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pro vyhledávání: '"621"'
Autor:
Huihui Chong, Meitian Wang, Chao Zhang, Sandro Waltersperger, Bo Qin, Yuxian He, Zonglin Qiu, Xue Yao, Sheng Cui, Ruiyun Han
Publikováno v:
Journal of Biological Chemistry
CP32M is a newly designed peptide fusion inhibitor possessing potent anti-HIV activity, especially against T20-resistant HIV-1 strains. In this study, we show that CP32M can efficiently inhibit a large panel of diverse HIV-1 variants, including subty
Publikováno v:
Journal of Biological Chemistry. 273:11150-11157
The extracellular domain of the human epidermal growth factor receptor (sEGFR) consists of 621 amino acid residues, including 50 cysteines. The connections of the 25 disulfide bonds in the recombinant sEGFR protein, obtained from Chinese hamster ovar