 Receptors, Amino Acid
"Receptors, Amino Acid" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
| Descriptor ID |
D017459
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| MeSH Number(s) |
D12.776.543.750.720.200
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| Concept/Terms |
Receptors, Amino Acid- Receptors, Amino Acid
- Amino Acid Receptors
- Receptor, Amino Acid
- Amino Acid Receptor
- Receptors, Amino Acids
- Amino Acids Receptors
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Below are MeSH descriptors whose meaning is more general than "Receptors, Amino Acid".
Below are MeSH descriptors whose meaning is more specific than "Receptors, Amino Acid".
This graph shows the total number of publications written about "Receptors, Amino Acid" by people in this website by year, and whether "Receptors, Amino Acid" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 1 | 0 | 1 | | 1995 | 2 | 0 | 2 | | 1996 | 2 | 1 | 3 | | 1997 | 1 | 0 | 1 | | 1998 | 2 | 0 | 2 | | 1999 | 3 | 0 | 3 | | 2000 | 1 | 0 | 1 | | 2001 | 1 | 0 | 1 | | 2003 | 2 | 0 | 2 | | 2004 | 1 | 0 | 1 | | 2005 | 3 | 0 | 3 | | 2009 | 1 | 0 | 1 | | 2020 | 0 | 1 | 1 |
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Below are the most recent publications written about "Receptors, Amino Acid" by people in Profiles.
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Abu Shehab M, Biggar K, Kakadia JH, Dhruv M, Jain B, Nandi P, Nygard K, Jansson T, Gupta MB. Inhibition of decidual IGF-1 signaling in response to hypoxia and leucine deprivation is mediated by mTOR and AAR pathways and increased IGFBP-1 phosphorylation. Mol Cell Endocrinol. 2020 07 15; 512:110865.
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Swain KE, Gonzalez MA, Falke JJ. Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor. Biochemistry. 2009 Oct 06; 48(39):9266-77.
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Winston SE, Mehan R, Falke JJ. Evidence that the adaptation region of the aspartate receptor is a dynamic four-helix bundle: cysteine and disulfide scanning studies. Biochemistry. 2005 Sep 27; 44(38):12655-66.
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Coleman MD, Bass RB, Mehan RS, Falke JJ. Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching. Biochemistry. 2005 May 31; 44(21):7687-95.
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Starrett DJ, Falke JJ. Adaptation mechanism of the aspartate receptor: electrostatics of the adaptation subdomain play a key role in modulating kinase activity. Biochemistry. 2005 Feb 08; 44(5):1550-60.
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Miller AS, Falke JJ. Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor. Biochemistry. 2004 Feb 24; 43(7):1763-70.
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Mehan RS, White NC, Falke JJ. Mapping out regions on the surface of the aspartate receptor that are essential for kinase activation. Biochemistry. 2003 Mar 18; 42(10):2952-9.
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Bornhorst JA, Falke JJ. Quantitative analysis of aspartate receptor signaling complex reveals that the homogeneous two-state model is inadequate: development of a heterogeneous two-state model. J Mol Biol. 2003 Mar 07; 326(5):1597-614.
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Bornhorst JA, Falke JJ. Evidence that both ligand binding and covalent adaptation drive a two-state equilibrium in the aspartate receptor signaling complex. J Gen Physiol. 2001 Dec; 118(6):693-710.
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Bornhorst JA, Falke JJ. Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state. Biochemistry. 2000 Aug 08; 39(31):9486-93.
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