Zobrazeno 1 - 7
of 7
pro vyhledávání: '"B M, Willardson"'
Publikováno v:
Molecular vision. 5
These investigations were undertaken to compare and contrast the roles of phosducin and phosducin-like protein in the retina.Phosducin and phosducin-like protein were compared in an in vitro assay measuring their inhibition of transducin binding to l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::07732d66ca3f9b9f943eda31f6f64b8e
https://pubmed.ncbi.nlm.nih.gov/10617777
https://pubmed.ncbi.nlm.nih.gov/10617777
Publikováno v:
The Journal of biological chemistry. 269(39)
Heterotrimeric GTP-binding proteins (G-proteins) serve many different signal transduction pathways. Phosducin, a 28-kDa phosphoprotein, is expressed in a variety of mammalian cell types and blocks activation of several classes of G-proteins. Phosphor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5ff03db7dcb95e136c6440552e2dd150
https://pubmed.ncbi.nlm.nih.gov/7929057
https://pubmed.ncbi.nlm.nih.gov/7929057
Publikováno v:
The Journal of biological chemistry. 268(9)
Direct measurements of the binding between light-activated rhodopsin (Rho*) and transducin, the retinal rod G-protein, revealed a strongly cooperative interaction. Cooperativity was assessed by measuring the association of 125I-labeled transducin (Gt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3c6212f6fc0f711a592038017c34b344
https://pubmed.ncbi.nlm.nih.gov/8454608
https://pubmed.ncbi.nlm.nih.gov/8454608
Publikováno v:
The Journal of biological chemistry. 267(14)
Of the several proteins that bind along the cytoplasmic domain of erythrocyte membrane band 3, only the sites of interaction of proteins 4.1 and 4.2 remain to be at least partially localized. Using five independent techniques, we have undertaken to m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ded32c40fed339a9ef5e4117f913fbf8
https://pubmed.ncbi.nlm.nih.gov/1374405
https://pubmed.ncbi.nlm.nih.gov/1374405
Publikováno v:
The Journal of biological chemistry. 262(10)
The cytoplasmic domain of band 3 (cdb3) of the human erythrocyte membrane is a good substrate of endogenous and exogenous protein-tyrosine kinases. Because one site of tyrosine phosphorylation is within the glycolytic enzyme/hemoglobin-binding region
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bb336eb85d3e22026672979f09f1d6bb
https://pubmed.ncbi.nlm.nih.gov/3558357
https://pubmed.ncbi.nlm.nih.gov/3558357
Publikováno v:
The Journal of biological chemistry. 264(27)
Previous studies have demonstrated that modification of erythrocyte membrane cysteine residues via disulfide cross-briding or direct derivatization with thiol reagents promotes massive morphological, rheological, and structural changes in the cell. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7bd8c8fc564364b33cd699d63af86897
https://pubmed.ncbi.nlm.nih.gov/2550425
https://pubmed.ncbi.nlm.nih.gov/2550425
Publikováno v:
The Journal of biological chemistry. 264(27)
The predominant attachment site of the spectrin-based cytoskeleton to the erythrocyte membrane occurs via the interaction of ankyrin with the cytoplasmic domain of band 3 (cdb3). In order to further characterize this interaction, we have conducted ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b8c35659b17fb9cce4f9f9378c8b5967
https://pubmed.ncbi.nlm.nih.gov/2476434
https://pubmed.ncbi.nlm.nih.gov/2476434