 Receptors, Adrenergic, beta-1
"Receptors, Adrenergic, beta-1" 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.
A subclass of beta-adrenergic receptors (RECEPTORS, ADRENERGIC, BETA). The adrenergic beta-1 receptors are equally sensitive to EPINEPHRINE and NOREPINEPHRINE and bind the agonist DOBUTAMINE and the antagonist METOPROLOL with high affinity. They are found in the HEART, juxtaglomerular cells, and in the central and peripheral nervous systems.
| Descriptor ID |
D018342
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| MeSH Number(s) |
D12.776.543.750.069.300.300.340.100 D12.776.543.750.100.150.300.340.700 D12.776.543.750.720.330.300.340.100
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| Concept/Terms |
Receptors, Adrenergic, beta-1- Receptors, Adrenergic, beta-1
- Adrenergic Receptor, beta-1
- Adrenergic Receptor, beta 1
- Receptor, beta-1 Adrenergic
- beta-1 Adrenergic Receptor
- Receptors, beta-1 Adrenergic
- Receptors, beta 1 Adrenergic
- beta-1 Adrenergic Receptors
- Adrenergic Receptors, beta-1
- beta 1 Adrenergic Receptors
- Receptor, Adrenergic, beta-1
- Adrenergic beta-1 Receptors
- Adrenergic beta 1 Receptors
- Receptors, Adrenergic beta-1
- beta-1 Receptors, Adrenergic
- beta 1 Adrenergic Receptor
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Below are MeSH descriptors whose meaning is more general than "Receptors, Adrenergic, beta-1".
- Chemicals and Drugs [D]
- Amino Acids, Peptides, and Proteins [D12]
- Proteins [D12.776]
- Membrane Proteins [D12.776.543]
- Receptors, Cell Surface [D12.776.543.750]
- Receptors, Biogenic Amine [D12.776.543.750.069]
- Receptors, Catecholamine [D12.776.543.750.069.300]
- Receptors, Adrenergic [D12.776.543.750.069.300.300]
- Receptors, Adrenergic, beta [D12.776.543.750.069.300.300.340]
- Receptors, Adrenergic, beta-1 [D12.776.543.750.069.300.300.340.100]
- Receptors, G-Protein-Coupled [D12.776.543.750.100]
- Receptors, Catecholamine [D12.776.543.750.100.150]
- Receptors, Adrenergic [D12.776.543.750.100.150.300]
- Receptors, Adrenergic, beta [D12.776.543.750.100.150.300.340]
- Receptors, Adrenergic, beta-1 [D12.776.543.750.100.150.300.340.700]
- Receptors, Neurotransmitter [D12.776.543.750.720]
- Receptors, Catecholamine [D12.776.543.750.720.330]
- Receptors, Adrenergic [D12.776.543.750.720.330.300]
- Receptors, Adrenergic, beta [D12.776.543.750.720.330.300.340]
- Receptors, Adrenergic, beta-1 [D12.776.543.750.720.330.300.340.100]
Below are MeSH descriptors whose meaning is more specific than "Receptors, Adrenergic, beta-1".
This graph shows the total number of publications written about "Receptors, Adrenergic, beta-1" by people in this website by year, and whether "Receptors, Adrenergic, beta-1" 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 |
|---|
| 1996 | 0 | 1 | 1 | | 2003 | 1 | 1 | 2 | | 2008 | 1 | 0 | 1 | | 2011 | 1 | 0 | 1 | | 2013 | 1 | 1 | 2 | | 2014 | 3 | 1 | 4 | | 2015 | 1 | 0 | 1 |
To return to the timeline, click here.
Below are the most recent publications written about "Receptors, Adrenergic, beta-1" by people in Profiles.
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Gherbi K, May LT, Baker JG, Briddon SJ, Hill SJ. Negative cooperativity across ß1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ß1-adrenoceptor binding conformation. FASEB J. 2015 Jul; 29(7):2859-71.
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Gherbi K, Briddon SJ, Hill SJ. Detection of the secondary, low-affinity ß1 -adrenoceptor site in living cells using the fluorescent CGP 12177 derivative BODIPY-TMR-CGP. Br J Pharmacol. 2014 Dec; 171(23):5431-45.
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Baker JG, Proudman RG, Hill SJ. Salmeterol's extreme ß2 selectivity is due to residues in both extracellular loops and transmembrane domains. Mol Pharmacol. 2015 Jan; 87(1):103-20.
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Baker JG, Proudman RG, Hill SJ. Identification of key residues in transmembrane 4 responsible for the secondary, low-affinity conformation of the human ß1-adrenoceptor. Mol Pharmacol. 2014 May; 85(5):811-29.
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Hutchings CJ, Cseke G, Osborne G, Woolard J, Zhukov A, Koglin M, Jazayeri A, Pandya-Pathak J, Langmead CJ, Hill SJ, Weir M, Marshall FH. Monoclonal anti-ß1-adrenergic receptor antibodies activate G protein signaling in the absence of ß-arrestin recruitment. MAbs. 2014 Jan-Feb; 6(1):246-61.
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Baker JG, Proudman RG, Hill SJ. Impact of polymorphic variants on the molecular pharmacology of the two-agonist conformations of the human ß1-adrenoceptor. PLoS One. 2013; 8(11):e77582.
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Mistry SN, Baker JG, Fischer PM, Hill SJ, Gardiner SM, Kellam B. Synthesis and in vitro and in vivo characterization of highly ß1-selective ß-adrenoceptor partial agonists. J Med Chem. 2013 May 23; 56(10):3852-65.
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Baker JG, Adams LA, Salchow K, Mistry SN, Middleton RJ, Hill SJ, Kellam B. Synthesis and characterization of high-affinity 4,4-difluoro-4-bora-3a,4a-diaza-s-indacene-labeled fluorescent ligands for human ß-adrenoceptors. J Med Chem. 2011 Oct 13; 54(19):6874-87.
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Baker JG, Proudman RG, Hawley NC, Fischer PM, Hill SJ. Role of key transmembrane residues in agonist and antagonist actions at the two conformations of the human beta1-adrenoceptor. Mol Pharmacol. 2008 Nov; 74(5):1246-60.
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Xiao RP, Zhang SJ, Chakir K, Avdonin P, Zhu W, Bond RA, Balke CW, Lakatta EG, Cheng H. Enhanced G(i) signaling selectively negates beta2-adrenergic receptor (AR)--but not beta1-AR-mediated positive inotropic effect in myocytes from failing rat hearts. Circulation. 2003 Sep 30; 108(13):1633-9.
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