Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Tung O. Chan"'
Autor:
Xavier Palomer, Eva Capdevila-Busquets, Gaia Botteri, Mercy M. Davidson, Cristina Rodríguez, José Martínez-González, Francisco Vidal, Emma Barroso, Tung O. Chan, Arthur M. Feldman, Manuel Vázquez-Carrera
Publikováno v:
Disease Models & Mechanisms, Vol 8, Iss 9, Pp 1081-1091 (2015)
miR-146a is a microRNA whose transcript levels are induced in the heart upon activation of NF-κB, a transcription factor induced by pro-inflammatory molecules (such as TNF-α) that is strongly related to the pathogenesis of cardiac disorders. The ma
Externí odkaz:
https://doaj.org/article/8b25dc11b1554cb3896abdbe27fadd61
Autor:
Deepak A. Deshpande, Ulrich Rodeck, Santosh K Yadav, Sushrut D. Shah, Jin Zhang, Brian Blumhof, Roger S. Armen, Brian C. Tiegs, Raymond B. Penn, Tung O. Chan, Nikhil Keny
Publikováno v:
J Biol Chem
Phosphorylation of specific residues in the activation loops of AGC kinase group (protein kinase A, G, and C families) is required for activity of most of these kinases, including the catalytic subunit of PKA (PKAc). Although many phosphorylated AGC
Autor:
Eman A Hamad, Weizhong Zhu, Tung O Chan, Valerie Myers, Erhe Gao, Xue Li, Jin Zhang, Jianliang Song, Xue-Qian Zhang, Joseph Y Cheung, Walter Koch, Arthur M Feldman
Publikováno v:
PLoS ONE, Vol 7, Iss 7, p e39919 (2012)
Adenosine binds to three G protein-coupled receptors (R) located on the cardiomyocyte (A(1)-R, A(2A)-R and A(3)-R) and provides cardiac protection during both ischemic and load-induced stress. While the role of adenosine receptor-subtypes has been we
Externí odkaz:
https://doaj.org/article/7d45b07a782940a28b938ae5ecdfddf9
Autor:
Xavier Palomer, David Álvarez-Guardia, Mercy M Davidson, Tung O Chan, Arthur M Feldman, Manuel Vázquez-Carrera
Publikováno v:
PLoS ONE, Vol 6, Iss 5, p e19724 (2011)
Pyruvate dehydrogenase kinase 4 (PDK4) inhibition by nuclear factor-κB (NF-κB) is related to a shift towards increased glycolysis during cardiac pathological processes such as cardiac hypertrophy and heart failure. The transcription factors estroge
Externí odkaz:
https://doaj.org/article/304fbede2b5345609576dd025b629f32
Autor:
Donald J. Fujita, Heung-Chin Cheng, Gregory J. Dusting, Andrew F. Hill, Carli L Roulston, Nicholas A. Williamson, Jeffrey D. Bjorge, Steve N. Cheung, M. Aizuddin Kamaruddin, Tung O. Chan, M. Iqbal Hossain, Dominic C.H. Ng, Percy W.Y. Chu
Publikováno v:
Journal of Biological Chemistry. 288:9696-9709
Excitotoxicity resulting from overstimulation of glutamate receptors is a major cause of neuronal death in cerebral ischemic stroke. The overstimulated ionotropic glutamate receptors exert their neurotoxic effects in part by overactivation of calpain
Autor:
JuFang Wang, Erhe Gao, Xiying Shang, Walter J. Koch, Xue-Qian Zhang, Jianliang Song, Jeffrey I. Joseph, Tung O. Chan, Arthur M. Feldman, Joseph Y. Cheung, Blaise Z. Peterson
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 302:H770-H781
Expression and activity of cardiac Na+/Ca2+ exchanger (NCX1) are altered in many disease states. We engineered mice in which the phosphomimetic phospholemman S68E mutant (inhibits NCX1 but not Na+-K+-ATPase) was constitutively overexpressed in a card
Publikováno v:
Cell Cycle. 11:475-478
AGC kinases, including the three Akt (protein kinase B) isoforms, protein kinase A (PKA) and all protein kinase C (PKC) isoforms, require activation loop phosphorylation (threonine 308 in Akt1) as well as phosphorylation of a C-terminal residue (seri
Autor:
Carmela Zincarelli, Erhe Gao, Tung O. Chan, Deana Mikhalkova, Jianliang Song, Yonghong Lei, Jin Zhang, Karsten Peppel, Arthur M. Feldman, Xue Li, Walter J. Koch, Valerie D. Myers, Joseph Y. Cheung
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 301:H1932-H1940
Akt2 protein kinase has been shown to promote cell migration and actin polymerization in several cell types, including macrophages. Because migrating macrophages constitute an important inflammatory response after myocardial ischemia, we determined c
Publikováno v:
American Journal of Physiology-Cell Physiology. 301:C833-C840
Using split cardiac Na+/Ca2+exchangers (NCX1), we previously demonstrated that phospholemman (PLM) regulates NCX1 by interacting with the proximal linker domain (residues 218–358) of the intracellular loop of NCX1. With the use of overlapping loop
Autor:
Joseph E. Rabinowitz, Jianliang Song, Erhe Gao, Joseph Y. Cheung, Xue-Qian Zhang, JuFang Wang, Tung O. Chan
Publikováno v:
Clinical and Translational Science. 3:189-196
Phospholemman (PLM), a member of the FXYD family of regulators of ion transport, is a major sarcolemmal substrate for protein kinases A and C in cardiac and skeletal muscle. In the heart, PLM co-localizes and co-immunoprecipitates with Na(+)-K(+)-ATP