Výsledky vyhledávání - "K, Drickamer"

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Specificity of lung surfactant protein SP-A for both the carbohydrate and the lipid moieties of certain neutral glycolipids

Autor: Chun-Ting Yuen, G F Ross, Wengang Chai, K Drickamer, J R Wright, Alexander M. Lawson, Ten Feizi, R A Childs

Publikováno v: Journal of Biological Chemistry. 267:9972-9979

Binding specificity of the major surfactant protein SP-A from human and dog lung has been investigated. Radiobinding experiments have shown that both proteins bind in a Ca(2+)-dependent manner to galactose, mannose, fucose, and glucose linked to bovi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cb45868908a6bd00bd2ab516066716e7
https://doi.org/10.1016/s0021-9258(19)50187-9

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Biosynthesis of Human Fibroblast Growth Factor-5

Autor: Mitchell Goldfarb, Jeff D. Hardin, Xi Zhan, K. Drickamer, B. Bates

Publikováno v: Molecular and Cellular Biology. 11:1840-1845

We have analyzed the biosynthesis of human fibroblast growth factor-5 (FGF-5) at the translational and posttranslational levels. FGF-5 RNA synthesized in vitro can be translated in rabbit reticulocyte lysates to yield a 29,500-Da protein, which is co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68a4de873a19b421b2a01d67c29d4308
https://doi.org/10.1128/mcb.11.4.1840-1845.1991

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Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins

Autor: K. Drickamer, Reiko T. Lee, Yuan C. Lee, M. Fay, Y. Ichikawa, Ming-Chuan Shao

Publikováno v: Journal of Biological Chemistry. 266:4810-4815

Sugar-binding characteristics of rat serum mannose-binding protein (MBP) were studied using the carbohydrate-recognition domain of this protein expressed from a cloned cDNA. To assess the binding affinity of various test compounds, they were added as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d04d733051277393be7968a0679490c5
https://doi.org/10.1016/s0021-9258(19)67721-5

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Endocytosis via coated pits mediated by glycoprotein receptor in which the cytoplasmic tail is replaced by unrelated sequences

Autor: G Proulx, K Drickamer, T Mellow, T Gilbert, François Verrey

Publikováno v: Europe PubMed Central

Rat 6 fibroblast cell lines expressing wild-type chicken liver glycoprotein receptor (CHL) or chimeric receptors with alternate cytoplasmic tails were produced to study the role of the cytoplasmic tail in mediating receptor localization in coated pit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c0b363afe3b22e2c125fd95bbb449ba
https://doi.org/10.1091/mbc.1.6.471

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Polarized expression of functional rat liver asialoglycoprotein receptor in transfected Madin-Darby canine kidney cells

Autor: K Drickamer, Enrique Rodriguez-Boulan, A Patzak, Lutz Graeve

Publikováno v: Journal of Biological Chemistry. 265:1216-1224

The rat liver asialoglycoprotein receptor or rat hepatic lectin (RHL) consists of two polypeptide species, a major one designated RHL-1 and a minor one designated RHL-2/3, which exists in two differentially glycosylated forms. We have studied the bio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::715d03cdfed9d4345d17d475958cbbdf
https://doi.org/10.1016/s0021-9258(19)40180-4

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A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands

Autor: D A, Mitchell, A J, Fadden, K, Drickamer

Publikováno v: The Journal of biological chemistry. 276(31)

DC-SIGN and DC-SIGNR are cell-surface receptors that mediate cell-cell interactions within the immune system by binding to intercellular adhesion molecule-3. The receptor polypeptides share 77% amino acid sequence identity and are type II transmembra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::03383abf36fae1692b67abc047a62042
https://pubmed.ncbi.nlm.nih.gov/11384997

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Binding of sugar ligands to Ca(2+)-dependent animal lectins. II. Generation of high-affinity galactose binding by site-directed mutagenesis

Autor: S T, Iobst, K, Drickamer

Publikováno v: The Journal of biological chemistry. 269(22)

Changes have been introduced into the Ca(2+)-dependent carbohydrate-recognition domain (CRD) of rat serum mannose-binding protein by site-directed mutagenesis to model the binding sites of homologous galactose-binding CRDs. Binding assays reveal that

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7618cca8bec5b22435b17fe5868a2004
https://pubmed.ncbi.nlm.nih.gov/8195195

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