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Items: 1 to 20 of 97

1.

Defining Structure-Functional Selectivity Relationships (SFSR) for a Class of Non-Catechol Dopamine D1 Receptor Agonists.

Martini ML, Liu J, Ray C, Yu X, Huang XP, Urs A, Urs N, McCorvy JD, Caron MG, Roth BL, Jin J.

J Med Chem. 2019 Apr 11;62(7):3753-3772. doi: 10.1021/acs.jmedchem.9b00351. Epub 2019 Mar 27.

PMID:
30875219
2.

Identification of G protein-biased agonists that fail to recruit β-arrestin or promote internalization of the D1 dopamine receptor.

Conroy JL, Free RB, Sibley DR.

ACS Chem Neurosci. 2015 Apr 15;6(4):681-92. doi: 10.1021/acschemneuro.5b00020. Epub 2015 Feb 20.

3.

Structure-functional selectivity relationship studies of β-arrestin-biased dopamine D₂ receptor agonists.

Chen X, Sassano MF, Zheng L, Setola V, Chen M, Bai X, Frye SV, Wetsel WC, Roth BL, Jin J.

J Med Chem. 2012 Aug 23;55(16):7141-53. doi: 10.1021/jm300603y. Epub 2012 Aug 13.

4.

Synthesis and Pharmacological Evaluation of Noncatechol G Protein Biased and Unbiased Dopamine D1 Receptor Agonists.

Wang P, Felsing DE, Chen H, Raval SR, Allen JA, Zhou J.

ACS Med Chem Lett. 2019 Apr 5;10(5):792-799. doi: 10.1021/acsmedchemlett.9b00050. eCollection 2019 May 9.

PMID:
31098001
5.

Analysis of functional selectivity through G protein-dependent and -independent signaling pathways at the adrenergic α(2C) receptor.

Kurko D, Kapui Z, Nagy J, Lendvai B, Kolok S.

Brain Res Bull. 2014 Aug;107:89-101. doi: 10.1016/j.brainresbull.2014.07.005. Epub 2014 Jul 29.

PMID:
25080296
6.

Functional selectivity of allosteric interactions within G protein-coupled receptor oligomers: the dopamine D1-D3 receptor heterotetramer.

Guitart X, Navarro G, Moreno E, Yano H, Cai NS, Sánchez-Soto M, Kumar-Barodia S, Naidu YT, Mallol J, Cortés A, Lluís C, Canela EI, Casadó V, McCormick PJ, Ferré S.

Mol Pharmacol. 2014 Oct;86(4):417-29. doi: 10.1124/mol.114.093096. Epub 2014 Aug 5.

7.

Discovery of G Protein-Biased D2 Dopamine Receptor Partial Agonists.

Chen X, McCorvy JD, Fischer MG, Butler KV, Shen Y, Roth BL, Jin J.

J Med Chem. 2016 Dec 8;59(23):10601-10618. Epub 2016 Nov 16.

8.

Impaired β-arrestin recruitment and reduced desensitization by non-catechol agonists of the D1 dopamine receptor.

Gray DL, Allen JA, Mente S, O'Connor RE, DeMarco GJ, Efremov I, Tierney P, Volfson D, Davoren J, Guilmette E, Salafia M, Kozak R, Ehlers MD.

Nat Commun. 2018 Feb 14;9(1):674. doi: 10.1038/s41467-017-02776-7.

9.

D2 Dopamine Receptor G Protein-Biased Partial Agonists Based on Cariprazine.

Shen Y, McCorvy JD, Martini ML, Rodriguiz RM, Pogorelov VM, Ward KM, Wetsel WC, Liu J, Roth BL, Jin J.

J Med Chem. 2019 May 9;62(9):4755-4771. doi: 10.1021/acs.jmedchem.9b00508. Epub 2019 Apr 18.

PMID:
30964661
10.

Receptor, Ligand and Transducer Contributions to Dopamine D2 Receptor Functional Selectivity.

Peterson SM, Pack TF, Caron MG.

PLoS One. 2015 Oct 30;10(10):e0141637. doi: 10.1371/journal.pone.0141637. eCollection 2015.

11.

Discovery of β-arrestin-biased dopamine D2 ligands for probing signal transduction pathways essential for antipsychotic efficacy.

Allen JA, Yost JM, Setola V, Chen X, Sassano MF, Chen M, Peterson S, Yadav PN, Huang XP, Feng B, Jensen NH, Che X, Bai X, Frye SV, Wetsel WC, Caron MG, Javitch JA, Roth BL, Jin J.

Proc Natl Acad Sci U S A. 2011 Nov 8;108(45):18488-93. doi: 10.1073/pnas.1104807108. Epub 2011 Oct 24.

12.

Detailed analysis of biased histamine H₄ receptor signalling by JNJ 7777120 analogues.

Nijmeijer S, Vischer HF, Sirci F, Schultes S, Engelhardt H, de Graaf C, Rosethorne EM, Charlton SJ, Leurs R.

Br J Pharmacol. 2013 Sep;170(1):78-88. doi: 10.1111/bph.12117.

13.

SKF-83959 is not a highly-biased functionally selective D1 dopamine receptor ligand with activity at phospholipase C.

Lee SM, Kant A, Blake D, Murthy V, Boyd K, Wyrick SJ, Mailman RB.

Neuropharmacology. 2014 Nov;86:145-54. doi: 10.1016/j.neuropharm.2014.05.042. Epub 2014 Jun 12.

14.

Split luciferase-based assay for simultaneous analyses of the ligand concentration- and time-dependent recruitment of β-arrestin2.

Littmann T, Buschauer A, Bernhardt G.

Anal Biochem. 2019 May 15;573:8-16. doi: 10.1016/j.ab.2019.02.023. Epub 2019 Mar 8.

PMID:
30853375
15.

Induction of cardiac fibrosis by β-blocker in G protein-independent and G protein-coupled receptor kinase 5/β-arrestin2-dependent Signaling pathways.

Nakaya M, Chikura S, Watari K, Mizuno N, Mochinaga K, Mangmool S, Koyanagi S, Ohdo S, Sato Y, Ide T, Nishida M, Kurose H.

J Biol Chem. 2012 Oct 12;287(42):35669-77. doi: 10.1074/jbc.M112.357871. Epub 2012 Aug 10.

16.

Molecular determinants of biased agonism at the dopamine D₂ receptor.

Weichert D, Banerjee A, Hiller C, Kling RC, Hübner H, Gmeiner P.

J Med Chem. 2015 Mar 26;58(6):2703-17. doi: 10.1021/jm501889t. Epub 2015 Mar 12.

PMID:
25734236
17.

Biased Ligands of G Protein-Coupled Receptors (GPCRs): Structure-Functional Selectivity Relationships (SFSRs) and Therapeutic Potential.

Tan L, Yan W, McCorvy JD, Cheng J.

J Med Chem. 2018 Nov 21;61(22):9841-9878. doi: 10.1021/acs.jmedchem.8b00435. Epub 2018 Jul 10.

PMID:
29939744
18.

Selective engagement of G protein coupled receptor kinases (GRKs) encodes distinct functions of biased ligands.

Zidar DA, Violin JD, Whalen EJ, Lefkowitz RJ.

Proc Natl Acad Sci U S A. 2009 Jun 16;106(24):9649-54. doi: 10.1073/pnas.0904361106. Epub 2009 Jun 2.

19.

Structure-activity relationship studies of functionally selective kappa opioid receptor agonists that modulate ERK 1/2 phosphorylation while preserving G protein over βarrestin2 signaling bias.

Lovell KM, Frankowski KJ, Stahl EL, Slauson SR, Yoo E, Prisinzano TE, Aubé J, Bohn LM.

ACS Chem Neurosci. 2015 Aug 19;6(8):1411-9. doi: 10.1021/acschemneuro.5b00092. Epub 2015 May 1. Erratum in: ACS Chem Neurosci. 2017 Jul 19;8(7):1628.

20.

Agonism, Antagonism, and Inverse Agonism Bias at the Ghrelin Receptor Signaling.

M'Kadmi C, Leyris JP, Onfroy L, Galés C, Saulière A, Gagne D, Damian M, Mary S, Maingot M, Denoyelle S, Verdié P, Fehrentz JA, Martinez J, Banères JL, Marie J.

J Biol Chem. 2015 Nov 6;290(45):27021-39. doi: 10.1074/jbc.M115.659250. Epub 2015 Sep 11.

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