Search

Your search keyword '"Araki, Shinsuke"' showing total 30 results
Start Over Author "Araki, Shinsuke"
30 results on '"Araki, Shinsuke"'

12. Identification of a selective DDX3X inhibitor with newly developed quantitative high-throughput RNA helicase assays

Author

Nakao, Shoichi, primary, Nogami, Masahiro, additional, Iwatani, Misa, additional, Imaeda, Toshihiro, additional, Ito, Masahiro, additional, Tanaka, Toshio, additional, Tawada, Michiko, additional, Endo, Satoshi, additional, Cary, Douglas R., additional, Ohori, Momoko, additional, Imaeda, Yasuhiro, additional, Kawamoto, Tomohiro, additional, Aparicio, Samuel, additional, Nakanishi, Atsushi, additional, and Araki, Shinsuke, additional

Published
2020
Full Text
View/download PDF

14. Discovery of 3-Benzyl-1-(trans-4-((5-cyanopyridin-2-yl)amino)cyclohexyl)-1-arylurea Derivatives as Novel and Selective Cyclin-Dependent Kinase 12 (CDK12) Inhibitors

Author

Ito, Masahiro, primary, Tanaka, Toshio, additional, Toita, Akinori, additional, Uchiyama, Noriko, additional, Kokubo, Hironori, additional, Morishita, Nao, additional, Klein, Michael G., additional, Zou, Hua, additional, Murakami, Morio, additional, Kondo, Mitsuyo, additional, Sameshima, Tomoya, additional, Araki, Shinsuke, additional, Endo, Satoshi, additional, Kawamoto, Tomohiro, additional, Morin, Gregg B., additional, Aparicio, Samuel A., additional, Nakanishi, Atsushi, additional, Maezaki, Hironobu, additional, and Imaeda, Yasuhiro, additional

Published
2018
Full Text
View/download PDF

17. CLK-dependent exon recognition and conjoined gene formation revealed with a novel small molecule inhibitor

Author

Funnell, Tyler, primary, Tasaki, Shinya, additional, Oloumi, Arusha, additional, Araki, Shinsuke, additional, Kong, Esther, additional, Yap, Damian, additional, Nakayama, Yusuke, additional, Hughes, Christopher S., additional, Cheng, S.-W. Grace, additional, Tozaki, Hirokazu, additional, Iwatani, Misa, additional, Sasaki, Satoshi, additional, Ohashi, Tomohiro, additional, Miyazaki, Tohru, additional, Morishita, Nao, additional, Morishita, Daisuke, additional, Ogasawara-Shimizu, Mari, additional, Ohori, Momoko, additional, Nakao, Shoichi, additional, Karashima, Masatoshi, additional, Sano, Masaya, additional, Murai, Aiko, additional, Nomura, Toshiyuki, additional, Uchiyama, Noriko, additional, Kawamoto, Tomohiro, additional, Hara, Ryujiro, additional, Nakanishi, Osamu, additional, Shumansky, Karey, additional, Rosner, Jamie, additional, Wan, Adrian, additional, McKinney, Steven, additional, Morin, Gregg B., additional, Nakanishi, Atsushi, additional, Shah, Sohrab, additional, Toyoshiba, Hiroyoshi, additional, and Aparicio, Samuel, additional

Published
2017
Full Text
View/download PDF

27. The RNA helicase DDX39B and its paralog DDX39A regulate androgen receptor splice variant AR-V7 generation.

Author

Nakata, Daisuke, Nakao, Shoichi, Nakayama, Kazuhide, Araki, Shinsuke, Nakayama, Yusuke, Aparicio, Samuel, Hara, Takahito, and Nakanishi, Atsushi

Subjects
*RNA helicase, *ANDROGEN receptors, *PROSTATE cancer treatment, *XENOGRAFTS, *PROTEIN expression
Abstract

Mounting evidence suggests that constitutively active androgen receptor (AR) splice variants, typified by AR-V7, are associated with poor prognosis and resistance to androgen deprivation therapy in prostate cancer patients. However, mechanisms governing the generation of AR splice variants are not fully understood. In this study, we aimed to investigate the dynamics of AR splice variant generation using the JDCaP prostate cancer model that expresses AR splice variants under androgen depletion. Microarray analysis of JDCaP xenografts before and after expression of AR splice variants suggested that dysregulation of RNA processing pathways is likely involved in AR splice variant generation. To explore factors contributing to generation of AR-V7 mRNA, we conducted a focused RNA interference screen in AR-V7-positive JDCaP-hr cells using an shRNA library targeting spliceosome-related genes. This screen identified DDX39B as a regulator of AR-V7 mRNA expression. Simultaneous knockdown of DDX39B and its paralog DDX39A drastically and selectively downregulated AR-V7 mRNA expression in multiple AR-V7-positive prostate cancer cell lines. DDX39B was upregulated in relapsed JDCaP xenografts expressing AR splice variants, suggesting its role in expression of AR splice variants. Taken together, our findings offer insight into the mechanisms of AR splice variant generation and identify DDX39 as a potential drug target for the treatment of AR splice variant-positive prostate cancer. [ABSTRACT FROM AUTHOR]

Published
2017
Full Text
View/download PDF

28. Possible contribution of DNase gamma to immunoglobulin V gene diversification.

Author

Okamoto N, Okamoto M, Araki S, Arakawa H, Mizuta R, and Kitamura D

Subjects
Animals, B-Lymphocytes metabolism, Cell Line, Chickens, DNA immunology, DNA metabolism, DNA Breaks, Double-Stranded, Endodeoxyribonucleases genetics, Mutation, B-Lymphocytes immunology, Endodeoxyribonucleases metabolism, Genes, Immunoglobulin, Immunoglobulin Variable Region genetics, Somatic Hypermutation, Immunoglobulin
Abstract

Somatic hypermutation (SHM) diversifies the rearranged immunoglobulin variable (V) region gene in B cells, contributing to affinity maturation of antibodies. It is believed that SHM is generated either by direct replication or by error-prone repair systems resolving V region DNA lesions caused directly or indirectly by cytidine deaminase AID. In accord with a part of these mechanisms, it was reported that SHM is associated with staggered double-strand DNA breaks (DSBs) occurring in the rearranged V regions. However, endonucleases responsible for the DSBs remain elusive. Here we show that DNase gamma, a member of DNase I family endonucleases, contributes to the generation of SHM including point mutation, and nucleotide insertion and deletion in chicken DT40 B cell line. DNase gamma also contributes to the generation of staggered DSBs in the rearranged V region. These results raise a possibility that DNase gamma is involved in the V gene mutation machinery.

Published
2009
Full Text
View/download PDF

29. DNase gamma-dependent and -independent apoptotic DNA fragmentations in Ramos Burkitt's lymphoma cell line.

Author

Mizuta R, Mizuta M, Araki S, Suzuki K, Ebara S, Furukawa Y, Shiokawa D, Tanuma S, and Kitamura D

Subjects
Burkitt Lymphoma pathology, Cell Nucleus metabolism, Deoxyribonucleases genetics, Deoxyribonucleases metabolism, Endodeoxyribonucleases genetics, Enzyme Inhibitors metabolism, Humans, Poly-ADP-Ribose Binding Proteins, Staurosporine metabolism, Apoptosis physiology, Burkitt Lymphoma genetics, Cell Line, Tumor, DNA Fragmentation, Endodeoxyribonucleases metabolism
Abstract

DNA fragmentation is a biochemical hallmark of apoptosis. Several endonucleases, including CAD/DFF40 and endonuclease G, are implicated in DNA fragmentation. DNase gamma has also been considered to be one of the enzymes involved, but its role in relation to CAD/DFF40 in apoptosis has not been fully elucidated. Here, we distinguished between DNase gamma-dependent and CAD/DFF40-dependent DNA fragmentations. We found that DNase gamma activities appeared in the late apoptotic phase and accelerated DNA fragmentation. Thus, even if the apoptotic DNA fragmentation is initiated by CAD/DFF40, DNase gamma is required for the more complete digestion of the genomic DNA in dying cells.

Published
2009
Full Text
View/download PDF

30. Action of apoptotic endonuclease DNase gamma on naked DNA and chromatin substrates.

Author

Mizuta R, Mizuta M, Araki S, Shiokawa D, Tanuma S, and Kitamura D

Subjects
Apoptosis physiology, Base Sequence, Cell Line, Tumor, DNA, Single-Stranded metabolism, Deoxyribonuclease I metabolism, Histones metabolism, Histones pharmacology, Humans, Molecular Sequence Data, Osmolar Concentration, Substrate Specificity, Chromatin metabolism, DNA metabolism, Endodeoxyribonucleases metabolism
Abstract

The internucleosomal cleavage of genomic DNA is a biochemical hallmark of apoptosis. DNase gamma, a Mg2+/Ca2+-dependent endonuclease, has been suggested to be one of the apoptotic endonucleases, but its biochemical characteristic has not been fully elucidated. Here, using recombinant DNase gamma, we showed that DNase gamma is a Mg2+/Ca2+-dependent single-stranded DNA nickase and has a high activity at low ionic strength. Under higher ionic strength, such as physiological buffer conditions, the endonuclease activity of DNase gamma is restricted, but its activity is enhanced in the presence of linker histone H1, which explains DNA cleavage at linker regions of apoptotic nuclei.

Published
2006
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results