Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Soichiro Kawagoe"'
Autor:
Saori Yoshimura, Ryuki Shimada, Koji Kikuchi, Soichiro Kawagoe, Hironori Abe, Sakie Iisaka, Sayoko Fujimura, Kei-ichiro Yasunaga, Shingo Usuki, Naoki Tani, Takashi Ohba, Eiji Kondoh, Tomohide Saio, Kimi Araki, Kei-ichiro Ishiguro
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-22 (2024)
Abstract Meiotic prophase progression is differently regulated in males and females. In males, pachytene transition during meiotic prophase is accompanied by robust alteration in gene expression. However, how gene expression is regulated differently
Externí odkaz:
https://doaj.org/article/6a02458e68fa47fb9b60342236eeb4b5
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 5, p 2485 (2022)
Despite recent developments in protein structure prediction, the process of the structure formation, folding, remains poorly understood. Notably, folding of multidomain proteins, which involves multiple steps of segmental folding, is one of the bigge
Externí odkaz:
https://doaj.org/article/8021590e145c40ec98eaa9c30c39602f
Publikováno v:
eLife, Vol 7 (2018)
Molecular chaperones alter the folding properties of cellular proteins via mechanisms that are not well understood. Here, we show that Trigger Factor (TF), an ATP-independent chaperone, exerts strikingly contrasting effects on the folding of non-nati
Externí odkaz:
https://doaj.org/article/280dceb6efa84fcbbf27658a7f42a616
Autor:
Soichiro Kawagoe, Munehiro Kumashiro, Takuya Mabuchi, Hiroyuki Kumeta, Koichiro Ishimori, Tomohide Saio
Publikováno v:
Biochemistry. 61:2897-2908
A transcriptional regulatory system called heat shock response (HSR) has been developed in eukaryotic cells to maintain proteome homeostasis under various stresses. Heat shock factor-1 (Hsf1) plays a central role in HSR, mainly by upregulating molecu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0e78bce81de03b673efd90092cbbc93
https://doi.org/10.1021/acs.biochem.2c00492
https://doi.org/10.1021/acs.biochem.2c00492
Publikováno v:
Thermal Medicine. 37:31-44
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8989a7da2701ea21246f2a6b9d4a1f3c
https://doi.org/10.3191/thermalmed.37.31
https://doi.org/10.3191/thermalmed.37.31
Autor:
Shuhei Yoshida, Shota Uehara, Noriyasu Kondo, Yu Takahashi, Shiho Yamamoto, Atsushi Kameda, Soichiro Kawagoe, Naoko Inoue, Masami Yamada, Norito Yoshimura, Yuki Tachibana
Publikováno v:
Journal of medicinal chemistry. 65(15)
Recent technological innovations have led to the development of methods for the rapid identification of high-affinity macrocyclic peptides for a wide range of targets; however, it is still challenging to achieve the desired activity and membrane perm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dba652531dfa6662aa6e199d8127f390
https://pubmed.ncbi.nlm.nih.gov/35904556
https://pubmed.ncbi.nlm.nih.gov/35904556
Heat shock factor 1 (Hsf1) was found as a central upregulator of molecular chaperones in stress adaptation, but it has recently been rediscovered as a major component of persistent nuclear stress bodies (nSBs). When the persistently stressed cells un
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07dcccc1e2a3f154d6d266781a16ba47
https://doi.org/10.1101/2021.12.02.471034
https://doi.org/10.1101/2021.12.02.471034
Publikováno v:
The Journal of Biological Chemistry
Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as a disulfide bridges and peptidyl–prolyl bonds in cis form, in the client protein. A ribosome-associated m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1b14ffa7d2ad047bd89f1bbbe06c32cf
https://pubmed.ncbi.nlm.nih.gov/30093407
https://pubmed.ncbi.nlm.nih.gov/30093407