Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Masami Yamashita"'
Autor:
Philip Lössl, Andrea M. Brunner, Fan Liu, Aneika C. Leney, Masami Yamashita, Richard A. Scheltema, Albert J. R. Heck
Publikováno v:
ACS Central Science, Vol 2, Iss 7, Pp 445-455 (2016)
Externí odkaz:
https://doaj.org/article/57ed0915ef654795926c124a629a8a8c
Autor:
Takashi Yamamura, Manabu Araki, Kazuo Fujihara, Tatsusada Okuno, Tatsuro Misu, Yuh-Cherng Guo, Cheryl Hemingway, Junnosuke Matsushima, Naofumi Sugaya, Masami Yamashita, H.-Christian von Büdingen, Katsuichi Miyamoto
Publikováno v:
Multiple Sclerosis and Related Disorders. 61:103772
Neuromyelitis optica spectrum disorder (NMOSD) is a rare, chronic, autoimmune disease, characterized by astrocytopathic lesions in the central nervous system (Beekman et al., 2019; Fujihara et al., 2020). The main aim of NMOSD maintenance therapy is
Publikováno v:
The Proceedings of Design & Systems Conference. :1202
Autor:
Jan M. Schuller, Mike Strauss, Elena Conti, Ingmar B. Schäfer, Steffen Schüssler, Masami Yamashita, Peter Reichelt
Publikováno v:
Cell
Summary The stability of eukaryotic mRNAs is dependent on a ribonucleoprotein (RNP) complex of poly(A)-binding proteins (PABPC1/Pab1) organized on the poly(A) tail. This poly(A) RNP not only protects mRNAs from premature degradation but also stimulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9de720de8e6962aed455a732255c4406
https://hdl.handle.net/21.11116/0000-0003-E98D-821.11116/0000-0003-E98F-621.11116/0000-0003-E990-3
https://hdl.handle.net/21.11116/0000-0003-E98D-821.11116/0000-0003-E98F-621.11116/0000-0003-E990-3
Autor:
Fabio Marino, Violette Gautier, Arjen Scholten, Albert J. R. Heck, Michiel van de Waterbeemd, Masami Yamashita, Philip Lössl, Elena Conti
Publikováno v:
Angewandte Chemie. 126:9815-9819
Die Phosphorylierung von Proteinen ist ein weit verbreiteter Prozess, welcher die mechanistische Grundlage fur zellulare Signalubertragung bildet. Derzeit werden Aspekte wie Ortsspezifitat, Reaktionskinetik, der Einfluss von Kofaktoren und Struktur-F
Autor:
Stephen E. Kaiser, Masami Yamashita, Kazuhiro Iwai, Hiroaki Fujita, Azusa Yoshikawa, Shuya Fukai, Yusuke Sato, Atsushi Yamagata
Publikováno v:
Proceedings of the National Academy of Sciences. 108:20520-20525
The linear ubiquitin chain assembly complex (LUBAC) is a key nuclear factor-κB (NF-κB) pathway component that produces linear polyubiquitin chains. The HOIL-1L subunit of LUBAC has been shown to bind linear chains; however, detailed structural and
Autor:
Hisatoshi Mimura, Yusuke Sato, Masami Yamashita, Azusa Yoshikawa, Shuya Fukai, Atsushi Yamagata
Publikováno v:
Genes to Cells. 15:29-41
Tail anchored (TA) proteins, which are important for numerous cellular processes, are defined by a single transmembrane domain (TMD) near the C-terminus. The membrane insertion of TA proteins is mediated by the highly conserved ATPase Get3. Here we r
Autor:
Masami Yamashita, Yusuke Sato, Atsushi Yamagata, Hisatoshi Mimura, Azusa Yoshikawa, Shuya Fukai
Publikováno v:
The EMBO Journal
RAP80 has a key role in the recruitment of the Abraxas-BRCC36-BRCA1-BARD1 complex to DNA-damage foci for DNA repair through specific recognition of Lys 63-linked polyubiquitinated proteins by its tandem ubiquitin-interacting motifs (UIMs). Here, we r
Autor:
Masami Yamashita, Atsushi Yamagata, Shuya Fukai, Yusuke Sato, Osamu Nureki, Azusa Yoshikawa, Kayoko Ookata, Masayuki Komada, Hisatoshi Mimura, Kazuhiro Iwai
Publikováno v:
Nature. 455:358-362
Deubiquitinating enzymes (DUBs) remove ubiquitin from conjugated substrates to regulate various cellular processes. The Zn(2+)-dependent DUBs AMSH and AMSH-LP regulate receptor trafficking by specifically cleaving Lys 63-linked polyubiquitin chains f
Autor:
Shuya Fukai, Osamu Nureki, Hisanori Horiuchi, Tomoyuki Ikeda, Tomohito Higashi, Tadaomi Takenawa, Masami Yamashita, Shiro Suetsugu, Yusuke Sato, Ryutaro Shirakawa, Toru Kita
Publikováno v:
Genes to Cells. 12:1255-1265
Reorganization of the actin filament is an essential process for cell motility, cell–cell attachment and intracellular transport. Formin proteins promote nucleation and elongation of the actin filament, and thus are key regulators for this process.