Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Chan Fong Chang"'
Autor:
Muhammad Sufyan Bin Masroni, Kee Wah Lee, Victor Kwan Min Lee, Siok Bian Ng, Chao Teng Law, Kok Siong Poon, Bernett Teck-Kwong Lee, Zhehao Liu, Yuen Peng Tan, Wee Ling Chng, Steven Tucker, Lynette Su-Mien Ngo, George Wai Cheong Yip, Min En Nga, Susan Swee Shan Hue, Thomas Choudary Putti, Boon Huat Bay, Qingsong Lin, Lihan Zhou, Mikael Hartman, Tze Ping Loh, Manikandan Lakshmanan, Sook Yee Lee, Vinay Tergaonkar, Huiwen Chua, Adeline Voon Hui Lee, Eric Yew Meng Yeo, Mo-Huang Li, Chan Fong Chang, Zizheng Kee, Karen Mei-Ling Tan, Soo Yong Tan, Evelyn Siew-Chuan Koay, Marco Archetti, Sai Mun Leong
Publikováno v:
Molecular Cancer, Vol 22, Iss 1, Pp 1-30 (2023)
Abstract Background Social behaviors such as altruism, where one self-sacrifices for collective benefits, critically influence an organism’s survival and responses to the environment. Such behaviors are widely exemplified in nature but have been un
Externí odkaz:
https://doaj.org/article/eb9275cb0ff74a91bcbbbfb6118beefa
Autor:
Karen Mei-Ling Tan, Boon-Huat Bay, Lynette Su Mien Ngo, Mikael Hartman, Soo Yong Tan, Sai Mun Leong, Steven Tucker, Evelyn Siew-Chuan Koay, Chan Fong Chang, Lihan Zhou, Kee Wah Lee, Muhammad Sufyan bin Masroni, Tze Ping Loh, Thomas C. Putti, Mo-Huang Li, Huiwen Chua
Publikováno v:
Cancer Research. 78:203-203
Introduction: Cancer is thought to represent a breakdown of multicellular cooperation and reversion to Darwinian dynamics characterized principally by self-interested competition. However, there is increasing evidence that cancer cells can behave as
Publikováno v:
Protein Expression and Purification. 40:396-403
CD38 is a type II transmembrane glycoprotein found in myriad mammalian tissues and cell types. It is known for its involvement in the metabolism of cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate, two nucleotides with calcium mobi
Publikováno v:
European Journal of Cell Biology. 79:697-706
CD157/BST-1 is expressed on mature myeloid cells but not on their precursors in vivo. Also CD38, a homologous gene to CD157, is upregulated in promyelocytic HL-60 cells by the monocyte and granulocyte differentiation-inducing 1alpha,25dihydroxyvitami
Autor:
Uh-Hyun Kim, Boon Huat Bay, Jin Bong Park, Soo Wan Chae, Chan Fong Chang, Keng Meng Khoo, Myung-Kwan Han, Hon Cheung Lee
Publikováno v:
Journal of Biological Chemistry. 275:24807-24817
CD38 is a type II transmembrane glycoprotein found on both hematopoietic and non-hematopoietic cells. It is known for its involvement in the metabolism of cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate, two nucleotides wi
Autor:
Chan Fong Chang, Keng Meng Khoo
Publikováno v:
Archives of Biochemistry and Biophysics. 373:35-43
CD38 is a 42- to 45-kDa type II transmembrane glycoprotein with the ability to synthesize cADPR, a metabolite with potent calcium mobilizing properties independent of IP(3). We report here the primary characterization and localization of CD38 in the
Autor:
Chan Fong Chang, Keng Meng Khoo
Publikováno v:
Brain Research. 821:17-25
CD38 is a 42-kDa type II transmembrane glycoprotein that has been shown to catalyze the synthesis and hydrolysis of cyclic ADP-ribose, a metabolite with well-known calcium mobilizing properties independent of IP3. In this report, characterization and
Publikováno v:
Archives of Biochemistry and Biophysics. 363:267-272
CD38 is a 46-kDa type II transmembrane glycoprotein that catalyses the synthesis of cyclic ADP-ribose (cADPR) from NAD+. cADPR is a second messenger known to regulate intracellular Ca2+-induced Ca2+-release (CICR). A recent study has revealed that CD
Autor:
Chan Fong Chang, Keng Meng Khoo
Publikováno v:
IUBMB Life. 44:841-850
Purification and characterization of CD38/ADP-ribosyl cyclase in the rat lung tissue was performed with microsomes solubilized in Triton X-100 and the ADP-ribosyl cyclase was then purified using sequential column chromatography. Partially purified ra
Publikováno v:
Experimental cell research. 316(20)
Protein phosphatase 2A (PP2A), in its activated form as a phosphatase, is a tumour suppressor. However, when PP2A is phosphorylated at the tyrosine residue (pY307), it loses its phosphatase activity and becomes inactivated. In our previous study, we