http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
장정호 고려대학교 한국언어문화학술확산연구소 2012 Journal of Korean Culture Vol.19 No.-
中․韓 訟事小說에서 긍정적인 女性形象 이미지 부각은 孝女․烈女에 그 초점을 맞추고 있다. 이는 중국이나 한국 모두 봉건시대 三從之道와 女必從夫 등의 유교적 이념이 바탕이 되고 있기 때문이다. 억울하게 죽은 아버지와 남편의 원수를 갚기 위해 복수하고, 사경에 처한 남편을 구출하기 위해 자신을 희생하는 것에는 이러한 동력이 뒷받침되고 있다. 이들의 복수에는 정의로운 동기가 부여되는데 이 정의로운 동기가 바로 孔子에서 비롯된 儒敎의 복수관이라고 할 수 있다. 中․韓 訟事小說은 계모라는 특정 인물을 통해 惡母의 형상을 부각시키고 있다. 작품 속의 계모들은 시기심으로 가득 차 있으며 가정 내의 재산상속권을 둘러싸고 악행을 벌인다.
Substrate recognition and catalytic mechanism of 5’–3’ exoribonucleases
장정호,Liang Tong 한국구조생물학회 2014 Biodesign Vol.2 No.2
The family of 5'-3' exoribonucleases (XRNs) plays a significant role in RNA processing, RNA turnover and decay, RNAinterference, mRNA transcription, and other cellular processes. Cytoplasmic Xrn1 and nuclear Xrn2/Rat1 are observed inmost eukaryotes. The structural information for Xrn1 and Rat1 is available, revealing the detailed enzymatic mechanism ofthese nucleases. Sequence analysis of XRNs shows 2 highly conserved regions, named CR1 and CR2, which form a singledomain. An additional C-terminal region containing 510 residues is only found in Xrn1. Structural analysis showed thatCR1 has homology with the FEN superfamily of endonucleases, while CR2 blocks substrate penetration to the active site. Therefore, XRNs are exclusive exoribonucleases. This review summarizes our current understanding of these enzymes,focusing on their crystal structures, substrate recognition, selectivity and processivity.
Crystal structure of the bacterial type VI secretion system component TssL from Vibrio cholerae
장정호,김연길 한국미생물학회 2015 The journal of microbiology Vol.53 No.1
The type VI secretion system (T6SS), commonly found inGram-negative bacteria, is responsible for exporting effectorproteins. The T6SS has been reported to be cytotoxic to hostcells. While the components and assembly of the T6SS complexhave been largely assessed, structural data on T6SS componentsfrom virulent bacteria is remarkably insufficient. Here, we report the crystal structure of Vibrio cholerae TssL(VcTssL), a core component of T6SS. In spite of a relativelylow sequence identity, the overall structure of VcTssL is largelysimilar to those from other bacterial homologs exceptfor several differences found in local structural elements. Aunique feature attributed to the C-terminal fragment of Vc-TssL is a crystallographic artifact. This incidental feature ofVcTssL may provide insights into screening of molecularpartners for the cytoplasmic domain of TssL. Additionally,our results may help in the design of molecular probes for adetailed understanding of the functional relationship betweenTssL and other T6SS components.