Zobrazeno 1 - 10
of 65
pro vyhledávání: '"Ho Zoon Chae"'
Autor:
Dong-Hyung Cho, Eunji Kim, Sang-Young Chun, Jeong Su Oh, Yong Seok Park, Jae-Sung Kim, Hyuk-Joon Jeon, Ho Zoon Chae
Publikováno v:
Biochemical and Biophysical Research Communications. 489:193-199
Peroxiredoxins (Prxs) are highly conserved antioxidant enzymes and are implicated in multiple biological processes; however, their function in oocyte meiosis has not been studied. Here we show that inhibition of Prx I and II results in spindle defect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecdbe58c6dbd3170feed8ded9332ce90
https://doi.org/10.1016/j.bbrc.2017.05.127
https://doi.org/10.1016/j.bbrc.2017.05.127
Autor:
Hae Young Lee, Hyun-Su Jo, Ho Zoon Chae, Nam-Soo Cho, Min-Hee Kim, Yang-Han Lee, In Kwan Hwang, Dong-Ho Choi, Pil-Won Kang, Ki-Won Park
Publikováno v:
Forensic Science International. 255:80-84
The mottled skate, Beringraja pulchra is one of the commercially important fishes in the market today. However, B. pulchra identification methods have not been well developed. The current study reports a novel real-time PCR method based on TaqMan tec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::778a2a8f3f0a881f7b384964849f8c53
https://doi.org/10.1016/j.forsciint.2015.05.028
https://doi.org/10.1016/j.forsciint.2015.05.028
Publikováno v:
Journal of Applied Pharmaceutical Science. :011-016
Importance of dedicated webservers and specialized software for simulations of protein-protein interactions is well established. The purpose of our study was to examine the protein-protein interaction that occurred under physiological and stress cond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44b061ee6f17585b73b4679fb20979a1
https://doi.org/10.7324/japs.2015.50803
https://doi.org/10.7324/japs.2015.50803
Autor:
Yong-Hoon Kim, Ho Zoon Chae, Dongryeol Ryu, Hueng Sik Choi, Brian A. Hemmings, Inkyu Lee, Chul-Ho Lee, Kyung Seok Kim, Eun Kyung Yoo, Seung Hoi Koo, Sudha B. Biddinger, Jeong Sun Kim, Keum Jin Yang, Yanning Wang, Jongsun Park, Debby Hynx, Don Kyu Kim
Publikováno v:
Diabetologia. 57:2576-2585
Aims/hypothesis Insulin resistance, a major contributor to the pathogenesis of type 2 diabetes, leads to increased hepatic glucose production (HGP) owing to an impaired ability of insulin to suppress hepatic gluconeogenesis. Nuclear receptor oestroge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0e6a338678ea3d2b706594449a6fcb9
https://doi.org/10.1007/s00125-014-3366-x
https://doi.org/10.1007/s00125-014-3366-x
Autor:
Doh Hoon Kim, Young Soo Chung, Hyun-Ah So, Hong-Kyu Choi, Jai-Heon Lee, Eunsook Chung, Chang-Woo Cho, Jee-Eun Heo, Ho Zoon Chae
Publikováno v:
Plant Cell, Tissue and Organ Culture (PCTOC). 108:473-484
A mungbean low temperature-inducible VrPrx1 encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced VrPrx1 amino acid sequence showed highest sequence homology to 2-Cys Prxs of Phaseolus vulgaris (95%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::225e3b85a52c86634f77f282c5623c8c
https://doi.org/10.1007/s11240-011-0061-1
https://doi.org/10.1007/s11240-011-0061-1
Publikováno v:
Scopus-Elsevier
To screen chaperone proteins from Schizosaccharomyce pombe (S. pombe), we prepared recombinant citrate synthase of the fission yeast as a substrate of anti-aggregation assay. Purified recombinant citrate synthase showed citrate synthase activity and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::312546b07dd461606d2f9468233f7d3c
https://doi.org/10.5483/bmbrep.2009.42.12.812
https://doi.org/10.5483/bmbrep.2009.42.12.812
Publikováno v:
Protein Expression and Purification. 66:35-38
In this study, we report the simultaneous refolding and reconstitution of the recombinant Bax inhibitor-1 (BI-1) from inclusion bodies expressed in Escherichia coli . A functional assay showed that the resulting proteoliposomes responded to acidic co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7146e9962bd7121dc3404b4764f77f4c
https://doi.org/10.1016/j.pep.2009.01.005
https://doi.org/10.1016/j.pep.2009.01.005
Autor:
Ho Zoon Chae, Yu Sam Kim, Jung Chae Lim, Jae Ho Seo, Taeho Ahn, Chul-Ho Yun, Kyung Seok Kim, Grzegorz Piszczek, Kanghwa Kim, P. Boon Chock, Duck-Yeon Lee, Hyung Wook Nam
Publikováno v:
Journal of Biological Chemistry. 284:13455-13465
Peroxiredoxins (Prxs) are a group of peroxidases containing a cysteine thiol at their catalytic site. During peroxidase catalysis, the catalytic cysteine, referred to as the peroxidatic cysteine (CP), cycles between thiol (CP-SH) and disulfide (–S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0d5e09b4b8344acfb46153db149cf404
https://doi.org/10.1074/jbc.m900641200
https://doi.org/10.1074/jbc.m900641200
Publikováno v:
FEBS Journal. 276:2285-2291
We investigated the functional activity of recombinant Bax inhibitor-1 reconstituted into liposomes. When proteoliposomes were suspended in acidic solutions, encapsulated Ca(2+) was released from the membranes, as previously suggested [Kim HR, Lee GH
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c2f83e556f0ef27109f0a2da7de2b11
https://doi.org/10.1111/j.1742-4658.2009.06956.x
https://doi.org/10.1111/j.1742-4658.2009.06956.x
Autor:
Ki-Sun Kwon, Sue Goo Rhee, Yu Sun Park, Yu Sam Kim, Ho Zoon Chae, Kanghwa Kim, Jung Chae Lim, Hyung Wook Nam, Hyun Ae Woo, Hoon-In Choi
Publikováno v:
Journal of Biological Chemistry. 283:28873-28880
The thiol (-SH) of the active cysteine residue in peroxiredoxin (Prx) is known to be reversibly hyperoxidized to cysteine sulfinic acid (-SO(2)H), which can be reduced back to thiol by sulfiredoxin/sestrin. However, hyperoxidized Prx of an irreversib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f271266c3d65c18b1a2870ad3304d1a5
https://doi.org/10.1074/jbc.m804087200
https://doi.org/10.1074/jbc.m804087200