Cited by 302Steroid Chemistry and BiochemistryEstrogen and related hormone effectsAdrenal Hormones and Disorders

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Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA

Peltoketo, H., Isomaa, V., Mäentausta, O., Vihko, R.·1988·FEBS Letters

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Abstract

cDNA clones for 17 beta-hydroxysteroid dehydrogenase (17-HSD; EC 1.1.1.62) were isolated from a placental lambda gt11 expression library using polyclonal antibodies against placental 17-HSD. The largest cDNA contained 1325 nucleotides, consisting of a short 5'-noncoding segment, a coding segment of 987 nucleotides terminated by a TAA codon, and a 329 nucleotide long 3'-noncoding segment. The open reading frame encoded a polypeptide of 327 amino acid residues with a predicted Mr of 34853. The amino acid sequence of 23 N-terminal amino acids determined from purified 17-HSD agreed with the sequence deduced from cDNA. The deduced amino acid sequence also contained two peptides previously characterized from the proposed catalytic area of placental 17-HSD.

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DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
[2] New M13 vectors for cloning
Messing, J. W. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)01005-8 · Cited by 5,240
Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
Kozak, M. (1986) · Cell · doi:10.1016/0092-8674(86)90762-2 · Cited by 4,741
Prediction of protein antigenic determinants from amino acid sequences.
Hopp, T. P., & Woods, K. R. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3824 · Cited by 3,726
DNA sequence analysis with a modified bacteriophage T7 DNA polymerase.
Tabor, S., & Richardson, C. C. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.14.4767 · Cited by 2,224
Phosphorylation-Dephosphorylation of Enzymes
Krebs, E. G., & Beavo, J. A. (1979) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.48.070179.004423 · Cited by 2,219
Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
Bause, E. (1983) · Biochemical Journal · doi:10.1042/bj2090331 · Cited by 605
Induction of Human Endometrial Estradiol Dehydrogenase by Progestins
Tseng, L., & Gurpide, E. (1975) · Endocrinology · doi:10.1210/endo-97-4-825 · Cited by 301
Sequence at the 3′ end of globin mRNA shows homology with immunoglobulin light chain mRNA
Proudfoot, N. J., & Brownlee, G. G. (1974) · Nature · doi:10.1038/252359a0 · Cited by 257
Identification of hormone-interacting amino acid residues within the steroid-binding domain of the glucocorticoid receptor in relation to other steroid hormone receptors.
Carlstedt‐Duke, J., Strömstedt, P. E., Persson, B., Cederlund, E., Gustafsson, J.-Α., & Jörnvall, H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68720-4 · Cited by 122

Show all 26 references

Research works printed but not linked: 5

Tseng L., 1980, Advances in Steroid Hormone Research, 329
Neumannova M., 1985, Obstet. Gynecol., 66, 695
Fournier S., 1985, Cancer Res., 45, 2895
Huynh T.V., 1985, DNA Cloning: A Practical Approach 1, 49
Engel L.L., 1974, Recent Prog. Horm. Res., 30, 139

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Self-citation
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Authors: Peltoketo, H., Isomaa, V., Mäentausta, O., & Vihko, R.
Affiliations: University of Oulu (FI)
Corresponding author: Peltoketo, H.
ORCID: Peltoketo, H.
Venue: FEBS Letters
Publisher: Wiley
Published: 1988-10-24
Volume: 239
Issue: 1
Pages: 73-77
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/0014-5793(88)80548-9
OpenAlex: W2073005394
Cited by: 294
References: 26
Citations by year: 2025: 2 · 2020: 1 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 4 · 2013: 1 · 2012: 3
FWCI: 4.22
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4743 d)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Topics: Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
Keywords: 17β-hydroxysteroid dehydrogenase, placenta, cDNA cloning, amino acid sequence, open reading frames, N-terminal sequence, steroid metabolism
MeSH terms: Amino Acid Sequence, Base Sequence, Cloning, Molecular, DNA, Female, Humans, Molecular Sequence Data, Placenta, Pregnancy, Protein Conformation, 17-Hydroxysteroid Dehydrogenases, Restriction Mapping

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Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA

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