Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Ellen B. Gilliam"'
Autor:
Howard M. Rosenblatt, Peter G. Schulam, J.Patrick Whelan, William T. Shearer, Ellen B. Gilliam
Publikováno v:
Cellular Immunology. 136:41-53
Binding of LA350, a lymphoblastoid human B cell line, by phorbol myristate acetate (PMA) plus a calcium ionophore, either ionomycin or A23187, produced unique alterations in the release of arachidonic acid (AA) from cellular phospholipids. After equi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f32cd90a77bfeebbd7fb39c0a13dda8e
https://doi.org/10.1016/0008-8749(91)90379-p
https://doi.org/10.1016/0008-8749(91)90379-p
Publikováno v:
Biochemistry. 16:4150-4156
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54aa8d02abcc27383df86d9515271ecd
https://doi.org/10.1021/bi00638a003
https://doi.org/10.1021/bi00638a003
Autor:
John J. Langone, Catherine G. Green, Ellen B. Gilliam, Chandra Das, John E. McClure, Robert G. Ulrich, William T. Shearer
Publikováno v:
Molecular and Cellular Biochemistry. 67:135-144
Surface binding of anti-actin IgG alone or in a Mr = 716 000 [(IgG)2 Protein A]2 complex results in a stimulation of DNA synthesis and cell growth in L cells. Cyclic-AMP (0.01-1.0 mM) added to such cell cultures augmented DNA synthesis as measured by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d05d99bee5f2158c356dc69a4f444cab
https://doi.org/10.1007/bf02370172
https://doi.org/10.1007/bf02370172
Publikováno v:
Cellular Immunology. 111:316-331
Anti-mu antibody binds to surface IgM on LA350, a transformed human B-cell line, and causes the immediate (5 min) hydrolysis of phosphatidylinositol (PI) into inositol 1,4,5-triphosphate (IP3) and diacylglycerol followed by a subsequent (48-72 hr) in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09c94122a45e306bc886d8c8892f5f17
https://doi.org/10.1016/0008-8749(88)90096-2
https://doi.org/10.1016/0008-8749(88)90096-2
Publikováno v:
Cellular Immunology. 89:55-65
Phosphorylation of cellular proteins was stimulated in a dose-dependent manner by the surface binding of IgG antibodies to antigens on L cells. Most prominent among the phosphorylated cellular proteins were Mr = 115,000, 93,000, 58,000, 38,000, and 3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bfe0770e82a878d6473c14ade0b14a3
https://doi.org/10.1016/0008-8749(84)90197-7
https://doi.org/10.1016/0008-8749(84)90197-7
Publikováno v:
Cellular Immunology. 111:296-315
Within 5 min of the binding of anti-μ antibody (anti-μ) to surface IgM on LA350, a human lymphoblastoid B-cell line, there was a significantly enhanced incorporation of 32 P into the phosphatidic acid (PA) and phosphatidylinositol (PI) fractions of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fee8b7fd4a37d33e4ce811f4bb16afe
https://doi.org/10.1016/0008-8749(88)90095-0
https://doi.org/10.1016/0008-8749(88)90095-0
Autor:
Ellen B. Gilliam, William T. Shearer
Publikováno v:
Biochemical and Biophysical Research Communications. 124:23-28
The effects of prostaglandins E 1 and F 2α upon the anti-actin antibody-induced stimulation of DNA synthesis and protein phosphorylation were studied in L cells. This system was previously shown by us to exhibit a rapid turnover of arachidonic acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af5a3cc7fe5419fffcb948f7c52953c0
https://doi.org/10.1016/0006-291x(84)90910-0
https://doi.org/10.1016/0006-291x(84)90910-0
Publikováno v:
Archives of biochemistry and biophysics. 165(1)
Novikoff ascites hepatoma cells were highly agglutinable by the plant lectins concanavalin A and wheat germ agglutinin. Treatment of the intact cells with papain released from the cell surface a glycopeptide fraction which possessed concanavalin A an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::781153f47b06c3b5edd65214afe07337
https://pubmed.ncbi.nlm.nih.gov/4374131
https://pubmed.ncbi.nlm.nih.gov/4374131
Publikováno v:
Biochemical and biophysical research communications. 109(4)
Serine proteases coisolate with human very low density lipoproteins (VLDL) which degrade apolipoprotein E and cause hypertriglyceridemic VLDL to lose the ability to interact with the LDL receptor of human skin fibroblasts. We identified proteolytic f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d021a1b3f787423814d759ea5e2a9116
https://pubmed.ncbi.nlm.nih.gov/6301435
https://pubmed.ncbi.nlm.nih.gov/6301435
Autor:
Edward M. Davis, John M. Robinson, Sylvia C. Capetillo, Ellen B. Gilliam, David F. Smith, Earl F. Walborg
Publikováno v:
Biochemical and biophysical research communications. 72(1)
Papain digestion of Novikoff or AS-30D rat hepatoma cells released glycopeptides from the cell surface. That portion of the glycopeptides accessible to Sephadex G-50 was digested with pronase and the component glycopeptides partially resolved by ion-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcb3d761dbf7f7cfc20e2f0e2cdc9a2d
https://pubmed.ncbi.nlm.nih.gov/186046
https://pubmed.ncbi.nlm.nih.gov/186046