Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Arisa, Murakami"'
Autor:
Taichi Kumanomidou, Kazuya Nishio, Kenji Takagi, Tomomi Nakagawa, Atsuo Suzuki, Takashi Yamane, Fuminori Tokunaga, Kazuhiro Iwai, Arisa Murakami, Yukiko Yoshida, Keiji Tanaka, Tsunehiro Mizushima
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0140366 (2015)
The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among thes
Externí odkaz:
https://doaj.org/article/ad4c2d6bf8a241b0a65ef102661646e9
Autor:
Yukiko, Yoshida, Makoto, Asahina, Arisa, Murakami, Junko, Kawawaki, Meari, Yoshida, Reiko, Fujinawa, Kazuhiro, Iwai, Ryuichi, Tozawa, Noriyuki, Matsuda, Keiji, Tanaka, Tadashi, Suzuki
Publikováno v:
Proc Natl Acad Sci U S A
Mutations in the human peptide:N-glycanase gene (NGLY1), which encodes a cytosolic de–N-glycosylating enzyme, cause a congenital autosomal recessive disorder. In rodents, the loss of Ngly1 results in severe developmental delay or lethality, but the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f99856f479a40fe48f3db6cbf1379944
https://pubmed.ncbi.nlm.nih.gov/34215698
https://pubmed.ncbi.nlm.nih.gov/34215698
Autor:
Arisa Murakami, Tadashi Suzuki, Noriyuki Matsuda, Kazuhiro Iwai, Reiko Fujinawa, Yukiko Yoshida, Keiji Tanaka, Ryuichi Tozawa, Makoto Asahina, Meari Yoshida, Junko Kawawaki
Publikováno v:
Proceedings of the National Academy of Sciences. 118
Significance Cytosolic peptide: N -glycanase (NGLY1) is a widely conserved enzyme involved in de– N -glycosylation of N -glycosylated proteins. Mutations in the human NGLY1 gene cause global developmental delay and multisystemic symptoms, but the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::adf03503537a194f00f5f1f2207ff077
https://doi.org/10.1073/pnas.2102902118
https://doi.org/10.1073/pnas.2102902118
Autor:
Sayaka Yasuda, Toshiharu Fujita, Keiji Tanaka, Yukiko Yoshida, Yasushi Saeki, Maho Hamasaki, Tamotsu Yoshimori, Arisa Murakami, Junko Kawawaki, Noriyuki Matsuda, Kazuhiro Iwai
Publikováno v:
Proceedings of the National Academy of Sciences. 114:8574-8579
Ubiquitination functions as a signal to recruit autophagic machinery to damaged organelles and induce their clearance. Here, we report the characterization of FBXO27, a glycoprotein-specific F-box protein that is part of the SCF (SKP1/CUL1/F-box prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::acda550eee957f0b268415e28075c790
https://doi.org/10.1073/pnas.1702615114
https://doi.org/10.1073/pnas.1702615114
Autor:
Yukiko Yoshida, Makoto Asahina, Arisa Murakami, Junko Kawawaki, Meari Yoshida, Reiko Fujinawa, Kazuhiro Iwai, Ryuichi Tozawa, Noriyuki Matsuda, Keiji Tanaka, Tadashi Suzuki
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America; 7/6/2021, Vol. 118 Issue 27, p1-9, 9p
Autor:
Yukiko, Yoshida, Sayaka, Yasuda, Toshiharu, Fujita, Maho, Hamasaki, Arisa, Murakami, Junko, Kawawaki, Kazuhiro, Iwai, Yasushi, Saeki, Tamotsu, Yoshimori, Noriyuki, Matsuda, Keiji, Tanaka
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(32)
Although lysosomes play a crucial role in autophagy, damaged lysosomes are eliminated by autophagy. The molecular mechanisms that recognize lysosomal damage in cells remain poorly understood, but ubiquitination is a known prerequisite for directing a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a5b041c2dd6869a6872bfcc1ade12dbe
https://pubmed.ncbi.nlm.nih.gov/28743755
https://pubmed.ncbi.nlm.nih.gov/28743755
Autor:
Arisa Murakami, Hikaru Tsuchiya, Yukiko Yoshida, Yasushi Saeki, Mayumi Shindo, Keiji Tanaka, Hidehito Yoshihara, Junko Kawawaki
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 112(15)
The identification of substrates for ubiquitin ligases has remained challenging, because most substrates are either immediately degraded by the proteasome or processed by deubiquitinating enzymes (DUBs) to remove polyubiquitin. Although a methodology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a106de35e7b2f72163ab4c2f67a1c2e
https://pubmed.ncbi.nlm.nih.gov/25827227
https://pubmed.ncbi.nlm.nih.gov/25827227
Autor:
Fuminori Tokunaga, Atsuo Suzuki, Kazuhiro Iwai, Arisa Murakami, Kenji Takagi, Taichi Kumanomidou, Takashi Yamane, Keiji Tanaka, Tsunehiro Mizushima, Yukiko Yoshida, Kazuya Nishio, Tomomi Nakagawa
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0140366 (2015)
PLoS ONE
PLoS ONE
The Skp1-Cul1-F-box protein (SCF) complex catalyzes protein ubiquitination in diverse cellular processes and is one of the best-characterized ubiquitin ligases. F-box proteins determine the substrate specificities of SCF ubiquitin ligases. Among thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c8e4f055d97ae278ed32fb800187d89
http://europepmc.org/articles/PMC4603797?pdf=render
http://europepmc.org/articles/PMC4603797?pdf=render
Autor:
Yuka Nakamura, Hideyo Yamaguchi, Rui Kano, Katsuhisa Uchida, Koichi Makimura, Yoshiko Tamura, Arisa Murakami, Atsuhiko Hasegawa
Publikováno v:
Microbiology and Immunology. 45:209-216
We performed a cluster analysis of human and animal pathogenic Microsporum species and their teleomorphic states, Arthroderma species, including A. otae-related species (M. canis, M. audouinii, M. distortum, M. equinum, M. langeronii, and M. ferrugin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2426f2e1f67c9f3b346fbce98ce6794d
https://doi.org/10.1111/j.1348-0421.2001.tb02609.x
https://doi.org/10.1111/j.1348-0421.2001.tb02609.x
Publikováno v:
Biochemical and biophysical research communications. 410(1)
The SCF ubiquitin ligase complex consists of four components, Skp1, Cul1, ROC1/Rbx1, and a variable subunit F-box protein, which serves as a receptor for target proteins. The F-box proteins consist of an N-terminal ∼40 amino acid F-box domain that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb6eaacc7827bcaeb74fe43b476b623d
https://pubmed.ncbi.nlm.nih.gov/21640084
https://pubmed.ncbi.nlm.nih.gov/21640084