Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Hajime Niwa"'
Publikováno v:
Biology Open, Vol 4, Iss 6, Pp 710-721 (2015)
Pex11p family proteins are key players in peroxisomal fission, but their molecular mechanisms remains mostly unknown. In the present study, overexpression of Pex11pβ caused substantial vesiculation of peroxisomes in mammalian cells. This vesicle for
Externí odkaz:
https://doaj.org/article/ebf4d3509d944358a65272b80f2bf903
Autor:
Heidi O. Yeung, Andreas Förster, Cecilia Bebeacua, Hajime Niwa, Caroline Ewens, Ciarán McKeown, Xiaodong Zhang, Paul S. Freemont
Publikováno v:
Open Biology, Vol 4, Iss 3 (2014)
The type II AAA+ protein p97 is involved in numerous cellular activities, including endoplasmic reticulum-associated degradation, transcription activation, membrane fusion and cell-cycle control. These activities are at least in part regulated by the
Externí odkaz:
https://doaj.org/article/8d739f2b35d54485953276f02fd15761
Autor:
Kentaro Noi, Satoru Mukai, Kanji Okumoto, Teru Ogura, Hajime Niwa, Yukio Fujiki, Yasuhiro Miyauchi-Nanri
Publikováno v:
The Journal of Biochemistry.
A newly isolated binding protein of peroxisomal targeting signal type 2 (PTS2) receptor Pex7, termed P7BP2, is transported into peroxisomes by binding to the longer isoform of Pex5p, Pex5pL, via Pex7p. The binding to Pex7p and peroxisomal localizatio
Publikováno v:
Biology Open
Biology Open, Vol 4, Iss 6, Pp 710-721 (2015)
Biology Open, Vol 4, Iss 6, Pp 710-721 (2015)
Pex11p family proteins are key players in peroxisomal fission, but their molecular mechanisms remains mostly unknown. In the present study, overexpression of Pex11pβ caused substantial vesiculation of peroxisomes in mammalian cells. This vesicle for
Autor:
Yousef Shafeghati, Masanori Honsho, Yuichi Abe, Ryusuke Toyama, Yoshiteru Sato, Hajime Niwa, Masafumi Noguchi, Kamran Ghaedi, Ali Rahmanifar, Yukio Fujiki
Publikováno v:
Journal of Human Genetics. 59:387-392
Rhizomelic chondrodysplasia punctata (RCDP) is an autosomal recessive disorder due to the deficiency in ether lipid synthesis. RCDP type 1, the most prominent type, is caused by the dysfunction of the receptor of peroxisome targeting signal type 2, P
Publikováno v:
The Journal of Biological Chemistry
Background: p97/VCP disease-linked mutations increase ATPase activity and destabilize the N-D1 domain interaction. Results: Increased N-domain flexibility in p97/VCP increases ATPase activity, whereas locking down the N-domain decreases it. Conclusio
Publikováno v:
Nuclear Engineering and Design. 238:66-73
For the transition phase analysis of core disruptive accidents, the development of a three-dimensional reactor safety analysis code, SIMMER-IV, has been carried out based on the technology of the two-dimensional SIMMER-III code. The world first appli
Publikováno v:
Molecular Cell. 22:575-585
Summary An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembran
Publikováno v:
Journal of Molecular Biology. 357:481-492
Bacterial enhancer-binding proteins (EBP) activate transcription by hydrolyzing ATP to restructure the sigma(54)-RNA polymerase-promoter complex. We compare six high resolution structures (
Autor:
Tomoyasu Mizuno, Hajime Niwa
Publikováno v:
Nuclear Technology. 146:155-163
Sodium-cooled mixed-oxide core design studies are performed with a target burnup of 150 GWd/t and possible measures against the recriticality issues in core disruptive accidents. Four types of core...