular processes.
Bradleigh Whitton   +3 more
doaj   +1 more source

The curious case of vacuolar ATPase: regulation of signaling pathways

open access: yesMolecular Cancer, 2018
The Vacuolar ATPase (V-ATPase) is a proton pump responsible for controlling the intracellular and extracellular pH of cells. The structure of V-ATPase has been highly conserved among all eukaryotic cells and is involved in diverse functions across ...
Sahithi Pamarthy   +3 more
doaj   +1 more source

Impact of Activities of Na+,K+-Atpase and Ca2+-Atpase in the Cochlear Lateral Wall on Recovery from Noise-Induced Temporary Threshold Shift

open access: yes, 2009
The present study was designed to investigate the relationship between the noise-induced temporary threshold shift (TTS) and the specific activities of sodium potassium adenosine triphosphatase (Na+,K+-ATPase) and calcium adenosine triphosphatase (Ca(2 ...
HSU, CHUAN-JEN;CHEN, YUH-SHYANG;SHAU, WEN-YI;YEH, TE-HUEI;LEE, SHIANN-YANN;LIN-SHIAU, SHOEI-YN   +1 more
core  

Conformational studies of peptides representing a segment of TM7 from Vo-H+-V-ATPase in SDS micelles [PDF]

open access: yes, 2009
The conformation of a transmembrane peptide, sMTM7, encompassing the cytoplasmic hemi-channel domain of the seventh transmembrane section of subunit a from V-ATPase from Saccharomyces cerevisiae solubilized in SDS solutions was studied by circular ...
Jong, E.R., de   +7 more
core   +1 more source

The slow sarco/endoplasmic reticulum Ca2+-ATPase declines independently of slow myosin in soleus muscle of diabetic rats [PDF]

open access: yes, 2009
The sarcoplasmic reticulum Ca2+-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions.
Rácz, Gábor   +3 more
core   +2 more sources

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