ArticleBiophysical journal2003
Solution structure of the tachykinin peptide eledoisin.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 26 citations in OpenAlex.
- Novel Pituitary Actions of TAC4 Gene Products in Teleost.International journal of molecular sciences · 2021Article
- Characterization of structure, dynamics, and detergent interactions of the anti-HIV chemokine variant 5P12-RANTES.Biophysical journal · 2013Article
- Structural heterogeneity of doubly-charged peptide b-ions.Journal of the American Society for Mass Spectrometry · 2011Article
- Membrane catalysis of peptide-receptor binding.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Membrane-Induced Structure of Scyliorhinin I: A Dual NK1/NK2 Agonist.Biophysical journal · 2005Article
- Three-dimensional structure of the mammalian tachykinin peptide neurokinin A bound to lipid micelles.Biophysical journal · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Both the aqueous and the lipid-induced structure of eledoisin, an undecapeptide of mollusk origin, have been studied by two-dimensional proton nuclear magnetic resonance spectroscopy and distance geometry calculations. Unambiguous nuclear magnetic resonance assignments of protons have been made with the aid of correlation spectroscopy experiments and nuclear Overhauser effect spectroscopy experiments. The distance constraints obtained from the nuclear magnetic resonance data have been utilized in a distance geometry algorithm to generate a family of structures, which have been refined using restrained energy minimization and dynamics. These data show that, while in water and dimethyl sulfoxide, eledoisin prefers to be in an extended chain conformation, whereas in the presence of perdeuterated dodecylphosphocholine micelles, a membrane model system, helical conformation is induced in the central core and C-terminal region (K4-M11) of the peptide. N terminus, though less defined, also displays some degree of order and a possible turn structure. The conformation adopted by eledoisin in the presence of dodecylphosphocholine micelles is similar to the structural motif typical of neurokinin-2 selective agonists and with that reported for kassinin in hydrophobic environment.
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Registered trials
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