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pro vyhledávání: '"Xing-Han Sun"'
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0157923 (2016)
Membrane proteins play key roles in many fundamental functions in cells including ATP synthesis, ion and molecule transporter, cell signalling and enzymatic reactions, accounting for ~30% genes of whole genomes. However, the hydrophobic nature of mem
Externí odkaz:
https://doaj.org/article/7ed9adaea2e84af98d63a232f6fa6607
Autor:
Xing-Han Sun, 孫倖涵
103
Cyclic-di-AMP, a new type of second messenger, has been found abundant in bacteria and archaea in recent years. Microbes utilize the signaling molecule to mediate physiological function in response to external stimuli. A previous study shows
Cyclic-di-AMP, a new type of second messenger, has been found abundant in bacteria and archaea in recent years. Microbes utilize the signaling molecule to mediate physiological function in response to external stimuli. A previous study shows
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/66524980757185239104
Autor:
Juin-Ming Liang, Shan-Ho Chou, Zhi-Le Tu, Nien-Jen Hu, J. Maxwell Dow, Yu-Chuang Wang, Robert P. Ryan, Xing-Han Sun, Jauo-Guey Yang, Ko-Hsin Chin, Zhao-Xun Liang, Min-Shao Shih
Publikováno v:
Biochemistry. 54:4936-4951
Cyclic di-AMP (c-di-AMP) is a relatively new member of the family of bacterial cyclic dinucleotide second messengers. It has attracted significant attention in recent years because of the abundant roles it plays in a variety of Gram-positive bacteria
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0157923 (2016)
PLoS ONE
PLoS ONE
Membrane proteins play key roles in many fundamental functions in cells including ATP synthesis, ion and molecule transporter, cell signalling and enzymatic reactions, accounting for ~30% genes of whole genomes. However, the hydrophobic nature of mem
Autor:
Ko-Hsin Chin, Juin-Ming Liang, Jauo-Guey Yang, Min-Shao Shill, Zhi-Le Tu, Yu-Chuang Wang, Xing-Han Sun, Nien-Jen Hu, Zhao-Xun Liang, Dow, J. Maxwell, Ryan, Robert P., Shan-Ho Chou
Publikováno v:
Biochemistry; 8/11/2015, Vol. 54 Issue 31, p4936-4951, 8p