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A chemical biology route to site-specific authentic protein modifications
Yang, Aerin,Ha, Sura,Ahn, Jihye,Kim, Rira,Kim, Sungyoon,Lee, Younghoon,Kim, Jaehoon,Sö,ll, Dieter,Lee, Hee-Yoon,Park, Hee-Sung American Association for the Advancement of Scienc 2016 Science Vol.354 No.6312
<P>Many essential biological processes are controlled by posttranslational protein modifications. The inability to synthetically attain the diversity enabled by these modifications limits functional studies of many proteins. We designed a three-step approach for installing authentic posttranslational modifications in recombinant proteins. We first use the established O-phosphoserine (Sep) orthogonal translation system to create a Sep-containing recombinant protein. The Sep residue is then dephosphorylated to dehydroalanine (Dha). Last, conjugate addition of alkyl iodides to Dha, promoted by zinc and copper, enables chemoselective carbon-carbon bond formation. To validate our approach, we produced histone H3, ubiquitin, and green fluorescent protein variants with site-specific modifications, including different methylations of H3K79. The methylated histones stimulate transcription through histone acetylation. This approach offers a powerful tool to engineer diverse designer proteins.</P>
김애린(Aerin Kim),임혜빈(Hye Bin Im),장한슬(Hansl Chang),박주화(Juhwa Park),기승연(Seungyeon Ki),정윤정(Yoon Jung Jeong),김수진(Sujin Kim),신주영(Juyeong Shin),이기형(Keehyeung Lee) 한국언론정보학회 2016 한국언론정보학보 Vol.80 No.6
이 연구는 지난 몇 년간 한국사회에서 상당한 관심과 조명을 받고 있는 ‘헬조선’ 현상을 진단한다. 특히 이 작업은 정파성을 달리하는 주요 언론들 속에 제시된 헬조선 관련 기사와 기고문, 그리고 특집을 텍스트 분석으로 진단하면서, 이 매우 복합적인 현상의 재현적인 측면의 함의와 명암을 다면적으로 탐구하고자 한다. 헬조선으로 지칭되는 특정한 문제의식과 감정의 생산이 현재 청년층이 대면하는 매우 심각하고 불안한 사회경제적인 현실 속에서 부상했다는 맥락성을 고려할 때, 이러한 문제의식과 방향성을 탐구하는 연구가 일정한 지적·비판적인 기여를 할 수 있을 것으로 판단된다. This work critically explores the so-called “Hell-Chosun” phenomenon which has gained much attention and responses in contemporary South Korea. The younger generation came to coin and utilize this new linguistic expression as well as poignant parody as a way of releasing their anger, cynicism, and frustration in the context of the omnipresent fierce competitions, deepening social instability, and job-related shrinking possibilities. The ‘Hell-Chosun’ phenomenon can be considered as a much complicated manifestation of the structures of feeling for the part of many younger generation South Koreans. This paper especially examines the varying representation of this phenomenon by established dailies through an in-depth textual analysis of newspaper articles, opinion pieces and reviews, as well as special issues. In doing so, this work examines the multiple implications of this particular socio-cultural phenomenon in a detailed and critical fashion.
Lee, Sukmook,Yoon, Il-Hee,Yoon, Aerin,Cook-Mills, Joan M,Park, Chung-Gyu,Chung, Junho American Association of Immunologists 2012 Journal of Immunology Vol. No.
<P>VCAM-1 plays a key role in leukocyte trafficking during inflammatory responses. However, molecular mechanisms underlying this function have not been clearly elucidated. In this study, using phage display technology, we developed a rabbit/human chimeric VCAM-1 Ab, termed VCAM-1 domain 6 (VCAM-1-D6), which specifically recognizes aa 511-599 within the sixth Ig-like domain. We report that the VCAM-1-D6 Ab blocked U937 cell transmigration across activated HUVECs but did not alter adhesion of U937 cells to the HUVECs. We also demonstrate that VCAM-1-D6 does not alter TNF-α-stimulated endothelial cell chemokine or cytokine production. Furthermore, through in vivo efficacy testing using a mouse islet allograft model, we demonstrate that VCAM-1-D6 significantly alleviates allograft rejection by blocking leukocyte infiltration to the grafted islets. Taken together, our results suggest that the VCAM-1-D6 Ab may block VCAM-1-mediated inflammation and could be a useful tool in treating inflammatory diseases.</P>
Yang, Wonjun,Yoon, Aerin,Lee, Sanghoon,Kim, Soohyun,Han, Jungwon,Chung, Junho Nature Publishing Group 2017 Experimental and molecular medicine Vol.49 No.3
<P>Phage display technology provides a powerful tool to screen a library for a binding molecule via an enrichment process. It has been adopted as a critical technology in the development of therapeutic antibodies. However, a major drawback of phage display technology is that because the degree of the enrichment cannot be controlled during the bio-panning process, it frequently results in a limited number of clones. In this study, we applied next-generation sequencing (NGS) to screen clones from a library and determine whether a greater number of clones can be identified using NGS than using conventional methods. Three chicken immune single-chain variable fragment (scFv) libraries were subjected to bio-panning on prostate-specific antigen (PSA). Phagemid DNA prepared from the original libraries as well as from the <I>Escherichia coli</I> pool after each round of bio-panning was analyzed using NGS, and the heavy chain complementarity-determining region 3 (HCDR3) sequences of the scFv clones were determined. Subsequently, through two-step linker PCR and cloning, the entire scFv gene was retrieved and analyzed for its reactivity to PSA in a phage enzyme immunoassay. After four rounds of bio-panning, the conventional colony screening method was performed for comparison. The scFv clones retrieved from NGS analysis included all clones identified by the conventional colony screening method as well as many additional clones. The enrichment of the HCDR3 sequence throughout the bio-panning process was a positive predictive factor for the selection of PSA-reactive scFv clones.</P>
한정원,이종혁,윤수민,Aerin Yoon,황도빈,Hwa K Lee,Min S Kim,이유진,Won J Yang,박선영,윤홍덕,김효리,정준호 생화학분자생물학회 2016 Experimental and molecular medicine Vol.48 No.-
The C-terminal domain of RNA polymerase II is an unusual series of repeated residues appended to the C-terminus of the largest subunit and serves as a flexible binding scaffold for numerous nuclear factors. The binding of these factors is determined by the phosphorylation patterns on the repeats in the domain. In this study, we generated a synthetic antibody library by replacing the third heavy chain complementarity-determining region of an anti-HER2 (human epidermal growth factor receptor 2) antibody (trastuzumab) with artificial sequences of 7–18 amino-acid residues. From this library, antibodies were selected that were specific to serine phosphopeptides that represent typical phosphorylation patterns on the functional unit (YSPTSPS)2 of the RNA polymerase II C-terminal domain (CTD). Antibody clones pCTD-1stS2 and pCTD-2ndS2 showed specificity for peptides with phosphoserine at the second residues of the first or second heptamer repeat, respectively. Additional clones specifically reacted to peptides with phosphoserine at the fifth serine of the first repeat (pCTD-1stS5), the seventh residue of the first repeat and fifth residue of the second repeat (pCTD-S7S5) or the seventh residue of either the first or second repeat (pCTD-S7). All of these antibody clones successfully reacted to RNA polymerase II in immunoblot analysis. Interestingly, pCTD-2ndS2 precipitated predominately RNA polymerase II from the exonic regions of genes in genome-wide chromatin immunoprecipitation sequencing analysis, which suggests that the phosphoserine at the second residue of the second repeat of the functional unit (YSPTSPS)2 is a mediator of exon definition.