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result(s) for
"Jo, Geunhyeong"
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Cell growth inhibitory effects of polyphenols with naphthalene skeleton against cisplatin-resistant ovarian cancer cells
by
Shin, Soon Young
,
Park, Jihyun
,
Jo, Geunhyeong
in
animal ovaries
,
Anticancer properties
,
Antitumor agents
2018
Cisplatin often shows the drug resistance which could limit the chemotherapeutic efficacy. Thus, it is necessary to develop anticancer agents against cisplatin-resistant cancer cells. To identify pharmacophores exhibiting the cell growth inhibitory effect against cisplatin-resistant A2780/Cis ovarian cancer cells, we prepared 35 synthetic polyphenols bearing naphthalene skeleton including naphthalenyl chalcones, naphthalenyl flavones, naphthalenyl flavanones, 4,5-dihydro-1
H
-pyrazol-3-yl)naphthalen-2-ols, naphthalen-1-yl-
N
-phenyl-4,5-dihydro-1
H
-pyrazole-1-carbothioamides, and 4,5-dihydro-1
H
-pyrazol-3-yl)naphthalen-1-ol. The correlation between their inhibitory effects and structural properties was evaluated using hologram quantitative structure activity relationship and comparative molecular field analysis. The pharmacophores derived here can lead us to design new polyphenols against the growth of cisplatin-resistant cells.
Journal Article
A Compound isolated from Rumex japonicus induces early growth response gene-1 expression
by
Hyun Jiye
,
Dong, Kwang Sik
,
Lee Young Han
in
Anticancer properties
,
Antitumor activity
,
Colon
2011
A compound was isolated from the root of Rumex japonicus. Based on spectroscopic data including nuclear magnetic resonance spectroscopy and mass spectrometry, the chemical structure of the compound was determined to be 1,8-dihydroxy-3-methoxy-6-methylanthracene-9,10-dione. The compound exhibits antitumor activity due to inhibition of clonogenicity and induction of tumor suppressor early growth response gene-1 in HCT116 colon cancer cells.
Journal Article
A peptide produced by Pseudomonas tolaasi, tolaasin binds to metal ions
2011
Brown blotch disease in mushrooms is caused by Pseudomonas tolaasin, which produces a peptide toxin, tolaasin I, and zinc ion inhibits the channel formed by tolaasin I. NMR experiments revealed that zinc, sodium, and calcium ions can bind to tolaasin I and their binding position on tolaasin I is the lactone ring.
Journal Article