Zobrazeno 1 - 10
of 70
pro vyhledávání: '"Chen-Pei D. TU"'
Autor:
Bünyamin Akgül, Kai-Wei Lin, Hui-Mei Ou Yang, Yen-Hui Chen, Tzu-Huan Lu, Chien-Hsiun Chen, Tateki Kikuchi, Yuan-Tsong Chen, Chen-Pei D Tu
Publikováno v:
PLoS ONE, Vol 5, Iss 12, p e15358 (2010)
Garlic (Allium sativum) has been valued in many cultures both for its health effects and as a culinary flavor enhancer. Garlic's chemical complexity is widely thought to be the source of its many health benefits, which include, but are not limited to
Externí odkaz:
https://doaj.org/article/f1a43b1e54ab4bc9825d48c734617cb4
Autor:
Amir N Saleem, Yen-Hui Chen, Hwa Jin Baek, Ya-Wen Hsiao, Hong-Wen Huang, Hsiao-Jung Kao, Kai-Ming Liu, Li-Fen Shen, I-Wen Song, Chen-Pei D Tu, Jer-Yuarn Wu, Tateki Kikuchi, Monica J Justice, Jeffrey J Y Yen, Yuan-Tsong Chen
Publikováno v:
PLoS Genetics, Vol 6, Iss 6, p e1000985 (2010)
Protein palmitoylation has emerged as an important mechanism for regulating protein trafficking, stability, and protein-protein interactions; however, its relevance to disease processes is not clear. Using a genome-wide, phenotype driven N-ethyl-N-ni
Externí odkaz:
https://doaj.org/article/4c64134e49014abaaa498ae40f536a15
Autor:
Chen-Pei D. Tu, Bünyamin Akgül
Publikováno v:
Archives of Biochemistry and Biophysics. 459:143-150
Pentobarbital, a general anesthetic and non-genotoxic carcinogen, can induce gene expression by activating transcription. In the Drosophila glutathione S-transferase D21 (gstD21) gene, pentobarbital's regulatory influence extends to the level of mRNA
Autor:
Chen-Pei D. Tu, Bünyamin Akgül
Publikováno v:
Journal of Biological Chemistry. 277:34700-34707
The neighboring genes gstD1 and gstD21 share 70% sequence identity. gstD1 encodes a 1,1,1-trichloro-2,2-bis-(P-chlorophenyl)ethane dehydrochlorinase; gstD21, a ligandin. Both of their mRNAs are inducible by pentobarbital but otherwise behave very dif
Autor:
Hailing CHENG, Tatyana TCHAIKOVSKAYA, Yen-Sheng L. TU, Jason CHAPMAN, Biao QIAN, Wei-Mei CHING, Ming TIEN, Jonathan D. ROWE, Yury V. PATSKOVSKY, Irving LISTOWSKY, Chen-Pei D. TU
Publikováno v:
Biochemical Journal. 356:403-414
Although the existence of the rat glutathione S-transferase (GST) M4 (rGSTM4) gene has been known for some time, the corresponding protein has not as yet been purified from tissue. A recombinant rGSTM4-4 was thus expressed in Escherichia coli from a
Autor:
J DeJong, Jan-Olov Höög, Chen-Pei D. Tu, Tomas Bergman, J Dypbukt, Ralf Morgenstern, Erifili Mosialou, H J Barnes, Rolf Weinander
Publikováno v:
Biochemical Journal. 311:861-866
The cDNA coding for rat liver microsomal glutathione transferase was subcloned into the mammalian expression vector pCMV-5 and the construct was transfected into, and transiently expressed in, simian COS cells. This resulted in high expression (0.7%
Publikováno v:
Journal of Biological Chemistry. 270:99-109
The common substrate for glutathione S-transferases (GSTs), 1-chloro-2,4-dinitrobenzene (CDNB), is an inhibitor of Escherichia coli growth. This growth inhibition by CDNB is enhanced when E. coli expresses a functional GST. Cells under growth inhibit
Publikováno v:
Proteins: Structure, Function, and Genetics. 20:259-263
A chimeric enzyme (GST121) of the human alpha-glutathione S-transferases GST1-1 and GST2-2, which has improved catalytic efficiency and thermostability from its wild-type parent proteins, has been crystallized in a space group that is isomorphous wit
Publikováno v:
Journal of Biological Chemistry. 268:9737-9746
We have characterized a cluster of glutathione S-transferase genes located at 87B on the Drosophila polytene chromosome near the heat shock genes, hsp70. These genes, designated gst Ds in the glutathione S-transferase gene superfamily, are closely li
Autor:
Jeffrey J.Y. Yen, Yuan-Tsong Chen, Li-Fen Shen, Jer-Yuarn Wu, Hong-Wen Huang, I-Wen Song, Ya-Wen Hsiao, Chen-Pei D. Tu, Kai-Ming Liu, Amir N. Saleem, Yen-Hui Chen, Hwa Jin Baek, Hsiao-Jung Kao, Monica J. Justice, Tateki Kikuchi
Publikováno v:
PLoS Genetics, Vol 6, Iss 6, p e1000985 (2010)
PLoS Genetics
PLoS Genetics
Protein palmitoylation has emerged as an important mechanism for regulating protein trafficking, stability, and protein–protein interactions; however, its relevance to disease processes is not clear. Using a genome-wide, phenotype driven N-ethyl-N-