Time filter

Source Type

Incheon, South Korea

Han S.H.,Konkuk University | Hahm S.-H.,Konkuk University | Tran A.H.V.,Konkuk University | Park J.W.,DKC Corporation | And 3 more authors.
Bulletin of the Korean Chemical Society | Year: 2015

Detection and quantification of 8-oxo-7,8-dihydroguanine (8-oxoG) within cells are important for the study of the molecular mechanisms in cancer. Human ribosomal protein S3 (hRpS3), which involved in DNA repair, has high binding affinity to 8-oxoG. We developed an imaging probe to detect 8-oxoG using a specific peptide of hRpS3. Sequence analysis was conducted to elucidate the 8-oxoG-specific binding region of hRpS3, and three truncated mutants, D1 (amino acids 1-85), D2 (amino acids 86-159), and D3 (amino acids 160-242), were constructed. Both wild-type-hRpS3 and D2 were able to bind 8-oxoG, which is consistent with the results of a previous report on the role of K134 in Drosophila melanogaster RpS3. We synthesized a specific peptide and covalently linked with a fluorophore (FPR-552, similar to Cy3) to generate an 8-oxoG imaging probe. Our 8-oxoG S3-probe successfully detected the presence of 8-oxoG in damaged cells. Furthermore, this probe has threefold higher sensitivity than 8-oxoG DNA lesion antibody. © 2015 Korean Chemical Society, Seoul & Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

The present disclosure relates to a novel benzindocyanine compound for labeling biomolecules and a method for preparing the same.

Dkc Llc. | Date: 2016-04-07

Belts; Hats; Sweatshirts; T-shirts. Retail store services featuring apparel and branded merchandise.

Huang X.,U.S. National Institutes of Health | Swierczewska M.,U.S. National Institutes of Health | Swierczewska M.,State University of New York at Stony Brook | Choi K.Y.,U.S. National Institutes of Health | And 9 more authors.
Angewandte Chemie - International Edition | Year: 2012

Turn off the lights! A universal nanoquencher that quenches a broad range of visible to near-infrared dyes by using a series of dark quenchers incorporated into a cell-permeable mesoporous silica nanoparticle has been developed. In combination with dye-labeled substrates, this nanoquencher boosts multiple fluorescence signals upon specific proteolysis, which allows real-time imaging of proteolytic cascades (see scheme). Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Agustina L.,Konkuk University | Hahm S.-H.,Konkuk University | Han S.H.,Konkuk University | Tran A.H.V.,Konkuk University | And 4 more authors.
BMC Molecular Biology | Year: 2014

Background: Human MutY glycosylase homolog (hMYH), a component of the base excision repair pathway, is responsible for the generation of apurinic/apyrimidinic sites. Rad9-Rad1-Hus1 (9-1-1) is a heterotrimeric protein complex that plays a role in cell cycle checkpoint control and DNA repair. In humans, hMYH and 9-1-1 interact through Hus1 and to a lesser degree with Rad1 in the presence of DNA damage. In Saccharomyces pombe, each component of the 9-1-1 complex interacts directly with SpMYH. The glycosylase activity of hMYH is stimulated by Hus1 and the 9-1-1 complex and enhanced by DNA damage treatment. Cells respond to different stress conditions in different manners. Therefore, we investigated whether Rad9 interacted with hMYH under different stresses. Here, we identified and visualized the interaction between hRad9 and hMYH and investigated the functional consequences of this interaction.Results: Co-IP and BiFC indicates that hMYH interacts with hRad9. As shown by GST-pull down assay, this interaction is direct. Furthermore, BiFC with deletion mutants of hMYH showed that hRad9 interacts with N-terminal region of hMYH. The interaction was enhanced by hydroxyurea (HU) treatment. mRNA and protein levels of hMYH and hRad9 were increased following HU treatment. A marked increase in p-Chk1 (S345) and p-Cdk2 (T14, Y15) was observed. But this phosphorylation decreased in siMYH- or siRad9-transfected cells, and more pronounced decrease observed in co-transfected cells.Conclusions: Our data reveal that hRad9 interacts directly with N-terminal region of hMYH. This interaction is enhanced by HU treatment. Knockdown of one or both protein result in decreasing Chk1 and Cdk2 phosphorylation. Since both protein functions in the early detection of DNA damage, we suggest that this interaction occurs early in DNA damage pathway. © 2014 Agustina et al.; licensee BioMed Central Ltd.

Discover hidden collaborations