Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Christine Diggle"'
Autor:
Toshiko Yamazawa, Takuya Kobayashi, Nagomi Kurebayashi, Masato Konishi, Satoru Noguchi, Takayoshi Inoue, Yukiko U. Inoue, Ichizo Nishino, Shuichi Mori, Hiroto Iinuma, Noriaki Manaka, Hiroyuki Kagechika, Arkady Uryash, Jose Adams, Jose R. Lopez, Xiaochen Liu, Christine Diggle, Paul D. Allen, Sho Kakizawa, Keigo Ikeda, Bangzhong Lin, Yui Ikemi, Kazuto Nunomura, Shinsaku Nakagawa, Takashi Sakurai, Takashi Murayama
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Mutations in ryanodine receptor 1 (RyR1), a Ca2+ release channel in skeletal muscle, cause malignant hyperthermia (MH) and are involved in heat stroke. Here, the authors show that an oxolinic acid-derivative RyR1 inhibitor effectively prevents and tr
Externí odkaz:
https://doaj.org/article/afd2999f767e49b494c83b5f5e5c1a4b
Publikováno v:
British Journal of Anaesthesia. 130:e207-e208
Publikováno v:
British Journal of Anaesthesia. 128:e60
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1320:265-274
Transhydrogenase from mitochondrial and bacterial membranes couples proton translocation to hydride transfer between NAD(H) and NADP(H). The enzyme has three domains, of which domains I and III protrude from the membrane. These possess the NAD(H)- an
Publikováno v:
European Journal of Biochemistry. 239:737-741
Transhydrogenase catalyses the transfer of reducing equivalents between NAD(H) and NADP(H) coupled to the translocation of protons across a membrane. The NAD(H)-binding domain of transhydrogenase (domain I protein) from Rhodospirillum rubrum and from
Autor:
Nick P.J. Cotton, Christopher M. Thomas, Rachel L. Grimley, Christine Diggle, Tania Bizouarn, Philip G. Quirk, J. Baz Jackson
Publikováno v:
Journal of Biological Chemistry. 271:10109-10115
The Tyr residue in the mobile loop region of the soluble, domain I polypeptide (called Ths) of the proton-translocating transhydrogenase from Rhodospirillum rubrum has been substituted by Asn and by Phe. The recombinant proteins were expressed at hig
Autor:
Nick P.J. Cotton, J. Baz Jackson, Christopher M. Thomas, Christine Diggle, Rachel L. Grimley, Philip G. Quirk
Publikováno v:
European Journal of Biochemistry. 232:315-326
Transhydrogenase catalyses the reversible transfer of reducing equivalents between NAD(H) and NADP(H) to the translocation of protons across a membrane. Uniquely in Rhodospirillum rubrum, the NAD(H)-binding subunit (called Ths) exists as a separate s
Publikováno v:
European Journal of Biochemistry. 228:719-726
Transhydrogenase, which catalyses the reduction of NADP+ by NADH coupled to proton translocation across a membrane, may be unique in the photosynthetic bacterium Rhodospirillum rubrum. Unlike the homologous enzyme from animal mitochondria and other b
Publikováno v:
European journal of biochemistry. 241(1)
Transhydrogenase comprises three domains. Domains I and III are peripheral to the membrane and possess the NAD(H)- and NADP(H)-binding sites, respectively, and domain II spans the membrane. Domain III of transhydrogenase from Rhodospirillum rubrum wa
Autor:
Christopher M. Thomas, Philip G. Quirk, Nick P.J. Cotton, Rachel Grimley, Christine Diggle, J. Baz Jackson, Tania Bizouarn
Publikováno v:
Photosynthesis: from Light to Biosphere ISBN: 9789401065627
Photosynthesis: from Light to Biosphere
Photosynthesis: from Light to Biosphere
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::aa25674a7d4d6d80dc4495617493318a
https://doi.org/10.1007/978-94-009-0173-5_389
https://doi.org/10.1007/978-94-009-0173-5_389