Isolated adrenal cells: ACTH11–24, a competitive antagonist of ACTH1–39 and ACTH1–10
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The first attempts to design ACTH-like peptide antagonists produced peptides that retained the tetrabasic address region but lacked the HFRW message sequence, leading to the development of ACTH [11-24] as a potential receptor antagonist.
“The first attempts to do this resulted in peptides that retained the tetrabasic address region, but lacked the HFRW message sequence. This led to the development of ACTH [11–24] (49, 50) as a potential receptor antagonist.”
From ACTH Antagonists (2016) · cites this paper as [49]
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“This led to the development of ACTH [11–24] (49, 50) as a potential receptor antagonist.”
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- Authors
- Seelig, S., Sayers, G., Schwyzer, R., & Schiller, P.
- Affiliations
- Case Western Reserve University (US)
- ETH Zurich (CH)
- Corresponding author
- Schwyzer, Robert
- ORCID
- Schiller, Peter
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1971-12-15
- Volume
- 19
- Issue
- 3
- Pages
- 232-234
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2054279604
- Cited by
- 68
- References
- 5
- Citations by year
- 2019: 1 · 2017: 2 · 2016: 3 · 2014: 3
- FWCI
- 8.51
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
- Keywords
- ACTH, competitive antagonism, adrenal cells, hormone-receptor binding
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