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Molecular modeling, mutational analysis and steroid specificity of the ligand binding pocket of mPRalpha (PAQR7): Shared ligand binding with AdipoR1 and its structural basis.
Kelder J, Pang Y, Dong J, Schaftenaar G, Thomas P. Kelder J, et al. J Steroid Biochem Mol Biol. 2022 May;219:106082. doi: 10.1016/j.jsbmb.2022.106082. Epub 2022 Feb 18. J Steroid Biochem Mol Biol. 2022. PMID: 35189329 Free article.
This is supported by experiments showing 100 M Zn(2+) addition restored [(3)H]-progesterone binding of the Q206R mutant to levels in WT mPRalpha and increased [(3)H]-progesterone binding to mPRgamma and AdipoR1 which have arginine residues in this region. The model predict …
This is supported by experiments showing 100 M Zn(2+) addition restored [(3)H]-progesterone binding of the Q206R mutant to levels in WT mPRa …
Expression, purification, crystallization, and preliminary X-ray crystallographic studies of the human adiponectin receptors, AdipoR1 and AdipoR2.
Tanabe H, Motoyama K, Ikeda M, Wakiyama M, Terada T, Ohsawa N, Hosaka T, Hato M, Fujii Y, Nakamura Y, Ogasawara S, Hino T, Murata T, Iwata S, Okada-Iwabu M, Iwabu M, Hirata K, Kawano Y, Yamamoto M, Kimura-Someya T, Shirouzu M, Yamauchi T, Kadowaki T, Yokoyama S. Tanabe H, et al. J Struct Funct Genomics. 2015 Mar;16(1):11-23. doi: 10.1007/s10969-014-9192-z. Epub 2015 Jan 10. J Struct Funct Genomics. 2015. PMID: 25575462 Free PMC article.
The full-length human AdipoR1 and a series of N-terminally truncated mutants of human AdipoR1 and AdipoR2 were expressed in insect cells. ...The purified AdipoR1delta88 and AdipoR2delta99 proteins were characterized by thermostability assays with 7-diethylamino-3-(4 …
The full-length human AdipoR1 and a series of N-terminally truncated mutants of human AdipoR1 and AdipoR2 were expressed in in …
Dimerization of adiponectin receptor 1 is inhibited by adiponectin.
Kosel D, Heiker JT, Juhl C, Wottawah CM, Blüher M, Mörl K, Beck-Sickinger AG. Kosel D, et al. J Cell Sci. 2010 Apr 15;123(Pt 8):1320-8. doi: 10.1242/jcs.057919. Epub 2010 Mar 23. J Cell Sci. 2010. PMID: 20332107
By mutating both glycine residues to phenylalanine or glutamic acid, we were able to modulate the dimerization of AdipoR1, implicating a role for the GxxxG motif in AdipoR1 dimerization. ...Accordingly, this is the first direct read-out signal of adiponectin …
By mutating both glycine residues to phenylalanine or glutamic acid, we were able to modulate the dimerization of AdipoR1, imp …
Impacts of Nonsynonymous Single Nucleotide Polymorphisms of Adiponectin Receptor 1 Gene on Corresponding Protein Stability: A Computational Approach.
Saleh MA, Solayman M, Paul S, Saha M, Khalil MI, Gan SH. Saleh MA, et al. Biomed Res Int. 2016;2016:9142190. doi: 10.1155/2016/9142190. Epub 2016 May 15. Biomed Res Int. 2016. PMID: 27294143 Free PMC article.
Despite the reported association of adiponectin receptor 1 (ADIPOR1) gene mutations with vulnerability to several human metabolic diseases, there is lack of computational analysis on the functional and structural impacts of single nucleotide polymorphisms (SNPs) of …
Despite the reported association of adiponectin receptor 1 (ADIPOR1) gene mutations with vulnerability to several human metabo …
Evolution of human genes encoding cell surface receptors involved in the regulation of appetite: an analysis based on the phylostratigraphic age and divergence indexes.
Ignatieva EV, Lashin SA, Mustafin ZS, Kolchanov NA. Ignatieva EV, et al. Vavilovskii Zhurnal Genet Selektsii. 2023 Dec;27(7):829-838. doi: 10.18699/VJGB-23-96. Vavilovskii Zhurnal Genet Selektsii. 2023. PMID: 38213702 Free PMC article.
Cell surface receptors are transmembrane proteins that interact with molecules (ligands) located outside the cell. This interaction activates signal transduction pathways in the cell. A large number of exogenous ligands of various origins, including drugs, are known …
Cell surface receptors are transmembrane proteins that interact with molecules (ligands) located outside the cell. This interaction a …