PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1704480-5 1990 In contrast to other antipeptide GR antibodies, these antibodies recognize and form stable complexes with unactivated and molybdate-stabilized forms of the GR, indicating that neither epitope is occluded when the receptor exists in an oligomeric state. molybdate 122-131 nuclear receptor subfamily 3 group C member 1 Homo sapiens 33-35 12027445-4 2002 Furthermore, accelerated nuclear export of GR was evidenced in digitonin-permeabilized cells treated with ATP and molybdate. molybdate 114-123 nuclear receptor subfamily 3 group C member 1 Homo sapiens 43-45 11867262-1 2002 Transition metal oxyanions, such as molybdate, tungstate and vandadate, have been shown to prevent in vitro hormone-induced activation of the glucocorticoid receptor (GR) by blocking dissociation of the GR/heat shock protein heterocomplex. molybdate 36-45 nuclear receptor subfamily 3 group C member 1 Homo sapiens 142-165 11867262-1 2002 Transition metal oxyanions, such as molybdate, tungstate and vandadate, have been shown to prevent in vitro hormone-induced activation of the glucocorticoid receptor (GR) by blocking dissociation of the GR/heat shock protein heterocomplex. molybdate 36-45 nuclear receptor subfamily 3 group C member 1 Homo sapiens 167-169 9261129-15 1997 Molybdate has the same ability as p23 to stabilize GR heterocomplexes with mammalian hsp90, but GR heterocomplexes with plant hsp90 are stabilized by p23 and not by molybdate. molybdate 0-9 nuclear receptor subfamily 3 group C member 1 Homo sapiens 51-53 2184891-6 1990 Scatchard analysis of the GR exposed to 0.4 M NaCl in the presence of 10 mM molybdate showed the presence of two types of binding sites with apparent dissociation constants of 0.52 +/- 0.07 and 64.1 +/- 16.2 nM, respectively. molybdate 76-85 nuclear receptor subfamily 3 group C member 1 Homo sapiens 26-28 2365690-0 1990 Selective molybdate-directed covalent modification of sulfhydryl groups in the steroid-binding versus the DNA-binding domain of the glucocorticoid receptor. molybdate 10-19 nuclear receptor subfamily 3 group C member 1 Homo sapiens 132-155 2365690-5 1990 When the glucocorticoid receptor is exposed simultaneously to molybdate and peroxide at concentrations that are optimal for receptor stabilization if each agent is present alone, there is an irreversible loss of steroid binding activity. molybdate 62-71 nuclear receptor subfamily 3 group C member 1 Homo sapiens 9-32 1704480-5 1990 In contrast to other antipeptide GR antibodies, these antibodies recognize and form stable complexes with unactivated and molybdate-stabilized forms of the GR, indicating that neither epitope is occluded when the receptor exists in an oligomeric state. molybdate 122-131 nuclear receptor subfamily 3 group C member 1 Homo sapiens 156-158 3517499-4 1986 The 98-100 kdalton phosphoprotein binds steroid and the 90 kdalton phosphoprotein is a structurally different, nonsteroid-binding protein that is bound to the untransformed, molybdate-stabilized glucocorticoid receptor. molybdate 174-183 nuclear receptor subfamily 3 group C member 1 Homo sapiens 195-218 2844180-4 1988 Polyclonal antibodies raised against the purified glucocorticoid receptor-associated hsp90 interact with the molybdate-stabilized 9 S dioxin-receptor complex but not with the 4 S dioxin receptor monomer, as assessed by sedimentation shift analysis on sucrose gradients. molybdate 109-118 nuclear receptor subfamily 3 group C member 1 Homo sapiens 50-73 3450871-0 1987 The effect of including molybdate in the eluting buffer used for DEAE-cellulose chromatography on the quantitation of glucocorticoid receptor transformation. molybdate 24-33 nuclear receptor subfamily 3 group C member 1 Homo sapiens 118-141 3450871-1 1987 This study analyzes the effect of including molybdate in the elution buffers used in DEAE cellulose chromatography on the fraction of glucocorticoid receptor which elutes as the transformed species. molybdate 44-53 nuclear receptor subfamily 3 group C member 1 Homo sapiens 134-157 3712357-0 1986 Molybdate affects glucocorticoid receptor chromatography on DEAE cellulose. molybdate 0-9 nuclear receptor subfamily 3 group C member 1 Homo sapiens 18-41 3712357-1 1986 How molybdate affects the chromatographic behavior of the glucocorticoid receptor on DEAE cellulose was investigated. molybdate 4-13 nuclear receptor subfamily 3 group C member 1 Homo sapiens 58-81 4084540-0 1985 Molybdate-stabilized glucocorticoid receptor: evidence for a receptor heteromer. molybdate 0-9 nuclear receptor subfamily 3 group C member 1 Homo sapiens 21-44 4084540-1 1985 The composition of the molybdate-stabilized glucocorticoid receptor (GR) complex has been investigated with a monoclonal antibody against the steroid-binding Mr 94 000 (94K) GR protein. molybdate 23-32 nuclear receptor subfamily 3 group C member 1 Homo sapiens 44-67 4084540-1 1985 The composition of the molybdate-stabilized glucocorticoid receptor (GR) complex has been investigated with a monoclonal antibody against the steroid-binding Mr 94 000 (94K) GR protein. molybdate 23-32 nuclear receptor subfamily 3 group C member 1 Homo sapiens 69-71 4084540-3 1985 This finding constituted the basis for calculating the number of antibodies bound to the molybdate-stabilized nonactivated GR complex, which has an Mr of 302 000 (302K). molybdate 89-98 nuclear receptor subfamily 3 group C member 1 Homo sapiens 123-125 4084540-6 1985 The possibility of steric hindrance not allowing more than one antibody molecule to bind to the molybdate-stabilized GR complex could be excluded. molybdate 96-105 nuclear receptor subfamily 3 group C member 1 Homo sapiens 117-119 4084540-7 1985 These results suggest that the molybdate-stabilized GR complex with an Mr of 302K only contains one steroid-binding 94K GR molecule and therefore represents a heteromeric complex. molybdate 31-40 nuclear receptor subfamily 3 group C member 1 Homo sapiens 52-54 4084540-7 1985 These results suggest that the molybdate-stabilized GR complex with an Mr of 302K only contains one steroid-binding 94K GR molecule and therefore represents a heteromeric complex. molybdate 31-40 nuclear receptor subfamily 3 group C member 1 Homo sapiens 120-122 6492789-0 1984 Molybdate-sensitive and molybdate-resistant activation-labile glucocorticoid-receptor mutants of the human lymphoid cell line CEM-C7. molybdate 0-9 nuclear receptor subfamily 3 group C member 1 Homo sapiens 62-85 4058426-0 1985 Multiple forms of molybdate-stabilized glucocorticoid-receptor complexes from HeLa cell cytosol. molybdate 18-27 nuclear receptor subfamily 3 group C member 1 Homo sapiens 39-62 4058426-1 1985 The investigation on hydrodynamic parameters of molybdate-stabilized glucocorticoid-receptor complexes from HeLa cell cytosol permitted resolution of four distinct forms. molybdate 48-57 nuclear receptor subfamily 3 group C member 1 Homo sapiens 69-92 4058426-7 1985 On the basis of our findings, it has been concluded that the most likely structure of molybdate-stabilized glucocorticoid-receptor complexes of HeLa cell cytosol can be represented by association of monomers in homodimers, and homotetramers. molybdate 86-95 nuclear receptor subfamily 3 group C member 1 Homo sapiens 107-130 6492789-0 1984 Molybdate-sensitive and molybdate-resistant activation-labile glucocorticoid-receptor mutants of the human lymphoid cell line CEM-C7. molybdate 24-33 nuclear receptor subfamily 3 group C member 1 Homo sapiens 62-85 6824734-4 1983 However, in the presence of heparin (40 micrograms per ml cytosol) the glucocorticoid receptor had a half-life of only 15 min at 25 degrees C. Interestingly, 10 mM molybdate (with or without 5 mM dithiothreitol) greatly inhibited heparin-dependent receptor inactivation at 4 degrees C. Dithiothreitol (alone) significantly stabilized receptor binding in control samples at 4 degrees C, but provided no protection from heparin-dependent receptor inactivation. molybdate 164-173 nuclear receptor subfamily 3 group C member 1 Homo sapiens 71-94 7142206-0 1982 Synergistic effect of molybdate plus dithiothreitol on stabilization, reactivation, and partial purification of the kidney glucocorticoid receptor. molybdate 22-31 nuclear receptor subfamily 3 group C member 1 Homo sapiens 123-146 7317071-0 1981 Physicochemical analysis of reversible molybdate effects on different molecular forms of glucocorticoid receptor. molybdate 39-48 nuclear receptor subfamily 3 group C member 1 Homo sapiens 89-112 500681-0 1979 Molybdate inhibition of glucocorticoid receptor inactivation and transformation. molybdate 0-9 nuclear receptor subfamily 3 group C member 1 Homo sapiens 24-47 500681-3 1979 Both molybdate and tungstate block temperature-dependent transformation of glucocorticoid.receptor complexes to the DNA-binding state, where fluoride and glucose 1-phosphate have no effect. molybdate 5-14 nuclear receptor subfamily 3 group C member 1 Homo sapiens 75-98 500681-7 1979 These observations support the proposal that molybdate and tungstate are interacting through a reversible association with the glucocorticoid receptor itself. molybdate 45-54 nuclear receptor subfamily 3 group C member 1 Homo sapiens 127-150