http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
유화정,이호섭,김애리,김일환 대한피부과학회 2003 大韓皮膚科學會誌 Vol.41 No.3
Basal cell carcinoma(BCC) exists in great variety. Adamantinoid BCC is one of the rare types of BCC. Histologically, the tumor masses are surrounded by a layer of cells in which the nuclei tend to palisade. Inside this layer, the tumor masses consist of cells with elongated nuclei and stellate cytoplasm stretched as thin, connection bridges across empty spaces, producing adamantinoid appearance. We report a case of adamantinoid BCC in a 49 year-old woman who had a single, asymptomatic, dusky erythematous to black colored nodule on her right jaw area. (Korean J Dermatol 2003;41(3) : 380∼382)
NMR elucidation of reduced B-Z transition activity of PKZ protein kinase at high NaCl concentration
Lee, Ae-Ree,Seo, Yeo-Jin,Choi, Seo-Ree,Ryu, Kyoung-Seok,Cheong, Hae-Kap,Lee, Shim Sung,Katahira, Masato,Park, Chin-Ju,Lee, Joon-Hwa Elsevier 2017 Biochemical and biophysical research communication Vol. No.
<P><B>Abstract</B></P> <P>A Z-DNA binding protein (ZBP)-containing protein kinase (PKZ) in fish species has an important role in the innate immune response. Previous structural studies of the Zα domain of the PKZ from <I>Carassius auratus</I> (caZα<SUB>PKZ</SUB>) showed that the protein initially binds to B-DNA and induces B-Z transition of double stranded DNA in a salt concentration-dependent manner. However, the significantly reduced B-Z transition activity of caZα<SUB>PKZ</SUB> at high salt concentration was not fully understood. In this study, we present the binding affinity of the protein for B-DNA and Z-DNA and characterize its extremely low B-Z transition activity at 250 mM NaCl. Our results emphasize that the B-DNA-bound form of caZα<SUB>PKZ</SUB> can be used as molecular ruler to measure the degree of B-Z transition.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The B-Z transition activity of caZα<SUB>PKZ</SUB> is uniquely dependent on salt concentration. </LI> <LI> caZα<SUB>PKZ</SUB> has reduced binding affinity for B-DNA at high NaCl. </LI> <LI> The equilibrium constant for the B-Z transition by a DNA-bound caZα<SUB>PKZ</SUB> was reduced. </LI> <LI> The chemical shifts of the B-DNA-bound form reflect the degree of B-Z transition. </LI> </UL> </P>
Lee, Sungjin,Lee, Ae-Ree,Ryu, Kyoung-Seok,Lee, Joon-Hwa,Park, Chin-Ju Academic Press 2019 Journal of molecular biology Vol.431 No.4
<P><B>Abstract</B></P> <P>Bloom syndrome protein (BLM) is one of five human RecQ helicases that participate in DNA metabolism. RecQ C-terminal (RQC) domain is the main DNA binding module of BLM and specifically recognizes G-quadruplex (G4) DNA structures. Because G4 processing by BLM is essential for regulating replication and transcription, both G4 and BLM are considered as potential targets for anticancer therapy. Although several studies have revealed the detailed mechanism of G4 unwinding by BLM, the initial recognition of the G4 structure by the RQC domain is unclear. Here, we investigated the interaction between BLM RQC and the G4 DNA from the c-Myc promoter by NMR spectroscopy. While the signals broadened upon reciprocal titrations, the β-wing of RQC had significant chemical shift perturbations and experienced millisecond timescale dynamics upon G4 binding. A point mutation in the β-wing (N1164A) reduced G4 binding affinity. Our hydrogen–deuterium exchange data indicate that imino protons of G4 were exchanged with deuterium much faster in the presence of RQC. We suggest that RQC binds to G4 by using the β-wing as a separating pin to destabilize the G4. By providing information about the RQC–G4 interaction, our study yields insight into potential strategies for preventing G4 processing by BLM.</P> <P><B>Highlights</B></P> <P> <UL> <LI> RecQ C-terminal (RQC) domain of Bloom syndrome protein (BLM) binds to the G-quadruplex with micromolar <I>K</I> <SUB>d</SUB>. </LI> <LI> β-wing and α2 region of the RQC domain play an important role in the G-quadruplex interaction. </LI> <LI> BLM RQC domain destabilizes G-quadruplex without the helicase domain of the protein. </LI> <LI> Our results contribute to the understanding of the initial G4 recognition process of BLM. </LI> </UL> </P> <P><B>Graphical Abstract</B></P> <P>[DISPLAY OMISSION]</P>
NMR Study on the Preferential Binding of the Zα Domain of Human ADAR1 to CG-repeat DNA Duplex
Lee, Ae-Ree,Choi, Seo-Ree,Seo, Yeo-Jin,Lee, Joon-Hwa Korean Magnetic Resonance Society 2017 Journal of the Korean Magnetic Resonance Society Vol.21 No.3
The Z-DNA domain of human ADAR1 ($Z{\alpha}_{ADAR1}$) produces B-Z junction DNA through preferential binding to the CG-repeat segment and destabilizing the neighboring AT-rich region. However, this study could not answer the question of how many base-pairs in AT-rich region are destabilized by binding of $Z{\alpha}_{ADAR1}$. Thus, we have performed NMR experiments of $Z{\alpha}_{ADAR1}$ to the longer DNA duplex containing an 8-base-paired (8-bp) CG-repeat segment and a 12-bp AT-rich region. This study revealed that $Z{\alpha}_{ADAR1}$ preferentially binds to the CG-repeat segment rather than AT-rich region in a long DNA and then destabilizes at least 6 base-pairs in the neighboring AT-rich region for efficient B-Z transition of the CG-repeat segment.
NMR Study of the pH Effect on the DNA Binding Affinity of Human RPA
Lee, Min-Woo,Choi, Ju-Hyeok,Choi, Jae-Gyu,Lee, Ae-Ree,Lee, Joon-Hwa 한국자기공명학회 2016 Journal of the Korean Magnetic Resonance Society Vol.20 No.3
The replication protein A (RPA) plays a crucial role in DNA replication, recombination, and repair. RPA consists of 70, 32 and 14 kDa subunits and has high single-stranded DNA (ssDNA) binding affinity. The largest subunit, RPA70, mainly contributes to bind to ssDNA as well as interact with many cellular and viral proteins. In this study, we performed nuclear magnetic resonance experiments on the complex of the DNA binding domain A of human RPA70 (RPA70A) with ssDNA, d(CCCCC), at various pH, to understand the effect of pH on the ssDNA binding of RPA70A. The chemical shift perturbations of binding residues were most significant at pH 6.5 and they reduced with pH increment. This study provides valuable insights into the molecular mechanism of the ssDNA binding of human RPA.