PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2443188-0 1987 Immunological difference between ribonuclease and temperature, time and salt-induced forms of the estrogen receptor detected by a monoclonal antibody. Salts 72-76 estrogen receptor 1 Homo sapiens 98-115 2811364-3 1989 [3H]TA labeled ER from cytosol prepared in low salt buffer without protease inhibitors migrates on 5%, 6%, or 7% nondenaturing PAGE as two discrete forms. Salts 47-51 estrogen receptor 1 Homo sapiens 15-17 2721439-4 1989 A bimodal pattern of ERn was seen, with peaks at 1 and 8 h. Further biochemical analysis of uterine samples showed that both peaks were comprised of similar levels of salt-resistant ERn forms. Salts 167-171 estrogen receptor 1 Homo sapiens 182-185 7240250-6 1981 Estrogen receptor complexes were activated by salt and nucleotide and translocated to the nucleus equivalently in R3 and MCF-7. Salts 46-50 estrogen receptor 1 Homo sapiens 0-17 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. Salts 66-70 estrogen receptor 1 Homo sapiens 13-30 7329060-0 1981 Salt-induced transformation of the human myometrial estrogen receptor. Salts 0-4 estrogen receptor 1 Homo sapiens 52-69 2443525-7 1987 Only 50-60% of the 150 mM ER isoform was eluted at a lower salt concentration. Salts 59-63 estrogen receptor 1 Homo sapiens 26-28 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. Salts 67-71 estrogen receptor 1 Homo sapiens 12-29 3840166-2 1985 The binding constant of estrogen receptor-DNA interaction was determined by analysis of the exponential elution profile of the estrogen receptor from DNA-Sepharose columns using Tris buffer at a constant salt concentration. Salts 204-208 estrogen receptor 1 Homo sapiens 24-41 6362861-4 1984 The product of estrogen receptor cleavage sedimented at approximately 4S in low-salt gradients and at 3 to 4S in high-salt gradients. Salts 80-84 estrogen receptor 1 Homo sapiens 15-32 6362861-4 1984 The product of estrogen receptor cleavage sedimented at approximately 4S in low-salt gradients and at 3 to 4S in high-salt gradients. Salts 118-122 estrogen receptor 1 Homo sapiens 15-32 7228867-9 1981 Estrogen receptor is activated by salt and nucleotide in both MCF-7 and R27; however, the extent of activation is much higher in MCF-7 than R27. Salts 34-38 estrogen receptor 1 Homo sapiens 0-17 429374-9 1979 Salt-extracted nuclear estrogen receptor was shown to partially aggregate to fast sedimenting species of heterogeneous size when sedimented in gradients containing low salt concentrations. Salts 0-4 estrogen receptor 1 Homo sapiens 23-40 429374-9 1979 Salt-extracted nuclear estrogen receptor was shown to partially aggregate to fast sedimenting species of heterogeneous size when sedimented in gradients containing low salt concentrations. Salts 168-172 estrogen receptor 1 Homo sapiens 23-40 26476919-4 2016 We found that the coating of AuNPs with unmodified ERalpha-RNA aptamer (GGGGUCAAGGUGACCCC) makes them resistant to salt-induced aggregation. Salts 115-119 estrogen receptor 1 Homo sapiens 51-58 474283-5 1979 The salt-extracted estrogen receptor isolated from uterine nuclei shows a single, slow dissociating component equal to the slower component of the cytoplasmic biphasic dissociation curve. Salts 4-8 estrogen receptor 1 Homo sapiens 19-36 744052-0 1978 Antiestrogen modulation of the salt-resistant nuclear estrogen receptor. Salts 31-35 estrogen receptor 1 Homo sapiens 54-71 27832947-3 2017 The colloidal AuNPs could be stabilized against a salt-induced aggregation by adding LBD-ERalpha protein. Salts 50-54 estrogen receptor 1 Homo sapiens 89-96 27832947-4 2017 However, with the presence of E2, the specific binding of LBD-ERalpha protein and E2 led to a salt-induced aggregation of AuNPs as seeing from a color change from red to blue. Salts 94-98 estrogen receptor 1 Homo sapiens 62-69 24280273-6 2014 Our results highlighted that parameters like solvent, ER concentration, salt and surfactant concentration, temperature and time deeply modify ER/ERE interaction. Salts 72-76 estrogen receptor 1 Homo sapiens 142-144 26029980-4 2015 Because it is hypothesized that such distinct behaviors may arise from various conformational stabilities and flexibilities, the effect of salt concentration and temperature was studied on the free and estrogen-activated hERalpha and hERbeta. Salts 139-143 estrogen receptor 1 Homo sapiens 221-241 11325520-5 2001 In buffer containing various concentrations of salt, the rate of dissociation of estradiol-occupied ERalpha from F-vitERE was accelerated by increasing salt concentrations. Salts 47-51 estrogen receptor 1 Homo sapiens 100-107 11795466-4 2001 When cells were treated with estradiol and the hormone treatment was maintained during cell homogenization, binding, and washing steps, GST.90 still interacted efficiently with ER, suggesting that ER may form complexes with Hsp90 even after its activation by hormone and salt extraction from nuclei. Salts 271-275 estrogen receptor 1 Homo sapiens 197-199 23382403-9 2013 CONCLUSIONS: We identified strong, consistent associations between ESR1 gene variants and salt sensitivity in men. Salts 90-94 estrogen receptor 1 Homo sapiens 67-71 17266332-8 2007 With these assay schemes, we reaffirmed that (1) ERalpha is more sensitive than ERbeta to base pair change(s) in the consensus ERE, (2) ERalpha and ERbeta form a heterodimer when they bind to the consensus ERE, and (3) the binding stoichiometry of both ERalpha- and ERbeta-ERE complexes is dependent on salt concentration. Salts 303-307 estrogen receptor 1 Homo sapiens 49-56 17266332-8 2007 With these assay schemes, we reaffirmed that (1) ERalpha is more sensitive than ERbeta to base pair change(s) in the consensus ERE, (2) ERalpha and ERbeta form a heterodimer when they bind to the consensus ERE, and (3) the binding stoichiometry of both ERalpha- and ERbeta-ERE complexes is dependent on salt concentration. Salts 303-307 estrogen receptor 1 Homo sapiens 136-143 17266332-8 2007 With these assay schemes, we reaffirmed that (1) ERalpha is more sensitive than ERbeta to base pair change(s) in the consensus ERE, (2) ERalpha and ERbeta form a heterodimer when they bind to the consensus ERE, and (3) the binding stoichiometry of both ERalpha- and ERbeta-ERE complexes is dependent on salt concentration. Salts 303-307 estrogen receptor 1 Homo sapiens 136-143 12503637-6 2002 At physiological conditions (150 mM salt, 37 degrees C) we determined the 17beta-estradiol Kd for ERalpha to be 281 +/- 13 pmol/L. Salts 36-40 estrogen receptor 1 Homo sapiens 98-105 11325520-5 2001 In buffer containing various concentrations of salt, the rate of dissociation of estradiol-occupied ERalpha from F-vitERE was accelerated by increasing salt concentrations. Salts 152-156 estrogen receptor 1 Homo sapiens 100-107 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. Salts 8-12 estrogen receptor 1 Homo sapiens 101-118 9374531-5 1997 Between 225 and 275 mM KCl, binding to the consensus ERE was independent of salt concentration and occurred with an equilibrium dissociation constant (Kd) of 1.8 +/- 0.6 nM, whereas binding to the mutant ERE was not detected at ER concentrations below 100 nM under the same conditions. Salts 76-80 estrogen receptor 1 Homo sapiens 53-55 9374531-8 1997 Unlike the full-length ER, the recombinant DNA binding domain of ER did not discriminate between the consensus and mutated ERE sequences even at buffer salt concentrations greater than 200 mM NaCl, suggesting that ER sequences outside the DNA binding domain may be important in promoting specific binding. Salts 152-156 estrogen receptor 1 Homo sapiens 65-67 9374531-8 1997 Unlike the full-length ER, the recombinant DNA binding domain of ER did not discriminate between the consensus and mutated ERE sequences even at buffer salt concentrations greater than 200 mM NaCl, suggesting that ER sequences outside the DNA binding domain may be important in promoting specific binding. Salts 152-156 estrogen receptor 1 Homo sapiens 65-67 1460605-4 1992 Both, modifications in binding characteristics of ER and cleavage of the native 67 KDa receptor were found to be extremely marked when unsaturated fatty acids were directly added to the high-salt cell extracts. Salts 191-195 estrogen receptor 1 Homo sapiens 50-52 1753379-4 1991 These results indicate the hormone-bound estrogen receptor has no strong preference for single-stranded vs. double-stranded nonspecific DNA, and has a similar conformation when bound to either form of DNA at physiological salt concentrations. Salts 222-226 estrogen receptor 1 Homo sapiens 41-58