Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Hsiuchin Yang"'
Autor:
Ying-Hsin Hsieh, Ying-Ju Huang, Hao Zhang, Qian Liu, Yang Lu, Hsiuchin Yang, John Houghton, Chun Jiang, Sen-Fang Sui, Phang C Tai
Publikováno v:
PLoS ONE, Vol 12, Iss 6, p e0178307 (2017)
SecA is an essential protein in the major bacterial Sec-dependent translocation pathways. E. coli SecA has 901 aminoacyl residues which form multi-functional domains that interact with various ligands to impart function. In this study, we constructed
Externí odkaz:
https://doaj.org/article/8f8cef8d106c4adfad9f43770a592d71
Autor:
Zhipeng You, Meijiang Liao, Hao Zhang, Hsiuchin Yang, Xijian Pan, John E Houghton, Sen-Fang Sui, Phang C Tai
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e72560 (2013)
SecA, an essential component of the Sec machinery, exists in a soluble and a membrane form in Escherichia coli. Previous studies have shown that the soluble SecA transforms into pore structures when it interacts with liposomes, and integrates into me
Externí odkaz:
https://doaj.org/article/efdf510d3e204723a436ebb5cd6d1bd5
Autor:
Hao Zhang, Krishna Damera, Hsiuchin Yang, Ying-Hsin Hsieh, Arpana S. Chaudhary, Phang C. Tai, Binghe Wang, Jianmei Cui, Jinshan Jin
Publikováno v:
Bioorganic & Medicinal Chemistry. 23:7061-7068
Due to the emergence and rapid spread of drug resistance in bacteria, there is an urgent need for the development of novel antimicrobials. SecA, a key component of the general bacterial secretion system required for viability and virulence, is an att
Publikováno v:
Biochemical and Biophysical Research Communications. 456:213-218
Previous studies showed that certain regions of E. coli SecA can be deleted from its N- and/or C-termini to complement a SecA amber ts mutant. In this study, we determined and characterized the dispensability of both ends of SecA molecules. With N-te
Autor:
Phang C. Tai, Hsiuchin Yang, Jinshan Jin, Li-Yan Yu, Binghe Wang, Chun Jiang, Ying-Ju Huang, Ying-Hsin Hsieh
Publikováno v:
Biochemical and Biophysical Research Communications. 454:308-312
SecA is an essential protein possessing ATPase activity in bacterial protein translocation for which Rose Bengal (RB) is the first reported sub-micromolar inhibitor in ATPase activity and protein translocation. Here, we examined the mechanisms of inh
Autor:
Jinshan Jin, Jianmei Cui, Krishna Damera, Binghe Wang, Bowen Ke, Ying-Hsin Hsieh, Phang C. Tai, Hsiuchin Yang
Publikováno v:
ChemMedChem. 8:1384-1393
SecA, a key component of bacterial Sec-dependent secretion pathway, is an attractive target for exploring novel antimicrobials. Rose bengal (RB), a polyhalogenated fluorescein derivative, was found from our previous study as a potent SecA inhibitor.
Autor:
Ying-Hsin Hsieh, Chun Jiang, Hao Zhang, Hsiuchin Yang, Sen-Fang Sui, Hongyun Wang, Phang C. Tai
Publikováno v:
Biochemical and Biophysical Research Communications. 431:388-392
Previous work showed that SecA alone can promote protein translocation and ion-channel activity in liposomes, and that SecYEG increases efficiency as well as signal peptide specificity. We now report that SecDF·YajC further increases translocation a
Autor:
Hao Zhang, Chaofeng Dai, Nannan Cao, Krishna Damera, Ying-Hsin Hsieh, Martti Vaara, Hsiuchin Yang, Jianmei Cui, Binghe Wang, Chun Jiang, Jinshan Jin, Arpana S. Chaudhary, Phang C. Tai
Publikováno v:
ChemMedChem. 11(22)
With the wide-spread emergence of drug resistance, there is an urgent need to search for new antimicrobials, especially those against Gram-negative bacteria. Along this line, the identification of viable targets is a critical first step. SecA is a pr
Autor:
Minyong Li, Fen-Biao Gao, Ying-Ju Huang, Phang C. Tai, Hsiuchin Yang, Hongyun Wang, Binghe Wang
Publikováno v:
ChemMedChem. 7:571-577
SecA is a central component of the general secretion system that is essential for bacterial growth and thus an ideal target for antimicrobial agents. A series of fluorescein analogues were first screened against the ATPase activity using the truncate
Autor:
Hsiuchin Yang, Bor-ruei Lin, Phang C. Tai, Chun Jiang, Ningren Cui, Bing Na, Hao Zhang, Ying-Hsin Hsieh, Sen-Fang Sui
Publikováno v:
Journal of Biological Chemistry. 286:44702-44709
SecA is an essential component of the Sec-dependent protein translocation pathway across cytoplasmic membranes in bacteria. Escherichia coli SecA binds to cytoplasmic membranes at SecYEG high affinity sites and at phospholipid low affinity sites. It