ArticleJournal of amino acids2013
In silico insights of L-glutamate: structural features in vacuum and in complex with its receptor.
Article in Journal of amino acids, 2013. 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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Who cites it
3 citing papers in PubMed.
- Enzyme-modified microelectrodes for measurement of glutamate: Characterization and applications.Electroanalysis · 2025Article
- Excitatory Amino Acid Transporters (EAATs): Glutamate Transport and Beyond.International journal of molecular sciences · 2019Review
- Protein modeling, molecular network and molecular dynamics study of newly sequenced interleukin-18 (IL-18) gene in Mus musculus.Journal of cellular physiology · 2019Article
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Authors and funding
2 authors.
Funding
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Abstract
Structural properties of the glutamate in vacuum and in complex with its receptor were analyzed. The analysis was focused on global properties, attempting to characterize features such as overall flexibility and common trends in the conformation set. The glutamate, as other ligands in complex with the receptor, adopts a spatial conformation that corresponds to one of the possible molecular equilibrium states in physiological conditions. The glutamate forms an extended structure for all cases, but the energy of the glutamate round out form is lower than the extended glutamate form. The results showed the glutamate as a flexible molecule, which can easily adapt to different interacting environments, and it can be considered as an approximation to address why glutamate interacts with a great number of molecules.
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Registered trials
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