Genes to Cells
© The Molecular Biology Society of Japan/Wiley Publishing Asia Pty Ltd.
Edited By: Mitsuhiro Yanagida
Impact Factor: 2.805
ISI Journal Citation Reports © Ranking: 2014: 70/167 (Genetics & Heredity); 111/184 (Cell Biology)
Online ISSN: 1365-2443
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Recently Published Articles
- Nuclear magnetic resonance analysis of the conformational state of cancer mutant of fibroblast growth factor receptor 1 tyrosine kinase domain
Yoshihiro Kobashigawa, Shinjiro Amano, Kaito Yoza, Rika Himeno, Shun Amemiya, Hiroshi Morioka, Mariko Yokogawa, Hiroyuki Kumeta, Joseph Schlessinger and Fuyuhiko Inagaki
Article first published online: 10 FEB 2016 | DOI: 10.1111/gtc.12345
NMR analysis pf the tyrosine kinase domain of fibroblast growth factor receptor 1 (FGFR1) revealed that cancer mutation induce locally activated conformation. Combination of the cancer mutation revealed that independent and additive feature of the cancer mutation to the conformational state of tyrosine kinase, which would help understand dynamic feature of regulation of tyrosine kinase.
- Chaperone complex BAG2–HSC70 regulates localization of Caenorhabditis elegans leucine-rich repeat kinase LRK-1 to the Golgi
Takashi Fukuzono, Strahil Iv. Pastuhov, Okinobu Fukushima, Chun Li, Ayuna Hattori, Shun-ichiro Iemura, Tohru Natsume, Hiroshi Shibuya, Hiroshi Hanafusa, Kunihiro Matsumoto and Naoki Hisamoto
Article first published online: 8 FEB 2016 | DOI: 10.1111/gtc.12338
Mutations in LRRK2 gene are linked to autosomal dominant forms of Parkinson's disease. We identified two human proteins that bind to LRRK2 protein: BAG2 and HSC70, which have been known to form a chaperone complex. We also demonstrated that the C. elegans homologs of BAG2 and HSC70 determine the polarized sorting of synaptic vesicle proteins by regulating the localization of LRK-1, the sole homolog of human LRRK2, to the Golgi apparatus.
- You have full text access to this OnlineOpen articleEfficient sequence-specific isolation of DNA fragments and chromatin by in vitro enChIP technology using recombinant CRISPR ribonucleoproteins
Toshitsugu Fujita, Miyuki Yuno and Hodaka Fujii
Article first published online: 5 FEB 2016 | DOI: 10.1111/gtc.12341
In this study, we developed in vitro enChIP using recombinant CRISPR ribonucleoproteins. in vitro enChIP technology is of potential use for sequence-specific isolation of DNA, as well as for identification of molecules interacting with genomic regions of interest in vivo.
- Ouro proteins are not essential to tail regression during Xenopus tropicalis metamorphosis
Yuya Nakai, Keisuke Nakajima, Jacques Robert and Yoshio Yaoita
Article first published online: 5 FEB 2016 | DOI: 10.1111/gtc.12337
We generated ouro-knockout tadpoles and T-cell deficient tadpoles using genomic editing. None of the knockout tadpoles showed any significant delay in the process of tail shortening during the climax of Xenopus tropicalis metamorphosis. Our results demonstrate that neither Ouro proteins nor T cells are necessary for tail elimination.
- You have full text access to this OnlineOpen articleC-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4
Hideaki Ohtomo, Satoko Akashi, Yoshihito Moriwaki, Mitsuru Okuwaki, Akihisa Osakabe, Kyosuke Nagata, Hitoshi Kurumizaka and Yoshifumi Nishimura
Article first published online: 4 FEB 2016 | DOI: 10.1111/gtc.12339
The two C-terminal acidic domains in the human NAP1 dimer provide binding-assistance for H2A-H2B but not H3-H4.