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Items: 1 to 20 of 151

1.

RGS proteins determine signaling specificity of Gq-coupled receptors.

Xu X, Zeng W, Popov S, Berman DM, Davignon I, Yu K, Yowe D, Offermanns S, Muallem S, Wilkie TM.

J Biol Chem. 1999 Feb 5;274(6):3549-56.

2.

The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling.

Zeng W, Xu X, Popov S, Mukhopadhyay S, Chidiac P, Swistok J, Danho W, Yagaloff KA, Fisher SL, Ross EM, Muallem S, Wilkie TM.

J Biol Chem. 1998 Dec 25;273(52):34687-90.

3.
5.

Lack of receptor-selective effects of either RGS2, RGS3 or RGS4 on muscarinic M3- and gonadotropin-releasing hormone receptor-mediated signalling through G alpha q/11.

Karakoula A, Tovey SC, Brighton PJ, Willars GB.

Eur J Pharmacol. 2008 Jun 10;587(1-3):16-24. doi: 10.1016/j.ejphar.2008.03.047. Epub 2008 Apr 4.

PMID:
18457830
6.

Application of RGS box proteins to evaluate G-protein selectivity in receptor-promoted signaling.

Hains MD, Siderovski DP, Harden TK.

Methods Enzymol. 2004;389:71-88. Review.

PMID:
15313560
7.
8.

Involvement of RhoA and its interaction with protein kinase C and Src in CCK-stimulated pancreatic acini.

Nozu F, Tsunoda Y, Ibitayo AI, Bitar KN, Owyang C.

Am J Physiol. 1999 Apr;276(4 Pt 1):G915-23.

9.

RGS3 is a GTPase-activating protein for g(ialpha) and g(qalpha) and a potent inhibitor of signaling by GTPase-deficient forms of g(qalpha) and g(11alpha).

Scheschonka A, Dessauer CW, Sinnarajah S, Chidiac P, Shi CS, Kehrl JH.

Mol Pharmacol. 2000 Oct;58(4):719-28.

10.

Characterization and comparison of RGS2 and RGS4 as GTPase-activating proteins for m2 muscarinic receptor-stimulated G(i).

Cladman W, Chidiac P.

Mol Pharmacol. 2002 Sep;62(3):654-9. Erratum in: Mol Pharmacol 2002 Oct;62(4):967.

11.

Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling.

Tu Y, Wilkie TM.

Methods Enzymol. 2004;389:89-105. Review.

PMID:
15313561
12.

Promiscuous coupling of receptors to Gq class alpha subunits and effector proteins in pancreatic and submandibular gland cells.

Xu X, Croy JT, Zeng W, Zhao L, Davignon I, Popov S, Yu K, Jiang H, Offermanns S, Muallem S, Wilkie TM.

J Biol Chem. 1998 Oct 16;273(42):27275-9.

14.

Polarity exchange at the interface of regulators of G protein signaling with G protein alpha-subunits.

Wieland T, Bahtijari N, Zhou XB, Kleuss C, Simon MI.

J Biol Chem. 2000 Sep 15;275(37):28500-6.

15.

Alternate coupling of receptors to Gs and Gi in pancreatic and submandibular gland cells.

Luo X, Zeng W, Xu X, Popov S, Davignon I, Wilkie TM, Mumby SM, Muallem S.

J Biol Chem. 1999 Jun 18;274(25):17684-90.

16.

G protein selectivity is a determinant of RGS2 function.

Heximer SP, Srinivasa SP, Bernstein LS, Bernard JL, Linder ME, Hepler JR, Blumer KJ.

J Biol Chem. 1999 Nov 26;274(48):34253-9.

17.

CCK, carbachol, and bombesin activate distinct PLC-beta isoenzymes via Gq/11 in rat pancreatic acinar membranes.

Piiper A, Stryjek-Kaminska D, Klengel R, Zeuzem S.

Am J Physiol. 1997 Jan;272(1 Pt 1):G135-40.

PMID:
9038886
18.

Palmitoylation regulates regulator of G-protein signaling (RGS) 16 function. II. Palmitoylation of a cysteine residue in the RGS box is critical for RGS16 GTPase accelerating activity and regulation of Gi-coupled signalling.

Osterhout JL, Waheed AA, Hiol A, Ward RJ, Davey PC, Nini L, Wang J, Milligan G, Jones TL, Druey KM.

J Biol Chem. 2003 May 23;278(21):19309-16. Epub 2003 Mar 17.

20.

Palmitoylation regulates regulators of G-protein signaling (RGS) 16 function. I. Mutation of amino-terminal cysteine residues on RGS16 prevents its targeting to lipid rafts and palmitoylation of an internal cysteine residue.

Hiol A, Davey PC, Osterhout JL, Waheed AA, Fischer ER, Chen CK, Milligan G, Druey KM, Jones TL.

J Biol Chem. 2003 May 23;278(21):19301-8. Epub 2003 Mar 17.

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