Yi Wang
Hokkaido University
6 Papers
5 Citations
Yi Wang is an academic researcher from Hokkaido University. The author has contributed to research in topics: Chemistry & Antimicrobial peptides. The author has an hindex of 1, co-authored 1 publications.
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Papers
Potent bactericidal activity of reduced cryptdin-4 derived from its hydrophobicity and mediated by bacterial membrane disruption
Yuji Sato,Yi Wang,Yuchi Song,Weiming Geng,Shaonan Yan,Kiminori Nakamura,Takashi Kikukawa,Makoto Demura,Tokiyoshi Ayabe,Tomoyasu Aizawa +9 more
TL;DR: The results suggest that the potent bactericidal activity of Crp4 red is derived from its hydrophobicity, and the bactericidal mechanism involves disruption of the bacterial membrane.
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The Dynamic Transcription Profiles of Proliferating Bovine Ovarian Granulosa When Exposed to Increased Levels of β-Hydroxybutyric Acid
TL;DR: The dynamic transcription profiles of granulosa cells under different levels of β-hydroxybutyric stress are described and key regulators that may underlie the detrimental effects on the development of follicles and granul Rosa cells are reported, thus representing potential therapeutic targets to improve fertility in dairy cows with subclinical ketosis or clinical ketosis.
4
Potent bactericidal activity of reduced cryptdin-4 derived from its hydrophobicity and mediated by bacterial membrane disruption
Yuji Sato,Yi Wang,Yuchi Song,Weiming Geng,Shaonan Yan,Kiminori Nakamura,Takashi Kikukawa,Makoto Demura,Tokiyoshi Ayabe,Tomoyasu Aizawa +9 more
TL;DR: The results suggest that the potent bactericidal activity of Crp4red is derived from its hydrophobicity, and the bactericidal mechanism involves disruption of the bacterial membrane.
4
Efficient recombinant production of mouse-derived cryptdin family peptides by a novel facilitation strategy for inclusion body formation
Yuchi Song,Yi Wang,Shaonan Yan,Kiminori Nakamura,Takashi Kikukawa,Tokiyoshi Ayabe,Tomoyasu Aizawa +6 more
TL;DR: In this paper , a method for the production of the cryptdin family of cysteine-containing antimicrobial peptides was proposed, which is able to significantly increase the expression efficiency of Crps by promoting the formation of erroneous intermolecular disulfide bonds between HLA and Crps, thereby promoting protein aggregation and inclusion body formation, which prevented degradation.
Antimicrobial Properties and Mode of Action of Cryptdin-4, a Mouse α-Defensin Regulated by Peptide Redox Structures and Bacterial Cultivation Conditions
Yi Wang,Yuchi Song,Shaonan Yan,Rina Hiramine,Yuki Ohnishi,Yuki Yokoi,Kiminori Nakamura,Takashi Kikukawa,Tokiyoshi Ayabe,Tomoyasu Aizawa +9 more
TL;DR: In this article , the antibacterial mechanisms of crp4 in both forms under both aerobic and anaerobic conditions were investigated using Escherichia coli (E. coli), a facultative bacterium, as a model.