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Akademický článek

V-ATPase V0a1 promotes Weibel–Palade body biogenesis through the regulation of membrane fission

Autor: Yasuo Yamazaki, Yuka Eura, Koichi Kokame

Publikováno v: eLife, Vol 10 (2021)

Membrane fission, the division of a membrane-bound structure into two discrete compartments, is essential for diverse cellular events, such as endocytosis and vesicle/granule biogenesis; however, the process remains unclear. The hemostatic protein vo

Externí odkaz: https://doaj.org/article/de5a409f66384711870d8dfbe0a26836

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Akademický článek

Arf GTPase-activating proteins SMAP1 and AGFG2 regulate the size of Weibel-Palade bodies and exocytosis of von Willebrand factor

Autor: Asano Watanabe, Hikari Hataida, Naoya Inoue, Kosuke Kamon, Keigo Baba, Kuniaki Sasaki, Rika Kimura, Honoka Sasaki, Yuka Eura, Wei-Fen Ni, Yuji Shibasaki, Satoshi Waguri, Koichi Kokame, Yoko Shiba

Publikováno v: Biology Open, Vol 10, Iss 9 (2021)

Arf GTPase-Activating proteins (ArfGAPs) mediate the hydrolysis of GTP bound to ADP-ribosylation factors (Arfs), which are critical to form transport intermediates. ArfGAPs have been thought to be negative regulators of Arfs; however, accumulating ev

Externí odkaz: https://doaj.org/article/37c4573f900a4b4b9c4c349226fa51b5

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Akademický článek

Commonly used anti–von Willebrand factor antibody for multimer analysis cross‐reacts with fibronectin, which is difficult to distinguish from von Willebrand factor

Autor: Yuka Eura, Koichi Kokame

Publikováno v: Research and Practice in Thrombosis and Haemostasis, Vol 5, Iss 6, Pp n/a-n/a (2021)

Abstract Von Willebrand factor (VWF) is a 500‐ to 15 000‐kDa multimeric protein circulating in the blood. When VWF has a higher molecular weight, its hemostatic activity is greater. The size distribution of VWF multimers is usually analyzed by SD

Externí odkaz: https://doaj.org/article/4c0a28ebea714f6c90ab12a6b024e93c

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Akademický článek

Derlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in mice.

Autor: Yuka Eura, Hiroji Yanamoto, Yuji Arai, Tomohiko Okuda, Toshiyuki Miyata, Koichi Kokame

Publikováno v: PLoS ONE, Vol 7, Iss 3, p e34298 (2012)

Accumulation of unfolded or misfolded proteins in the endoplasmic reticulum (ER) causes a cellular condition called ER stress. To overcome ER stress, unfolded proteins are eliminated by an ER-associated degradation (ERAD) system. To explore the physi

Externí odkaz: https://doaj.org/article/33e7377376e14a0081e16765701989d8

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Siglec-5 and Siglec-14 mediate the endocytosis of ADAMTS13

Autor: Masashi Akiyama, Yuka Eura, Koichi Kokame

Publikováno v: Thrombosis Research. 219:49-59

The plasma metalloprotease ADAMTS13 regulates the thrombotic activity of the von Willebrand factor (VWF). ADAMTS13 is highly glycosylated and its carbohydrate chains are capped with sialic acid (SA). Thus, ADAMTS13 may interact with carbohydrate- and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbcd635d2354c47f3a86270629b07043
https://doi.org/10.1016/j.thromres.2022.09.005

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