Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Yuki Ishiwata-Kimata"'
Autor:
Yuki Ishiwata-Kimata, Yukio Kimata
Publikováno v:
Journal of Fungi, Vol 9, Iss 10, p 989 (2023)
Upon the dysfunction or functional shortage of the endoplasmic reticulum (ER), namely, ER stress, eukaryotic cells commonly provoke a protective gene expression program called the unfolded protein response (UPR). The molecular mechanism of UPR has be
Externí odkaz:
https://doaj.org/article/a20198e89da6460e92fd12e433fe6b88
Autor:
Huong Thi Phuong, Yuki Ishiwata-Kimata, Yuki Nishi, Norie Oguchi, Hiroshi Takagi, Stefan Pukatzki
Publikováno v:
Microbial Cell, Vol 8, Iss 4, Pp 77-86 (2021)
Saccharomyces cerevisiae is a facultative anaerobic organism that grows well under both aerobic and hypoxic conditions in media containing abundant fermentable nutrients such as glucose. In order to deeply understand the physiological dependence of S
Externí odkaz:
https://doaj.org/article/3bad8fe3dc2244f8826859be8a043025
Autor:
Quynh Giang Le, Yuki Ishiwata-Kimata, Thi Huong Phuong, Shigeto Fukunaka, Kenji Kohno, Yukio Kimata
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
Abstract Upon endoplasmic-reticulum (ER) stress, the ER-located transmembrane protein, Ire1, is autophosphorylated and acts as an endoribonuclease to trigger the unfolded protein response (UPR). Previous biochemical studies have shown that Ire1 exhib
Externí odkaz:
https://doaj.org/article/244f0bfeceb04e76b0aedb99335c2c9a
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 9 (2022)
Phosphatidylcholine (PC) is produced via two distinct pathways in both hepatocytes and yeast, Saccharomyces cerevisiae. One of these pathways involves the sequential methylation of phosphatidylethanolamine (PE). In yeast cells, the methyltransferase,
Externí odkaz:
https://doaj.org/article/d3940a52076f4ce2b779fb2a03226529
Publikováno v:
Biochemical and Biophysical Research Communications. 667:58-63
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 86:739-746
Upon endoplasmic reticulum (ER) stress, eukaryotic cells commonly induce unfolded protein response (UPR), which is triggered, at least partly, by the ER stress sensor Ire1. Upon ER stress, Ire1 is dimerized or forms oligomeric clusters, resulting in
Publikováno v:
Appl Environ Microbiol
In Saccharomyces cerevisiae cells, dysfunction of the endoplasmic reticulum (ER), so-called ER stress, leads to conversion of HAC1 mRNA to the spliced form (HAC1i), which is translated into a transcription factor that drastically changes the gene exp
Autor:
Yuki Ishiwata-Kimata, Yukio Kimata, Huong Thi Phuong, Hiroshi Takagi, Norie Oguchi, Yuki Nishi
Publikováno v:
Microbial Cell
Microbial Cell, Vol 8, Iss 4, Pp 77-86 (2021)
Microbial Cell, Vol 8, Iss 4, Pp 77-86 (2021)
Saccharomyces cerevisiae is a facultative anaerobic organism that grows well under both aerobic and hypoxic conditions in media containing abundant fermentable nutrients such as glucose. In order to deeply understand the physiological dependence of S
Autor:
Yukio Kimata, Yuki Ishiwata-Kimata
Publikováno v:
KAGAKU TO SEIBUTSU. 58:404-410
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1669
International Journal of Molecular Sciences, Vol 23, Iss 1669, p 1669 (2022)
International Journal of Molecular Sciences, Vol 23, Iss 1669, p 1669 (2022)
Ire1 is an endoplasmic reticulum (ER)-located endoribonuclease that is activated in response to ER stress. In yeast Saccharomyces cerevisiae cells, Ire1 promotes HAC1-mRNA splicing to remove the intron sequence from the HAC1u mRNA (“u” stands for