PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32807064-7 2021 Docking studies indicated favorable interactions of the di-substituted peptide coumarin derivatives with the Asp 351 and Thr 347 amino acids at the active site of human estrogen receptor. Aspartic Acid 109-112 estrogen receptor 1 Homo sapiens 169-186 29045135-2 2017 Here, we report the co-crystal structure of a helical peptide stabilized by a N-terminal unnatural cross-linked aspartic acid (TD) in complex with the ERalpha ligand binding domain (LBD). Aspartic Acid 112-125 estrogen receptor 1 Homo sapiens 151-158 16179380-8 2006 Mutations of aspartate 351 and leucine 372 can inhibit ERalpha transcriptional activity gained at high concentrations and discriminate concentration-inducible ERalpha function from that induced by estrogen. Aspartic Acid 13-22 estrogen receptor 1 Homo sapiens 55-62 26848530-6 2016 Compared with estrogen receptor (ER)-negative group, ER-positive patients showed elevated alanine, aspartate and glutamate metabolism, decreased glycerolipid catabolism, and enhanced purine metabolism. Aspartic Acid 99-108 estrogen receptor 1 Homo sapiens 53-55 16679488-0 2006 Tamoxifen and raloxifene differ in their functional interactions with aspartate 351 of estrogen receptor alpha. Aspartic Acid 70-79 estrogen receptor 1 Homo sapiens 87-110 16179380-8 2006 Mutations of aspartate 351 and leucine 372 can inhibit ERalpha transcriptional activity gained at high concentrations and discriminate concentration-inducible ERalpha function from that induced by estrogen. Aspartic Acid 13-22 estrogen receptor 1 Homo sapiens 159-166 15965534-3 2005 Previous studies of the chimeric proteins, which incorporate the ligand-binding domain of the human ER, identified Cys 381, Cys 447, Glu 523, His 524 and Asp 538 as possible sites of interactions with cadmium. Aspartic Acid 154-157 estrogen receptor 1 Homo sapiens 100-102 16326832-0 2005 Role of aspartate 351 in transactivation and active conformation of estrogen receptor alpha. Aspartic Acid 8-17 estrogen receptor 1 Homo sapiens 68-91 16326832-6 2005 Furthermore Asp-351 was required not only for the estrogen-dependent conformational change of wild-type ERalpha but also for the constitutive transcriptional activity and ligand-independent active conformation of ERalpha mutant Y537N. Aspartic Acid 12-15 estrogen receptor 1 Homo sapiens 104-111 16326832-6 2005 Furthermore Asp-351 was required not only for the estrogen-dependent conformational change of wild-type ERalpha but also for the constitutive transcriptional activity and ligand-independent active conformation of ERalpha mutant Y537N. Aspartic Acid 12-15 estrogen receptor 1 Homo sapiens 213-220 16326832-7 2005 Similarly, in the orphan nuclear receptor called estrogen-related receptor 3 (ERR3), the replacement of Asp-273 (the corresponding amino acid to Asp-351 in ERalpha) with lysine abolished constitutive transcriptional activity of ERR3 without affecting DNA-binding activity and impaired the ability of the receptor to interact with p160 coactivators. Aspartic Acid 104-107 estrogen receptor 1 Homo sapiens 156-163 16326832-7 2005 Similarly, in the orphan nuclear receptor called estrogen-related receptor 3 (ERR3), the replacement of Asp-273 (the corresponding amino acid to Asp-351 in ERalpha) with lysine abolished constitutive transcriptional activity of ERR3 without affecting DNA-binding activity and impaired the ability of the receptor to interact with p160 coactivators. Aspartic Acid 145-148 estrogen receptor 1 Homo sapiens 156-163 16326832-8 2005 These data suggest a role of Asp-351 in inducing and stabilizing the active conformation of ERalpha, and our results experimentally confirm the concept that Asp-351 in helix 3 interacts with the amide hydrogen of L540 in helix 12 to form a transcriptionally competent surface for binding p160 coactivators. Aspartic Acid 29-32 estrogen receptor 1 Homo sapiens 92-99 16326832-8 2005 These data suggest a role of Asp-351 in inducing and stabilizing the active conformation of ERalpha, and our results experimentally confirm the concept that Asp-351 in helix 3 interacts with the amide hydrogen of L540 in helix 12 to form a transcriptionally competent surface for binding p160 coactivators. Aspartic Acid 157-160 estrogen receptor 1 Homo sapiens 92-99 16191480-3 2006 Asp-351 and Leu-536 participate in hydrogen bond (Asp-351) and hydrophobic (Leu-536) interactions at the start of helix 12 in the ligand-binding domain (LBD) of the ERalpha. Aspartic Acid 0-3 estrogen receptor 1 Homo sapiens 165-172 16191480-3 2006 Asp-351 and Leu-536 participate in hydrogen bond (Asp-351) and hydrophobic (Leu-536) interactions at the start of helix 12 in the ligand-binding domain (LBD) of the ERalpha. Aspartic Acid 50-53 estrogen receptor 1 Homo sapiens 165-172 15604293-4 2004 Mutation of this phosphorylation site to aspartic acid to mimic constitutive phosphorylation blocks acetylation of the K303 ERalpha site and generates an enhanced transcriptional response similar to that seen with the naturally occurring K303R mutant receptor. Aspartic Acid 41-54 estrogen receptor 1 Homo sapiens 124-131 10787412-7 2000 This stabilizing role of Asp-351 could be due to interaction of Asp-351 with the amide group of the peptide bond between Leu-539 and Leu-540 in helix 12 observed in the active conformation of the ERalpha ligand binding domain. Aspartic Acid 64-67 estrogen receptor 1 Homo sapiens 196-203 12790809-4 2003 However, replacement of a conserved tyrosine residue in Helix 12 with alanine or aspartate (Y541A and Y541D), which renders ERalpha constitutively active in mammalian cells, had only a weak stimulatory effect on ligand-independent reporter activation by ERalpha in yeast. Aspartic Acid 81-90 estrogen receptor 1 Homo sapiens 124-131 12790809-4 2003 However, replacement of a conserved tyrosine residue in Helix 12 with alanine or aspartate (Y541A and Y541D), which renders ERalpha constitutively active in mammalian cells, had only a weak stimulatory effect on ligand-independent reporter activation by ERalpha in yeast. Aspartic Acid 81-90 estrogen receptor 1 Homo sapiens 254-261 11159857-13 2001 Using computer-assisted molecular models of ER complexes, we found that the antiestrogenic side chain of 4-OHT weakly interacted with the surface amino acid 351 (aspartate), but the carboxylic acid of GW7604 caused a strong repulsion of aspartate 351. Aspartic Acid 162-171 estrogen receptor 1 Homo sapiens 44-46 11159857-13 2001 Using computer-assisted molecular models of ER complexes, we found that the antiestrogenic side chain of 4-OHT weakly interacted with the surface amino acid 351 (aspartate), but the carboxylic acid of GW7604 caused a strong repulsion of aspartate 351. Aspartic Acid 237-246 estrogen receptor 1 Homo sapiens 44-46 10787412-0 2000 Aspartate 351 of estrogen receptor alpha is not crucial for the antagonist activity of antiestrogens. Aspartic Acid 0-9 estrogen receptor 1 Homo sapiens 17-40 10787412-7 2000 This stabilizing role of Asp-351 could be due to interaction of Asp-351 with the amide group of the peptide bond between Leu-539 and Leu-540 in helix 12 observed in the active conformation of the ERalpha ligand binding domain. Aspartic Acid 25-28 estrogen receptor 1 Homo sapiens 196-203 12496244-0 2003 Modulation of estrogen receptor alpha function and stability by tamoxifen and a critical amino acid (Asp-538) in helix 12. Aspartic Acid 101-104 estrogen receptor 1 Homo sapiens 14-37 11751902-1 2002 Amino acid Asp-351 in the ligand binding domain of estrogen receptor alpha (ERalpha) plays an important role in regulating the estrogen-like activity of selective estrogen receptor modulator-ERalpha complexes. Aspartic Acid 11-14 estrogen receptor 1 Homo sapiens 51-74 11751902-1 2002 Amino acid Asp-351 in the ligand binding domain of estrogen receptor alpha (ERalpha) plays an important role in regulating the estrogen-like activity of selective estrogen receptor modulator-ERalpha complexes. Aspartic Acid 11-14 estrogen receptor 1 Homo sapiens 76-83 11751902-1 2002 Amino acid Asp-351 in the ligand binding domain of estrogen receptor alpha (ERalpha) plays an important role in regulating the estrogen-like activity of selective estrogen receptor modulator-ERalpha complexes. Aspartic Acid 11-14 estrogen receptor 1 Homo sapiens 191-198 11751902-11 2002 These results support the concept that the side chain of raloxifene shields and neutralizes the Asp-351 to produce an antiestrogenic ERalpha complex. Aspartic Acid 96-99 estrogen receptor 1 Homo sapiens 133-140 9219916-4 1997 We have taken a different approach and examined the naturally occurring codon 351 asp --> tyr mutation in the LBD of ER to stimulate the expression of an endogenous target gene. Aspartic Acid 82-85 estrogen receptor 1 Homo sapiens 120-122 9581827-0 1998 The key to the antiestrogenic mechanism of raloxifene is amino acid 351 (aspartate) in the estrogen receptor. Aspartic Acid 73-82 estrogen receptor 1 Homo sapiens 91-108 7476979-1 1995 We previously identified a codon 351 (Asp-->Tyr) mutant estrogen receptor (ER) in a tamoxifen-stimulated human breast tumor line. Aspartic Acid 38-41 estrogen receptor 1 Homo sapiens 59-76 7476979-1 1995 We previously identified a codon 351 (Asp-->Tyr) mutant estrogen receptor (ER) in a tamoxifen-stimulated human breast tumor line. Aspartic Acid 38-41 estrogen receptor 1 Homo sapiens 78-80