Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Aya Masaoka"'
Autor:
Aya Masaoka, Natalie R Gassman, Julie K Horton, Padmini S Kedar, Kristine L Witt, Cheryl A Hobbs, Grace E Kissling, Keizo Tano, Kenjiro Asagoshi, Samuel H Wilson
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e66801 (2013)
The breast cancer 1 (BRCA1) protein is a tumor suppressor playing roles in DNA repair and cell cycle regulation. Studies of DNA repair functions of BRCA1 have focused on double-strand break (DSB) repair pathways and have recently included base excisi
Externí odkaz:
https://doaj.org/article/8c8ec1591f79421093a6465237cd408a
Autor:
Akira Fujimori, Jac A. Nickoloff, Shigeaki Sunada, Huizi Keiko Li, Younghyun Lee, Hirokazu Hirakawa, Aya Masaoka, Ryuichi Okayasu
Publikováno v:
Radiotherapy and Oncology. 121:162-168
Background and purpose PU-H71 is a purine-scaffold Hsp90 inhibitor developed to overcome limitations of conventional Hsp90 inhibitors. This study was designed to investigate the combined effect of PU-H71 and heavy ion irradiation on human tumor and n
Autor:
Ryuichi Okayasu, Akira Fujimori, Hirokazu Hirakawa, Hiroshi Fujisawa, Aya Masaoka, Ryoichi Hirayama, Miho Noguchi, Momoko Takahashi
Publikováno v:
Cancer Medicine
Hsp90 inhibitors have become well-studied antitumor agents for their selective property against tumors versus normal cells. The combined treatment of Hsp90 inhibitor and conventional photon radiation also showed more effective tumor growth delay than
Autor:
Samuel H. Wilson, Aya Masaoka, Natalie R. Gassman, Julie K. Horton, Padmini S. Kedar, Esther W. Hou, Michael Bustin, Rajendra Prasad
Publikováno v:
Journal of Biological Chemistry. 287:27648-27658
In mammalian cells, the nucleosome-binding protein HMGN1 (high mobility group N1) affects the structure and function of chromatin and plays a role in repair of damaged DNA. HMGN1 affects the interaction of DNA repair factors with chromatin and their
Publikováno v:
DNA Repair. 8:1290-1299
To examine base excision repair (BER) capacity in the context of living cells, we developed and applied a plasmid-based reporter assay. Non-replicating plasmids containing unique DNA base lesions were designed to express luciferase only after lesion
Autor:
Atsushi Katafuchi, Toshiaki Nakano, Hiroshi Ide, Fumio Hanaoka, Aya Masaoka, Shigenori Iwai, Hiroaki Terato
Publikováno v:
Journal of Biological Chemistry. 279:14464-14471
In human cells, oxidative pyrimidine lesions are restored by the base excision repair pathway initiated by homologues of Endo III (hNTH1) and Endo VIII (hNEIL1 and hNEIL2). In this study we have quantitatively analyzed and compared their activity tow
Autor:
Mayumi Matsubara, Rei Hasegawa, Aya Masaoka, Hiroshi Ide, Hiroaki Terato, and Akira Matsuda, Yoshihiko Ohyama, Tamon Tanaka, Naoko Karino, Satofumi Kurisu
Publikováno v:
Biochemistry. 42:5003-5012
In the accompanying paper [Matsubara, M., et al. (2003) Biochemistry 42, 4993-5002], we have partially purified and characterized rat 5-formyluracil (fU)-DNA glycosylase (FDG). Several lines of evidence have indicated that FDG is a rat homologue of s
Autor:
Takayuki Miyano, Hiroshi Ide, Yoshihiko Ohyama, Nagisa Kato, Tamon Tanaka, Shigenori Iwai, Hiroaki Terato, Mayumi Matsubara, Aya Masaoka
Publikováno v:
Biochemistry. 42:4993-5002
5-Formyluracil (fU) is a major oxidative thymine lesion produced by reactive oxygen species and exhibits genotoxic and cytotoxic effects via several mechanisms. In the present study, we have searched for and characterized mammalian fU-DNA glycosylase
Publikováno v:
Journal of Biological Chemistry. 276:16501-16510
5-Formyluracil (fU) is a major oxidative thymine lesion generated by ionizing radiation and reactive oxygen species. In the present study, we have assessed the influence of fU on DNA replication to elucidate its genotoxic potential. Oligonucleotide t
Publikováno v:
Journal of Biological Chemistry. 274:25136-25143
5-Formyluracil (fU) is a major thymine lesion produced by reactive oxygen radicals and photosensitized oxidation. We have previously shown that fU is a potentially mutagenic lesion due to its elevated frequency to mispair with guanine. Therefore, fU