ArticleJournal of molecular neuroscience : MN2011
The triplet puzzle of homologies in receptor heteromers exists also in other types of protein-protein interactions.
Article in Journal of molecular neuroscience : MN, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 10 citations in OpenAlex.
- The G protein-coupled receptor heterodimer network (GPCR-HetNet) and its hub components.International journal of molecular sciences · 2014Article
- Moonlighting proteins and protein-protein interactions as neurotherapeutic targets in the G protein-coupled receptor field.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Review
- Integrin triplets of marine sponges in the murine and human MHCI-CD8 interface and in the interface of human neural receptor heteromers and subunits.SpringerPlus · 2013Article
- Design, synthesis and biological evaluation of bivalent ligands against A(1)-D(1) receptor heteromers.Acta pharmacologica Sinica · 2013Article
- Integrin triplets of marine sponges in human brain receptor heteromers.Journal of molecular neuroscience : MN · 2012Article
- On the origin of the triplet puzzle of homologies in receptor heteromers: Toll-like receptor triplets in different types of receptors.Journal of neural transmission (Vienna, Austria : 1996) · 2012Article
- On the origin of the triplet puzzle of homologies in receptor heteromers: immunoglobulin triplets in different types of receptors.Journal of molecular neuroscience : MN · 2012Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Based on our theory, we point out main triplets of amino acid residues in the GABAB1 receptor, found in the central and peripheral nervous system, which seem to be critical for both receptor heterodimerization and chemokine binding. The obtained results suggest that these triplets may "guide-and-clasp" protein-protein interactions playing a role, e.g., in neuroinflammation disorders.
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Registered trials
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