Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Kai Y Xu"'
Autor:
Takeshi Arai, Shinji Muroya, Yifei Yang, Eiju Watanabe, Putra Santoso, Darambazar Gantulga, Yuko Maejima, Alan Kawarai Lefor, Katsuya Dezaki, Masafumi Kakei, Toshihiko Yada, Hideharu Kurita, Masanori Nakata, Kai Y. Xu
Publikováno v:
American Journal of Physiology-Endocrinology and Metabolism. 309:E320-E333
Feeding is regulated by perception in the hypothalamus, particularly the first-order arcuate nucleus (ARC) neurons, of the body's energy state. However, the cellular device for converting energy states to the activity of critical neurons in ARC is le
Autor:
Devin Sok, Paul W. H. I. Parren, Gary L. Gilliland, Lubna Abuqayyas, Wayne A. Marasco, Fridtjof Lund-Johansen, Robert Mabry, Kai Y Xu, Jamie K. Scott, Janice M. Reichert, James S. Huston, James E. Voss, Stefan Barghorn, Gustavo Helguera, Raiees Andrabi, Eshel Ben-Jacob, Juan Carlos Almagro, Stephen Albert Johnston, Juha Laurén, James E. Crowe, Eric Krauland, Matthias Pauthner, Felix Breden, Mathieu Bléry
Publikováno v:
mAbs. 6:577-618
The 24th Antibody Engineering & Therapeutics meeting brought together a broad range of participants who were updated on the latest advances in antibody research and development. Organized by IBC Life Sciences, the gathering is the annual meeting of T
Autor:
Kai Y. Xu
Publikováno v:
Biochemical and Biophysical Research Communications. 415:479-484
(Na++K+)-ATPase (NKA) comprises two basic α and β subunits: The larger α subunit catalyzes the hydrolysis of ATP for active transport of Na+ and K+ ions across the plasma membrane; the smaller β subunit does not take part in the catalytic process
Publikováno v:
Biochemical and Biophysical Research Communications. 406:200-203
(Na(+)+K(+))-ATPase (NKA) mediates positive inotropy in the heart. Extensive studies have demonstrated that the reverse-mode Na(+)/Ca(2+)-exchanger (NCX) plays a critical role in increasing intracellular Ca(2+) concentration through the inhibition of
Publikováno v:
Biochemical and Biophysical Research Communications. 402:319-323
Activation of (Na++K+)-ATPase (NKA) regulates cardiac L-type Ca2+ channel (LTCC) function through molecular crosstalk. The mechanism underlying NKA–LTCC crosstalk remains poorly understood. We have previously shown that activation of NKA leads to p
Publikováno v:
Molecular Pharmacology. 75:774-781
Cellular Ca(2+) signaling underlies diverse vital biological processes, including muscle contractility, memory encoding, fertilization, cell survival, and cell death. Despite extensive studies, the fundamental control mechanisms that regulate intrace
Autor:
Kai Y. Xu
Publikováno v:
Biochemical and Biophysical Research Communications. 377:469-473
(Na(+)+K(+))-ATPase is a target receptor of digitalis (cardiac glycoside) drugs. It has been demonstrated that the H1-H2 domain of the alpha-subunit of the (Na(+)+K(+))-ATPase is one of the digitalis drug interaction sites of the enzyme. Despite the
Autor:
Kai Y. Xu
Publikováno v:
Biochemical and Biophysical Research Communications. 338:1669-1677
Enzymes catalyze essential chemical reactions needed for living processes. (Na+ +K+)-ATPase (NKA) is one of the key enzymes that control intracellular ion homeostasis and regulate cardiac function. Little is known about activation of NKA and its biol
Autor:
Periannan Kuppusamy, Kai Y. Xu
Publikováno v:
Biochemical and Biophysical Research Communications. 336:1190-1193
Copper–zinc superoxide dismutase (CuZnSOD) specifically catalyzes the removal of superoxide radicals to protect cellular function against the generation of superoxide-dependent hydroxyl radicals ( OH). However, an unexpected observation reveals tha
Autor:
Shanmuga P. Kuppusamy, Hongmei Cui, Haiquan Li, Arthur L. Burnett, Paul L. Huang, Jing Q. Wang, Kai Y. Xu, Ted M. Dawson, Periannan Kuppusamy, Lewis C. Becker
Publikováno v:
Journal of Biological Chemistry. 278:41798-41803
Nitric oxide (NO.) generated from nitric oxide synthase (NOS) isoforms bound to cellular membranes may serve to modulate oxidative stresses in cardiac muscle and thereby regulate the function of key membrane-associated enzymes. Ischemia is known to i