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Cited by 488

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Molecular cloning and charcterization of rat estrogen receptor cDNA

Open access
Koike, Satoshi, Sakai, Masaharu, Muramatsu, Masami·1987·Nucleic Acids Research

Abstract

A cDNA clone of rat uterus estrogen receptor (ER) has been isolated and sequenced. This clone contains a complete open reading frame encoding 600 amino acid residues which is 5 and 11 amino acids larger than the corresponding molecules of human and chicken, respectively. The molecular weight of this protein is calculated to be 67,029. When this clone was ligated to the pSV2 vector and transfected into COS7 cells, a protein was produced that had the same affinity to estrogen as rat uterus ER. This sequence shows 88% homology with human ER; 528 amino acids are identical and 14 amino acids are conservative substitutions. The comparison of rat, human and chicken ER sequences indicate the presence of three highly conserved regions suggesting that these regions play important roles in ER function. The putative DNA-binding domain is completely identical in rat, human and chicken. The C-terminal half region which is thought to be the estrogen binding domain is also highly conserved and is rich in hydrophobic amino acid residues. Southern blot analysis of genomic DNA with ER cDNA as a probe has shown that related sequences are present in the genome.

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Metadata

Authors
Koike, S., Sakai, M., & Muramatsu, M.
Venue
Nucleic Acids Research
Published
1987
Volume
15
Issue
6
Pages
2499-2513
ISSN
  • 0305-1048 (ISSN-L)
  • 1362-4962
OpenAlex
W2092049238
Cited by
488
References
1
FWCI
11.89
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Molecular cloning and charcterization of rat estrogen receptor cDNA. https://app.cochat.ai/papers/10.1093/nar/15.6.2499
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Koike, S., Sakai, M., & Muramatsu, M. (1987). Molecular cloning and charcterization of rat estrogen receptor cDNA. Nucleic Acids Research. https://doi.org/10.1093/nar/15.6.2499

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