Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Shoko Kawasaki-Nishi"'
Autor:
Yu Hisano, Naoki Kobayashi, Shoko Kawasaki-Nishi, Akihito Yamaguchi, Tsuyoshi Nishi, Masato Otsuka
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)
Scientific Reports
Scientific Reports
Sphingosine 1-phosphate (S1P) is an intercellular signaling molecule present in blood. Erythrocytes have a central role in maintaining the S1P concentration in the blood stream. We previously demonstrated that S1P is exported from erythrocytes by a g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75f0bda6998371de63c643eff602d36f
https://doi.org/10.1038/s41598-018-23300-x
https://doi.org/10.1038/s41598-018-23300-x
Publikováno v:
Biochemical and Biophysical Research Communications. 364:1032-1036
We have identified splicing variants of the mouse a4 subunit which have the same open reading frame but have a different 5′-noncoding sequence. Further determination of the 5′-upstream region of the a4 gene in mouse indicated the presence of two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b79a4c925e793233327d7fc70a79ae00
https://doi.org/10.1016/j.bbrc.2007.10.118
https://doi.org/10.1016/j.bbrc.2007.10.118
Publikováno v:
Journal of Biological Chemistry. 278:46396-46402
We have identified a cDNA encoding a novel isoform of the mouse V-ATPase d subunit (d2). The protein encoded is 350 amino acids in length and shows 42 and 67% identity to the yeast d subunit (Vma6p) and the mouse d1 isoform, respectively. Reverse tra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7acedd4703141b0a6c9ae65399c28b3f
https://doi.org/10.1074/jbc.m303924200
https://doi.org/10.1074/jbc.m303924200
Autor:
Yoichiro Arata, Michael Forgac, Elim Shao, Tsuyoshi Nishi, Shoko Kawasaki-Nishi, Stephan Wilkens
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1555(1-3):71-74
The vacuolar (H+)-ATPases (or V-ATPases) are ATP-dependent proton pumps that function to acidify intracellular compartments in eukaryotic cells. This acidification is essential for such processes as receptor-mediated endocytosis, intracellular target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a5f88a82631b88fd16765d66895c1e7
Publikováno v:
Journal of Biological Chemistry. 276:47411-47420
The 100-kDa "a" subunit of the vacuolar proton-translocating ATPase (V-ATPase) is encoded by two genes in yeast, VPH1 and STV1. The Vph1p-containing complex localizes to the vacuole, whereas the Stv1p-containing complex resides in some other intracel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6c5daccfe73631f61620796ed9d668
https://doi.org/10.1074/jbc.m108310200
https://doi.org/10.1074/jbc.m108310200
Publikováno v:
The Journal of biological chemistry. 278(43)
Proton translocation by the vacuolar (H+)-ATPase (or V-ATPase) has been shown by mutagenesis to be dependent upon charged residues present within transmembrane segments of subunit a as well as the three proteolipid subunits (c, c', and c"). Interacti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::087bf1b5e7a2241a70302d1c67c14850
https://pubmed.ncbi.nlm.nih.gov/12917411
https://pubmed.ncbi.nlm.nih.gov/12917411
Publikováno v:
FEBS letters. 545(1)
The vacuolar H(+)-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells. They are multisubu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de8fc1e759d1867b896c5a98d5a449f2
https://pubmed.ncbi.nlm.nih.gov/12788495
https://pubmed.ncbi.nlm.nih.gov/12788495
Publikováno v:
The Journal of biological chemistry. 278(15)
Subunit A is the catalytic nucleotide binding subunit of the vacuolar proton-translocating ATPase (or V-ATPase) and is homologous to subunit beta of the F(1)F(0) ATP synthase (or F-ATPase). Amino acid sequence alignment of these subunits reveals a 90
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dcb64099eb9de920bf78aef65277a53
https://pubmed.ncbi.nlm.nih.gov/12569096
https://pubmed.ncbi.nlm.nih.gov/12569096
Publikováno v:
The Journal of biological chemistry. 278(8)
The yeast vacuolar ATPase (V-ATPase) contains three proteolipid subunits: c (Vma3p), c' (Vma11p), and c" (Vma16p). Each subunit contains a buried glutamate residue that is essential for function, and these subunits are not able to substitute for each
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34c20c453f59b80b575c352d9f388614
https://pubmed.ncbi.nlm.nih.gov/12482875
https://pubmed.ncbi.nlm.nih.gov/12482875
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 98(22)
The vacuolar (H + )-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular compartments and pump protons across specialized plasma membranes. Proton translocation occurs through the integral V 0 domain, which contains five diff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afde1b1985defcd5b7f67a181cd03851
https://pubmed.ncbi.nlm.nih.gov/11592980
https://pubmed.ncbi.nlm.nih.gov/11592980