Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Rahel Pfeiffer"'
Autor:
Vanessa Summa, Luca Mastroberardino, Rahel Pfeiffer, Benjamin Spindler, David A. Pearce, François Verrey, Marija Zecevic
Publikováno v:
Kidney International. 57(4):1277-1282
Pleiotropic action of aldosterone in epithelia mediated by transcription and post-transcription mechanisms. The aldosterone-induced increase in sodium reabsorption across tight epithelia can be divided schematically into two functional phases: an ear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a984c5bc0f4f877e2df6752b294018f5
Autor:
François Verrey, Grégoire Rossier, Jan Loffing, Rahel Pfeiffer, Thomas Eggermann, Christian Bauch, Christian Meier, Lukas C. Kühn, Dominique Loffing-Cueni
Publikováno v:
Molecular Biology of the Cell. 10:4135-4147
Mutations of the glycoprotein rBAT cause cystinuria type I, an autosomal recessive failure of dibasic amino acid transport (b0,+type) across luminal membranes of intestine and kidney cells. Here we identify the permease-like protein b0,+AT as the cat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf10f7362a934289f3380fa34e318d2
https://doi.org/10.1091/mbc.10.12.4135
https://doi.org/10.1091/mbc.10.12.4135
Publikováno v:
Parasitology. 119:569-576
The Schistosoma mansoni protein, SPRM1lc, is a light chain member of a new family of heterodimeric amino acid permeases. These proteins require covalent association with a type II glycoprotein (like h4F2hc) for functional surface localization when ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a32ba23d1d78e518ace64b941b7eba3f
https://doi.org/10.1017/s0031182099005181
https://doi.org/10.1017/s0031182099005181
Autor:
Charles B. Shoemaker, Rahel Pfeiffer, Luca Mastroberardino, Patrick J. Skelly, Jan Loffing, Benjamin Spindler, François Verrey
Publikováno v:
Nature. 395:288-291
Amino-acid transport across cellular plasma membranes depends on several parallel-functioning (co-)transporters and exchangers. The widespread transport system L accounts for a sodium-independent exchange of large, neutral amino acids, whereas the sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4fc6be482ce9fe5862673f0b1df9021
https://doi.org/10.1038/26246
https://doi.org/10.1038/26246
Publikováno v:
The Journal of membrane biology. 172(3)
The L-type amino acid transporter LAT1 has recently been identified as being a disulfide-linked "light chain" of the ubiquitously expressed glycoprotein 4F2hc/CD98. Several LAT1-related transporters have been identified, which share the same putative
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::704e061c9ac9c97940cda12b7552f2ab
https://pubmed.ncbi.nlm.nih.gov/10568788
https://pubmed.ncbi.nlm.nih.gov/10568788
Autor:
Christian Meier, Grégoire Rossier, François Verrey, Rahel Pfeiffer, Benjamin Spindler, Lukas C. Kühn
Amino acid transport across cellular membranes is mediated by multiple transporters with overlapping specificities. We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7a60aa63d430a5acd7856deca07d959
https://europepmc.org/articles/PMC1171101/
https://europepmc.org/articles/PMC1171101/
Autor:
Rahel Pfeiffer
Publikováno v:
Biomedical Engineering / Biomedizinische Technik, 41 (s1)
Biomedical Engineering / Biomedizinische Technik, 41 (s1)
ISSN:0013-5585
ISSN:1862-278X
ISSN:0013-5585
ISSN:1862-278X
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc3223922255b52888805429116f5b8b
Autor:
Benjamin Spindler, François Verrey, Patrick J. Skelly, Jan Loffing, Charles B. Shoemaker, Rahel Pfeiffer
Publikováno v:
FEBS Letters. (1-2):157-162
The protein mediating system L amino acid transport, AmAT-L, is a disulfide-linked heterodimer of a permease-related light chain (AmAT-L-lc) and the type II glycoprotein 4F2hc/CD98. The Schistosoma mansoni protein SPRM1 also heterodimerizes with h4F2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3699dea14af0036416ed68d587f25f15