ArticleACS omega2017
Unraveling the Stability of Plasma Proteins upon Interaction of Synthesized Androstenedione and Its Derivatives-A Biophysical and Computational Approach.
Article in ACS omega, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed, 24 citations in OpenAlex.
- Metabolomic-based analysis reveals bile acid-mediated ovarian failure induced by low temperature in zebrafish.Zoological research · 2024Article
- Androstenedione (a Natural Steroid and a Drug Supplement): A Comprehensive Review of Its Consumption, Metabolism, Health Effects, and Toxicity with Sex Differences.Molecules (Basel, Switzerland) · 2021Review
- Elucidating the active interaction mechanism of phytochemicals withanolide and withanoside derivatives with human serum albumin.PloS one · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
4-Androstene-3-17-dione (4A), also known as androstenedione, is the key intermediate of steroid metabolism. 5β-Androstane-3-17-dione (5A) and (+)-6-methyl-5β-androstane-3-17-dione (6M) are the steroid derivatives of androstenedione. The interactions of androstenedione and its derivatives with plasma proteins are important in understanding the distribution and bioavailability of these molecules. In our present study, we have studied the binding affinity of androstenedione and its derivatives with plasma proteins such as human serum albumin (HSA) and α1-acid glycoprotein (AGP). Our results showed that the 4A, 5A, and 6M steroid molecules can form stable complexes with HSA and AGP. The affinity of the studied steroid molecules with HSA is high compared to that with AGP, and the binding constants obtained for 4A, 5A, and 6M with HSA are 5.3 ± 2 × 10
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.