Výsledky vyhledávání - "Barbara Legrum"

A gene-fusion strategy for stoichiometric and co-localized expression of light-gated membrane proteins

Autor: Ulrich Terpitz, Barbara Legrum, Ernst Bamberg, Edward S. Boyden, Christian Bamann, Phillip G. Wood, Sonja Kleinlogel, Deniz Gökbuget

Publikováno v: Nature methods. 8(12)

The precise co-localization and stoichiometric expression of two different light-gated membrane proteins can vastly improve the physiological usefulness of optogenetics for the modulation of cell excitability with light. Here we present a gene-fusion

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94b0b529db3cca62ddbf57e34e717656
https://pubmed.ncbi.nlm.nih.gov/22127216

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The influence of two anion-transport inhibitors, 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate and 4,4'-dibenzoylstilbene-2,2'-disulfonate, on the self-association of erythrocyte band 3 protein

Autor: Peter Schuck, Hermann Passow, Dieter Schubert, Barbara Legrum

Publikováno v: European journal of biochemistry. 230(2)

4,4'-Diisothiocyanatodihydrostilbene-2,2'-disulfonate and 4,4'-dibenzoylstilbene-2,2'-disulfonate potently inhibit the erythrocyte anion transporter. These inhibitors act by binding, with a 1:1 stoichiometry, to the band 3 transport protein. We have

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc07c429fe21ad69c942eadfce818b1f
https://pubmed.ncbi.nlm.nih.gov/7607255

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Inhibition of inorganic anion transport across the human red blood cell membrane by chloride-dependent association of dipyridamole with a stilbene disulfonate binding site on the band 3 protein

Autor: Hermann Passow, Barbara Legrum

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. 979:193-207

The inhibition of inorganic anion transport by dipyridamole (2,6-bis(diethanolamino)-4,8-dipiperidinopyrimido[5,4-d] pyrimidine) takes place only in the presence of Cl-, other halides, nitrate or bicarbonate. At any given dipyridamole concentration,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44abfb9d0f0f80149af5ab8be4dfaad5
https://doi.org/10.1016/0005-2736(89)90435-5

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ANION TRANSPORT ACROSS THE RED BLOOD CELL MEMBRANE AND THE CONFORMATION OF THE PROTEIN IN BAND 3

Autor: Laila Zaki, Barbara Legrum, Hermann Passow, Hugo Fasold, Eva-Maria Gärtner, W. Ruffing

Publikováno v: Annals of the New York Academy of Sciences. 341:361-383

Measuring the rate of dinitrophenylation of a specific lysine residue (called a) that is allosterically linked to the transfer site, it could be demonstrated that the anion transport protein may exist in two different conformational states, designate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3988036d54193fe5b957e1526c4da6cf
https://doi.org/10.1111/j.1749-6632.1980.tb47184.x

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Three different actions of phenylglyoxal on band 3 protein-mediated anion transport across the red blood cell membrane

Autor: Eva-Maria Gärtner, Barbara Legrum, Katja M. Liebold, Hermann Passow, Hugo Fasold

Publikováno v: Biochimica et Biophysica Acta (BBA) - Biomembranes. (2):208-222

Phenylglyoxalation of the red blood cell membrane leads to three superimposed effects on band 3 protein-mediated anion equilibrium exchange as measured by means of radiosulfate: (1) a shift of the curve relating transport activity to pH towards lower

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Anion transport in oocytes of Xenopus laevis induced by expression of mouse erythroid band 3 protein--encoding cRNA and of a cRNA derivative obtained by site-directed mutagenesis at the stilbene disulfonate binding site

Autor: Detlef Bartel, Sigrid Lepke, Gerlinde Layh-Schmitt, Hermann Passow, Barbara Legrum

Publikováno v: The EMBO journal. 8(12)

A vector was constructed containing a cDNA for mouse band 3 obtained from Demuth et al. (1986, EMBO J., 5, 1205-1214), a synthetic linker (containing 5'-non-translated region, start codon and a coding region for the first 12 N-terminal amino acids),

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23b447823fad9bf22b36d5d90bb5e13a
https://pubmed.ncbi.nlm.nih.gov/2479548

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Enhancement of anion equilibrium exchange by dansylation of the red blood cell membrane

Autor: Barbara Legrum, Hermann Passow, Hugo Fasold

Publikováno v: Hoppe-Seyler's Zeitschrift fur physiologische Chemie. 361(10)

Dansylation of resealed red cell ghosts enhances the band 3 protein-mediated equilibrium exchange of sulfate ions. After dansylation, the specific anion transport inhibitor 4,4'-diisothiocyanato-dihydrostilbene 2,2'-disulfonate (H2DIDS) is still capa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6876567401da8dc2db3f2ca7544f7d1
https://pubmed.ncbi.nlm.nih.gov/7450677

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