Zobrazeno 1 - 10 of 53 pro vyhledávání: '"Mee-Kyung Cha"'
1
Akademický článek
Decreased serum level of thioredoxin 1 in female patients with pneumonia and its combinational use with haptoglobin for the specific diagnoses of pneumonia and lung cancer
Autor: Mee-Kyung Cha, Il-Han Kim
Publikováno v: Pneumonia, Vol 6, Iss 0, Pp 18-25 (2015)
Thioredoxin 1 (Trx1) and haptoglobin (Hp) are known to be involved in pathophysiology. This study was conducted to evaluate their diagnostic significance. We employed an enzyme-linked immunosorbent assay (ELISA) to determine the concentrations of bot
Externí odkaz: https://doaj.org/article/dfc26f37938b412a9e47ddb313fb8f14
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3
Akademický článek
Thioredoxin 1 as a serum marker for breast cancer and its use in combination with CEA or CA15-3 for improving the sensitivity of breast cancer diagnoses.
Autor: Byung-Joon Park1 bjsl308@naver.com, Mee-Kyung Cha1 mkcha@pcu.ac.kr, Il-Han Kim1 ihkim@pcu.ac.kr
Publikováno v: BMC Research Notes. 2014, Vol. 7 Issue 1, p2-26. 25p. 5 Charts, 6 Graphs.
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4
Thioredoxin 1 as a serum marker for ovarian cancer and its use in combination with CA125 for improving the sensitivity of ovarian cancer diagnoses
Autor: Il-Han Kim, Mee-Kyung Cha, Byung-Joon Park
Publikováno v: Biomarkers. 19:604-610
The serum levels of Trx1 in patients with ovarian cancer were significantly higher than those in normal persons and patients with non-cancer inflammatory diseases. The level of Trx1 increased with the Figo stage. Ovarian cancer patients who were dete
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::233bdc3df1601574d7a9fc0c0eb0f526
https://doi.org/10.3109/1354750x.2014.956793
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5
Interaction between Saccharomyces cerevisiae glutaredoxin 5 and SPT10 and their in vivo functions
Autor: Mee-Kyung Cha, Seung-Keun Hong, Jeong-Tae Yeon, Il-Han Kim, Young-Mee Oh
Publikováno v: Free Radical Biology and Medicine. 52:1519-1530
Glutaredoxin 5 (Grx5) is a monothiol member of the Grx family that comprises two dithiol and three monothiol members. Using a yeast two-hybrid system, we isolated a Grx5-binding protein, SPT10, which has been previously suggested to act as a global t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c97771065afa9f071d42780528c80b3
https://doi.org/10.1016/j.freeradbiomed.2012.01.032
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6
Four thiol peroxidases contain a conserved GCT catalytic motif and act as a versatile array of lipid peroxidases in Anabaena sp. PCC7120
Autor: Seung-Keun Hong, Il-Han Kim, Mee-Kyung Cha
Publikováno v: Free Radical Biology and Medicine. 42:1736-1748
The Anabaena sp. (ANASP) genome contains seven open reading frames with homology to thiol peroxidase (TPx), also known as peroxiredoxin (Prx). Based on sequence similarities among putative TPx's derived from various cyanobacteria genomes, we designat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55f1d843c7b0e3ed1c53d85a7a26a177
https://doi.org/10.1016/j.freeradbiomed.2007.03.003
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7
Crystallization and preliminary X-ray analysis of a truncated mutant of yeast nuclear thiol peroxidase, a novel atypical 2-Cys peroxiredoxin
Autor: Soonwoong Choi, Jongkeun Choi, Mee-Kyung Cha, Jung Won Choi, Whanchul Shin, Il-Han Kim
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:659-662
Saccharomyces cerevisiae nTPx is a thioredoxin-dependent thiol peroxidase that is localized in the nucleus. nTPx belongs to the C-type atypical 2-Cys peroxiredoxin family members, which are frequently called BCPs or PrxQs. A double mutant (C107S/C112
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aad1eb3ad865ea870b8f0a9de00490f0
https://doi.org/10.1107/s1744309105016970
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8
Crystal Structure of Escherichia coli Thiol Peroxidase in the Oxidized State
Autor: Il-Han Kim, Mee-Kyung Cha, Jongkeun Choi, Soonwoong Choi, Jungwon Choi, Whanchul Shin
Publikováno v: Journal of Biological Chemistry. 278:49478-49486
Thioredoxin-dependent thiol peroxidase (Tpx) from Escherichia coli represents a group of antioxidant enzymes that are widely distributed in pathogenic bacterial species and which belong to the peroxiredoxin (Prx) family. Bacterial Tpxs are unique in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec7dec6f34a034dfddfce9395ed5bdcc
https://doi.org/10.1074/jbc.m309015200
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9
The Protein Interaction of Saccharomyces cerevisiae Cytoplasmic Thiol Peroxidase II with SFH2p and Its in Vivo Function
Autor: Young-Mee Oh, Seung-Keun Hong, Il-Han Kim, Mee-Kyung Cha
Publikováno v: Journal of Biological Chemistry. 278:34952-34958
Previously, we reported that the yeast cytoplasmic thiol peroxidase type II isoform (cTPx II), a member of the TSA/AhpC family, showed a very low peroxidase activity when compared with other cytoplasmic yeast isoforms, and that cTPx II mutant (cTPx I
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4d46d325a6c80815270071b61f41be0
https://doi.org/10.1074/jbc.m301819200
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10
Nuclear Thiol Peroxidase as a Functional Alkyl-hydroperoxide Reductase Necessary for Stationary Phase Growth of Saccharomyces cerevisiae
Autor: Won Cheol Kim, Kyoung Tai No, Seung-Keun Hong, Yong Soo Choi, Mee Kyung Cha, Il Han Kim
Publikováno v: Journal of Biological Chemistry. 278:24636-24643
Yeast nucleus-localized thiol peroxidase (nTPx) was characterized as a functional peroxidase. There are two cysteine residues in nTPx. Replacement of Cys-106 or Cys-111 with serine resulted in a complete loss of thioredoxin-linked peroxidase activity
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dc4a851d57dbf6996cf5a641ca8a4ee
https://doi.org/10.1074/jbc.m302628200
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