PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15037120-3 2004 Subcellular localization of ERalpha and ERbeta was determined on formaldehyde-fixed, Saponin-permeabilized cells using conventional immunofluorescence techniques, as well as immunodetection of differential cellular components after subjecting the cultured cells to fractionation by sucrose gradient centrifugation. Sucrose 282-289 estrogen receptor 1 Homo sapiens 28-35 30137221-8 2019 However, sucrose density centrifugation and Cav-1 immunoisolation columns uniquely demonstrated very high protein-protein association only between ESR1, but not ESR2, with Cav-1. Sucrose 9-16 estrogen receptor 1 Homo sapiens 147-151 15291741-3 2004 In the present study, we have evaluated the expression of ERalpha and ERbeta by immunohistochemistry in normal tissue samples, and in purified human breast fibroblasts by Western blotting, RT-PCR analysis and ligand-binding sucrose gradient assay. Sucrose 224-231 estrogen receptor 1 Homo sapiens 58-65 8206333-5 1994 When performing ER immunoassay after sedimentation of estrogen receptors on sucrose gradients, we show that exposure of new epitopes induced by anti-estrogens can occur on a 4 s molecular form related to the 66 kDa monomeric estrogen receptor. Sucrose 76-83 estrogen receptor 1 Homo sapiens 16-18 9628887-6 1998 Western blot analysis of vaults purified on sucrose gradient showed the presence of estrogen receptor co-migrating with the vault peak. Sucrose 44-51 estrogen receptor 1 Homo sapiens 84-101 7918110-3 1994 By high salt sucrose density gradient centrifugation, we could observe that the four monoclonal anti-estrogen receptor antibodies bound different forms of receptor complexes from crosslinked cells. Sucrose 13-20 estrogen receptor 1 Homo sapiens 101-118 8206333-5 1994 When performing ER immunoassay after sedimentation of estrogen receptors on sucrose gradients, we show that exposure of new epitopes induced by anti-estrogens can occur on a 4 s molecular form related to the 66 kDa monomeric estrogen receptor. Sucrose 76-83 estrogen receptor 1 Homo sapiens 54-71 2737141-5 1989 Three of these antisera recognized the functional form of ER, as determined by sucrose density gradient analysis. Sucrose 79-86 estrogen receptor 1 Homo sapiens 58-60 1574257-2 1992 Estrogen receptor (ER) assays were performed by sucrose gradient centrifugation method at multiple sites in large breast cancers. Sucrose 48-55 estrogen receptor 1 Homo sapiens 0-17 1574257-2 1992 Estrogen receptor (ER) assays were performed by sucrose gradient centrifugation method at multiple sites in large breast cancers. Sucrose 48-55 estrogen receptor 1 Homo sapiens 19-21 2282976-8 1990 Sucrose gradient experiments confirmed the generation of small molecular forms of ER, following its binding with estradiol. Sucrose 0-7 estrogen receptor 1 Homo sapiens 82-84 2605215-5 1989 Purified receptor has an electrophoretic mobility consistent with a molecular weight of 68,000, sediments as a 5S species on sucrose gradients, and reacts with antibody specific to the human estrogen receptor. Sucrose 125-132 estrogen receptor 1 Homo sapiens 191-208 2542691-5 1989 Sucrose density gradient centrifugation revealed that both 2- and 4-hydroxyestradiol inhibited the binding of estradiol-17 beta to both the 4S and 8S isoforms of the estrogen receptor in a competitive manner, with a Ki = 0.94 nM for 2-hydroxyestradiol and a Ki = 0.48 nM for 4-hydroxyestradiol. Sucrose 0-7 estrogen receptor 1 Homo sapiens 166-183 2458030-4 1988 Quantitative estrogen receptor content was determined by dextran-coated charcoal analysis and sucrose density gradient analysis. Sucrose 94-101 estrogen receptor 1 Homo sapiens 13-30 3770030-12 1986 ER settled predominantly in the 4S region and AEBS settled in the 5-5.5S region in a 5-20% sucrose gradient. Sucrose 91-98 estrogen receptor 1 Homo sapiens 0-2 3669657-3 1987 The complexes of estrogen receptor from MCF-7 cells with [3H]11 beta-CME2 and [3H]E2 show identical velocity sedimentation profiles on sucrose gradients, under conditions when the receptor is either a monomer of a dimer. Sucrose 135-142 estrogen receptor 1 Homo sapiens 17-34 3796221-3 1987 Competitive binding assays including the use of double-reciprocal plots and sucrose gradient analyses revealed that the levo and not the dextro enantiomer could inhibit the estradiol binding to the estrogen receptor. Sucrose 76-83 estrogen receptor 1 Homo sapiens 198-215 3023306-6 1986 Sucrose gradient centrifugation analysis of the cytosol fraction confirmed the presence of estradiol receptor activity in MCF-7 but not in U-2. Sucrose 0-7 estrogen receptor 1 Homo sapiens 91-109 3943090-4 1986 The nuclear estrogen receptor sediments as a 4.6 S species on high salt sucrose gradients, and it can be detected on sodium dodecyl sulfate-polyacrylamide gel immunoblot analysis as a species of molecular weight 65,000, identical to that of the MCF-7 estrogen receptor, using the monoclonal antibodies D75P3 gamma and H222Sp gamma prepared against the MCF-7 estrogen receptor. Sucrose 72-79 estrogen receptor 1 Homo sapiens 12-29 2983797-0 1985 Estrogen receptor separation employing sucrose deuterium oxide gradients generated during sample centrifugation. Sucrose 39-46 estrogen receptor 1 Homo sapiens 0-17 2983797-3 1985 Our results show that an identical pattern of protein separation can be achieved by layering the nuclear extracted estrogen receptor either on top of one single sucrose concentration or on a preformed gradient. Sucrose 161-168 estrogen receptor 1 Homo sapiens 115-132 6173208-2 1982 In sucrose gradient ultracentrifugation (10-30% w/v, 0.4 M KCl), the cytosol estrogen receptor complex, which migrates with a coefficient of sedimentation of 4.5 S, is shifted to 7.4 S when bound to the estrogen receptor monoclonal antibody. Sucrose 3-10 estrogen receptor 1 Homo sapiens 77-94 6824366-1 1983 The cytosolic estrogen receptor (CER) content of 1037 primary breast carcinomas was evaluated by sucrose density gradient analysis. Sucrose 97-104 estrogen receptor 1 Homo sapiens 14-31 6479094-2 1984 This nuclear estrogen receptor form sediments close to 5S on high salt sucrose density gradients, similar to receptor activated in vitro by gentle heating. Sucrose 71-78 estrogen receptor 1 Homo sapiens 13-30 6692388-8 1984 The [3H]MHT-ER antibody complex consistently sedimented as a higher-molecular-weight complex on sucrose density gradients than did the corresponding estrogenic complexes. Sucrose 96-103 estrogen receptor 1 Homo sapiens 12-14 6690295-2 1984 We have determined the rates of ER synthesis and turnover in MCF-7 breast cancer cells by incubating cells in medium supplemented with 13C15N2H-amino acids (dense amino acids) and monitoring the shift from "old-light" (preexisting) to "new-dense" (newly synthesized) receptors by velocity sedimentation on 0.4-M KCl, 5-20% sucrose gradients prepared in buffered deuterium oxide. Sucrose 323-330 estrogen receptor 1 Homo sapiens 32-34 6866366-2 1983 When cytosols of estrogen receptor-rich ovarian adenocarcinomas were analyzed on sucrose gradients containing 0.4 M KCl, the presence of monoclonal antibody against breast cancer estrogen receptor caused a binding peak for [125I]- and [3H]estradiol to shift from the 4S to the 8-9S region, indicating antibody complex formation with ovarian adenocarcinoma estrogen receptor. Sucrose 81-88 estrogen receptor 1 Homo sapiens 17-34 6866366-2 1983 When cytosols of estrogen receptor-rich ovarian adenocarcinomas were analyzed on sucrose gradients containing 0.4 M KCl, the presence of monoclonal antibody against breast cancer estrogen receptor caused a binding peak for [125I]- and [3H]estradiol to shift from the 4S to the 8-9S region, indicating antibody complex formation with ovarian adenocarcinoma estrogen receptor. Sucrose 81-88 estrogen receptor 1 Homo sapiens 179-196 6866366-2 1983 When cytosols of estrogen receptor-rich ovarian adenocarcinomas were analyzed on sucrose gradients containing 0.4 M KCl, the presence of monoclonal antibody against breast cancer estrogen receptor caused a binding peak for [125I]- and [3H]estradiol to shift from the 4S to the 8-9S region, indicating antibody complex formation with ovarian adenocarcinoma estrogen receptor. Sucrose 81-88 estrogen receptor 1 Homo sapiens 179-196 6191047-7 1983 Sucrose gradient analysis of the estrogen receptor of benign prostatic hyperplasia revealed that it sedimented in the region of 8S, and steroid specificity studies confirmed that the binding to estrogen receptor was estrogen-specific. Sucrose 0-7 estrogen receptor 1 Homo sapiens 33-50 6191047-7 1983 Sucrose gradient analysis of the estrogen receptor of benign prostatic hyperplasia revealed that it sedimented in the region of 8S, and steroid specificity studies confirmed that the binding to estrogen receptor was estrogen-specific. Sucrose 0-7 estrogen receptor 1 Homo sapiens 194-211 6173208-2 1982 In sucrose gradient ultracentrifugation (10-30% w/v, 0.4 M KCl), the cytosol estrogen receptor complex, which migrates with a coefficient of sedimentation of 4.5 S, is shifted to 7.4 S when bound to the estrogen receptor monoclonal antibody. Sucrose 3-10 estrogen receptor 1 Homo sapiens 203-220 7314260-10 1981 Sucrose gradient centrifugation showed that cytoplasmic ER of colorectal cancer sedimented at 3 S in the absence of protease inhibitors and at 4.5 S in the presence of 1 mM phenylmethylsulphonyl fluoride (PMSF) both in low and in high ionic strength. Sucrose 0-7 estrogen receptor 1 Homo sapiens 56-58 7240250-5 1981 The same dissociation constant (Kd) and the same molecular weight (estimated by Sephadex chromatography) and sucrose density behavior for both cytoplasmic and nuclear estrogen receptor are seen in R3 and MCF-7. Sucrose 109-116 estrogen receptor 1 Homo sapiens 167-184 577259-1 1977 Estrogen receptor determination by the sucrose gradient method was applied to 295 tumor tissues of various origins. Sucrose 39-46 estrogen receptor 1 Homo sapiens 0-17 7414375-6 1980 Estrogen receptor content was determined by titration and sucrose gradient methods; both gave results indicating the absence of estrogen receptor in the biopsy specimen. Sucrose 58-65 estrogen receptor 1 Homo sapiens 0-17 466771-3 1979 Similarly, the sedimentation profiles of estrogen-receptor species as determined by sucrose gradient centrifugation were identical. Sucrose 84-91 estrogen receptor 1 Homo sapiens 41-58