Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Youichi Naoe"'
Autor:
Eriya Kenjo, Hiroyuki Hozumi, Yukimasa Makita, Kumiko A. Iwabuchi, Naoko Fujimoto, Satoru Matsumoto, Maya Kimura, Yuichiro Amano, Masataka Ifuku, Youichi Naoe, Naoto Inukai, Akitsu Hotta
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
In vivo delivery of CRISPR-Cas9 holds promise for treating muscular dystrophy, however, AAV delivery is known to be immunogenic. Here, the authors show that LNP delivery of CRISPR-Cas9 enables repeated injections into skeletal muscle and leads to res
Externí odkaz:
https://doaj.org/article/82ba1424688643b8923145dd7be8e610
Autor:
Youichi Naoe, Nozomi Nakamura, Akihiro Doi, Mia Sawabe, Hiro Nakamura, Yoshitsugu Shiro, Hiroshi Sugimoto
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Pathogenic bacteria acquire iron from heme cofactors imported by ABC heme transporters. Here the authors present crystal structures of Burkholderia cenocepaciaheme importer BhuUV with and without the heme-binding protein BhuT, gathering mechanistic i
Externí odkaz:
https://doaj.org/article/7ca204fe49ee4f9494486ae36341efae
Autor:
Nozomi Nakamura, Yoshitsugu Shiro, Kouhei Tsumoto, Youichi Naoe, Takehiko Tosha, Md. Mahfuzur Rahman, Hiroshi Sugimoto, Satoru Nagatoishi
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:2217-2230
Periplasmic heme-binding proteins (PBPs) in Gram-negative bacteria are components of the heme acquisition system. These proteins shuttle heme across the periplasmic space from outer membrane receptors to ATP-binding cassette (ABC) heme importers loca
Autor:
Hiro Nakamura, Akihiro Doi, Mia Sawabe, Nozomi Nakamura, Hiroshi Sugimoto, Yoshitsugu Shiro, Youichi Naoe
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Communications
Nature Communications
Pathogenic bacteria remove iron from the haem of host tissues and use it as a catalytic center of many enzymes. Haem uptake by pathogenic bacteria is facilitated by the membrane-integrated haem importer, which belongs to the type II ATP-binding casse
Autor:
Miyako Ueguchi-Tanaka, Ko Hirano, Youichi Naoe, Hiroaki Kato, Rie Mitani, Makoto Matsuoka, Sayaka Takehara, Tomomi Sato, Yohei Miyanoiri, Mitsuhiro Takeda, Masatsune Kainosho
Publikováno v:
Protein Expression and Purification. 95:248-258
GRAS proteins belong to a plant specific protein family that participates in diverse and important functions in growth and development. GRAS proteins are typically composed of a variable N-terminal domain and highly conserved C-terminal GRAS domain.
Autor:
Makoto Matsuoka, Miyako Ueguchi-Tanaka, Youichi Naoe, Hiroaki Kato, Hiroko Ohmiya, Toru Nakatsu, Masatoshi Nakajima, Asako Shimada
Publikováno v:
Nature. 456:520-523
Gibberellins (GAs) are phytohormones essential for many developmental processes in plants. A nuclear GA receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), has a primary structure similar to that of the hormone-sensitive lipases (HSLs). Here we analyse
Autor:
Hiroshi Kanazawa, Mamoru Sato, Kyouhei Arita, Youichi Naoe, Toshiyuki Shimizu, Hiroshi Hashimoto
Publikováno v:
The Journal of biological chemistry. 280(37)
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding EF-hand protein that plays a role in membrane trafficking. It binds to multiple effector proteins, including Na(+)/H(+) exchangers, a serine/threonine kinase, and calc
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 70:C1500-C1500
Iron is an essential element for almost all organisms, since iron serves as a catalytic center for redox reactions in many enzymes. Bacterial pathogens need to acquire iron from tissues of host to survive. Heme transport by ATP-binding cassette (ABC)
Autor:
Mamoru Sato, Kyouhei Arita, Youichi Naoe, Toshiyuki Shimizu, Hiroshi Kanazawa, Hiroshi Hashimoto
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61:612-613
Calcineurin B homologous protein 1 (CHP1), also known as p22, is a calcium-binding protein that plays a role in membrane trafficking and binds to multiple effector proteins, including Na+/H+ exchangers, serine/threonine protein kinase and calcineurin
Autor:
Naoe, Youichi, Nakamura, Nozomi, Rahman, Md. Mahfuzur, Tosha, Takehiko, Nagatoishi, Satoru, Tsumoto, Kouhei, Shiro, Yoshitsugu, Sugimoto, Hiroshi
Publikováno v:
Proteins; Dec2017, Vol. 85 Issue 12, p2217-2230, 14p