• Journal of Microbiology and Biotechnology
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• 제26권12호
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• pp.2019-2029
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• 2016

Zinc finger proteins are among the most extensively applied metalloproteins in the field of biotechnology owing to their unique structural and functional aspects as transcriptional and translational regulators. The classical zinc fingers are the largest family of zinc proteins and they provide critical roles in physiological systems from prokaryotes to eukaryotes. Two cysteine and two histidine residues ($Cys_2His_2$) coordinate to the zinc ion for the structural functions to generate a ${\beta}{\beta}{\alpha}$ fold, and this secondary structure supports specific interactions with their binding partners, including DNA, RNA, lipids, proteins, and small molecules. In this account, the structural similarity and differences of well-known $Cys_2His_2$-type zinc fingers such as zinc interaction factor 268 (ZIF268), transcription factor IIIA (TFIIIA), GAGA, and Ros will be explained. These proteins perform their specific roles in species from archaea to eukaryotes and they show significant structural similarity; however, their aligned amino acids present low sequence homology. These zinc finger proteins have different numbers of domains for their structural roles to maintain biological progress through transcriptional regulations from exogenous stresses. The superimposed structures of these finger domains provide interesting details when these fingers are applied to specific gene binding and editing. The structural information in this study will aid in the selection of unique types of zinc finger applications in vivo and in vitro approaches, because biophysical backgrounds including complex structures and binding affinities aid in the protein design area.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1998년도 학술발표회
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• pp.11-11
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• 1998

Zinc fingers of Cys$_2$His$_2$ class constitute one of the most common DNA binding motifs in eukaryotes. Unlike other DNA binding motifs, zinc finger proteins recognize very diverse DNA sites, and their sequence specificities can be systematically changed by phage display.(omitted)

• Molecules and Cells
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• 제23권3호
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• pp.316-322
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• 2007

Zinc finger transcription factor genes are a significant fraction of the genes in the vertebrate genome. Here we report the isolation and characterization of a human zinc finger-containing gene, ZNF435, from a fetal brain cDNA library. ZNF435 cDNA is 1290 base pairs in length and contains an open reading frame encoding 349 amino acids with four C2H2-type zinc fingers at its carboxyl terminus and a SCAN motif at its amino terminus. RT-PCR results showed that ZNF435 was expressed in all tested tissues. A ZNF435-GFP fusion protein was located in the nucleus and the four zinc fingers acted as nuclear localization signals (NLSs). ZNF435 was found to be capable of homo-association, and this effect was independent of its zinc fingers. Furthermore, ZNF435 proved to be a transcription repressor as its overexpression in AD293 cells inhibited the transcriptional activities of AP-1.

• Molecules and Cells
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• 제40권8호
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• pp.533-541
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• 2017

Engineered DNA-binding domains provide a powerful technology for numerous biomedical studies due to their ability to recognize specific DNA sequences. Zinc fingers (ZF) are one of the most common DNA-binding domains and have been extensively studied for a variety of applications, such as gene regulation, genome engineering and diagnostics. Another novel DNA-binding domain known as a transcriptional activator-like effector (TALE) has been more recently discovered, which has a previously undescribed DNA-binding mode. Due to their modular architecture and flexibility, TALEs have been rapidly developed into artificial gene targeting reagents. Here, we describe the methods used to design these DNA-binding proteins and their key applications in biomedical research.

• Molecules and Cells
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• 제26권2호
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• pp.175-180
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• 2008

$I{\kappa}B$ kinase (IKK), the pivotal kinase in signal-dependent activation of nuclear factor-${\kappa}B$ (NF-${\kappa}B$), is composed of multiple protein components, including IKK ${\alpha}/{\beta}/{\gamma}$ core subunits. To investigate the regulation of the IKK complex, we immunoaffinity purified the IKK complex, and by MALDI-TOF mass spectrometry identified a splice variant of zinc finger protein 268 (ZNF268) as a novel IKKinteracting protein. Both the full-length and the spliced form of the ZNF268 protein were detected in a variety of mammalian tissues and cell lines. The genes were cloned and expressed by in vitro transcription/translation. Several deletion derivatives, such as KRAB domain (KRAB) on its own, the KRAB/spacer/4-zinc fingers (zF4), and the spacer/4-zinc fingers (zS4), were ectopically expressed in mammalian cells and exhibited had different subcellular locations. The KRAB-containing mutants were restricted to the nucleus, while zS4 was localized in the cytosol. TNF-${\alpha}$-induced NF-${\kappa}B$ activation was examined using these mutants and only zS4 was found to stimulate activation. Collectively, the results indicate that a spliced form of ZNF268 lacking the KRAB domain is located in the cytosol, where it seems to play a role in TNF-${\alpha}$-induced NF-${\kappa}B$ activation by interacting with the IKK complex.

• 한국표면공학회지
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• 제26권6호
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• pp.307-315
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• 1993

A study on a new anti-finger printed EGI steel sheet with high corrosion resistance has been carried out to meet the recent requirement of high quality and performance of the pure zinc electrogalvanized steel sheet. The substrate was the pure zinc electrogalvanized sheet with the metallic coating of 20g/$\m^2$. The two differ-ent processes for inorganic(chromating) and organic(resin) coating were applied. One was a two coat/two bake type to separately treat chromating and resin coating which is now widely used. The other was a one coat/one bake type to simultaneously treat them which is newly developed in this study. The solution for the one coat/one bake type was an aqua-base coating agents which was composed of inorganic and organic components. The new anti-finger printed EGI steel sheet with the Cr and resin coating weight of 13mg/$\m^2$ and 800mg/$\m^2$, respectively shows the superior corrosion resistance besides the good paintability, formability fingerprint resistance and earth characteristics properties.

• 한국식물병리학회:학술대회논문집
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• 한국식물병리학회 2003년도 정기총회 및 추계학술발표회
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• pp.79.2-80
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• 2003

To better understand plant defense responses against pathogen attack, we identified the transcription factor-encoding genes in the hot pepper Capsicum annuum that show altered expression patterns during the hypersensitive response raised by challenge with bacterial pathogens. One of these genes, Ca1244, was characterized further. This gene encodes a plant-specific Type IIIA - zinc finger protein that contains two Cys$_2$His$_2$zinc fingers. Ca1244 expression is rapidly and specifically induced when pepper plants are challenged with bacterial pathogens to which they are resistant. In contrast, challenge with a pathogen to which the plants are susceptible only generates weak Ca1244 expression. Ca1244 expression is also strongly induced in pepper leaves by the exogenous application of ethephon, an ethylene releasing compound. Whereas, salicylic acid and methyl jasmonate had moderate effects. Pepper protoplasts expressing a Ca1244-smGFP fusion protein showed Ca1244 localizes in the nucleus. Transgenic tobacco plants overexpressing Ca1244 driven by the CaMV 355 promoter show increased resistance to challenge with a tobacco-specific bacterial pathogen. These plants also showed constitutive upregulation of the expression of multiple defense-related genes. These observations provide the first evidence that an Type IIIA - zinc finger protein, Ca1244, plays a crucial role in the activation of the pathogen defense response in plants.

• 분석과학
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• 제32권3호
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• pp.105-112
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• 2019

Fingerprints may be contaminated with ethanol solutions. In order to solve the case, the law enforcement agency may need to visualize the fingerprint from these samples, but the development method has not been studied. The paper with latent fingerprint was contaminated with ethanol solution and then the blurring of ridge detail was observed. As a result, when the copy paper was contaminated with ethanol solutions of less than 75 % (v/v), the amino acid components of latent fingerprint residue blurred but lipid components of latent fingerprint residue didn't blurred. On the other hand, when the paper was contaminated with ethanol solution of more than 80 % (v/v), the amino acid components of latent fingerprint didn't blurred but the lipid components of latent fingerprint blurred. Therefore, it is found that the paper contaminated with ethanol solutions of less than 75 % (v/v) should be treated by oil red O (ORO) enhancing lipid components, and the paper contaminated with ethanol solutions of 80 % (v/v) or more should be treated by 1,2-indandione/zinc (1,2-IND/Zn) enhancing amino acid components. The blurring of ridge detail was not observed when the fingerprints were deposited with fingers contaminated with ethanol solution. This fingerprints were treated with 1,2-IND/Zn or ORO to compare the latent fingerprint development ability, and using 1,2-IND/Zn was able to visualize the latent fingerprint more clearly than using ORO.

• BMB Reports
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• 제40권4호
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• pp.517-524
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• 2007

There were many different families of zinc finger proteins that contained multiple cysteine and/or histidine residues and used zinc to stabilize their folds. The classical C2H2 zinc finger proteins were the founding members of this superfamily and were among the most abundant proteins in eukaryotic genomes. C2H2 proteins typically contained several C2H2 fingers that made tandem contacts along the DNA. Here we reported a novel C2H2 type zinc finger gene, ZNF438, which encoded 828 amino acids that formed five zinc finger domains. Bioinformatics analysis revealed that the ZNF438 was mapped to human chromosome 10p11.2 and shared 62% identity with rat and mouse homologues. RT-PCR analysis indicated that it was ubiquitously expressed in 18 human adult tissues. With immunofluorescence assay, it was shown that the exogenous Flag-tagged ZNF438 was located in nucleus of COS-7 cells. To further explore the function of ZNF438, we examined the transcriptional activity of ZNF438 protein by transfecting recombinant pM-ZNF438 into mammalian cells. The subsequent analysis based on the duel luciferase assay system showed that ZNF438 was a transcriptional repressor.

• Journal of Preventive Medicine and Public Health
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• 제26권2호
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• pp.251-267
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• 1993

연폭로의 정도와 자각증상과의 관계를 알아보기 위하여 435명의 연폭로 남자 근로자와 212명의 일반 사무직 남자 근로자를 대상으로 연폭로 지표가 되는 혈중 연, 혈중 Zinc Protoporphyrin(ZPP), 요중 Delta-aminolevulinic acid(DALA), 혈색소, 혈구 용적 측정을 위한 혈액 시료 및 소변 시료를 채취하여 분석하였고, 연관련 자각증상 조사는 14개의 증상 조사 항목을(표 3 및 별첨 1) 피검자가 응답 하도록하여 상담 의사의 면접을 통한 확인을 거쳐 수집 하였다. 수집된 각 항목은 인체 조직계 증상군별로 1) 위장관계 증상 2) 신경과 근육 및 관절계 증상 3) 일반 체질적 증상 4) 정신과적 증상으로 구분하여 연폭로 지표 수준과 연폭로 작업 여부에 따른 자각증상 호소율을 비교 조사하여 얻은 결론은 다음과 같다. 1. 연폭로군에서 대조군보다 유의하게 높은 자각증상 호소율을 보인 증상군은 신경과 근육 및 관절계 증상으로 "손이나 발이 저리거나 쥐가 잘난다", "관절이 아프거나 쑤신다", "손가락, 손, 발 등에 힘이 없다", "근육통을 느낀다" 순 이었다. 2. 연폭로군과 대조군의 자각증상 호소율에 가장 큰 차이를 보인 증상 항목은 "손이나 발이 저리거나 쥐가 잘 난다"였으며, 전체 조사 대상에서 가장 높은 증상 호소율을 보인 증상 항목은 일반 체질적 자각 증상군의 "전보다 피곤감을 느낀다"였다. 3. 전체 조사 대상의 혈중 연과 혈중 ZPP 수준에 따른 연폭로량의 증가와 자각증상 호소율의 증가를 보인 증상 항목은 신경과 근육 및 관절계 증상군의 "손이나 발이 저리거나 쥐가 잘난다", "관절이 아프거나 쑤신다", "손가락. 손 발 등에 힘이 없다", "근육통을 느낀다"와 위장관계 증상군의 "아랫배가 아파서 고생한 적이 있다"였다. 4 연폭로군에서 혈중 연과 혈중 ZPP 수준에 따른 연폭로량의 증가와 자각증상 호소율의 증가를 보인 증상 항목은 신경과 근육 및 관절계 증상으로 혈중 연의 증가에 따라 증상 호소율이 증가하였다. 5. 연폭로군에서 39세 이하 와 40세 이상 연령군으로 나누어 비교시 39세 이하 군의 증상 호소율이 40세 이상 군보다 높게 나왔으며. 신경과 근육 및 관절계 증상이 39세이하 군에서 혈중 연의 증가와 함께, 40세 이상 군에서 혈중 ZPP의 증가와 함께 자각증상 호소율의 증가를 나타냈다. 6. 연폭로 지표에 따른 폭로수준과 증상 호소율과의 관계를 알아보기 위하여 대조군에 대한 폭로군, 연폭로군의 저농도 폭로군에 대한 고농도 폭로군의 교차비를 산출한 결과 신경과 근육 및 관절계 증상군의 "손이나 발이 저리거나 쥐가 잘난다", "관절이 아프거나 쑤신다", "손가락, 손, 발 등에 힘이 없다", "근육통을 느낀다"와 위장관계 증상군의 "아랫배가 아파서 고생한 적이 있다"가 연폭로량의 증가에 따른 교차비의 증가를 보여 양-반응의 관계를 추정할 수 있었다.