ライフサイエンスコーパス: RGS

1 RGS (regulator of G protein signaling) proteins are nega

2 RGS (regulator of G protein signaling) proteins of the R

3 RGS proteins are best understood as negative regulators

4 RGS proteins interact with, and affect the activity of,

5 RGS proteins limit the duration that Galphai subunits re

6 RGS proteins primarily act as GTPase accelerators for ac

7 RGS seldom led to clinician-perceived confusion or distr

8 RGS was perceived as beneficial irrespective of whether

9 RGS-containing RhoGEFs (RGS-RhoGEFs) represent a direct

10 f these small-molecule inhibitors against 12 RGS proteins, as well as against the cysteine-null mutan

11 pan-cancer bioinformatics analysis of the 20 RGS domains with GAP activity revealed hundreds of low-f

12 The 2 most abundant RGS proteins in human and mouse platelets are RGS10 and

13 ve NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Galpha proteins in

14 ai2 (G184S/G184S) mutation that disables all RGS protein/Galphai2 interactions exhibit an unexpectedl

15 y tested multiple mutations representing all RGS GAP subfamilies and sampling both G protein interfac

16 Alternatively, RGS proteins might also have a direct role in regulating

17 Although RGS proteins canonically function as G-protein regulator

18 lated to differential protein dynamics among RGS proteins.

19 flexibility and potency of inhibition among RGS isoforms.

20 targeting conserved cysteine residues among RGS proteins have emerged as potential candidates to inh

21 rs bind to conserved cysteine residues among RGS proteins, we have previously suggested [J. Am.

22 do this, a knock-in mouse that expresses an RGS-insensitive (RGSi) mutant Galphao protein, Galphao(G

23 ective for Galpha (q) Despite only having an RGS domain, responsible for the canonical GTPase activat

24 Pases in the intracellular trafficking of an RGS protein.

25 h the GEF activity of p115-RhoGEF (p115), an RGS-RhoGEF, can be stimulated by Galpha(13), the exact m

26 RGS14 possesses an RGS domain that binds active Galpha(i/o)-GTP subunits to

27 Experiments with pertussis toxin, an RGS domain-deficient mutant of RGS7, and UBO-QIC {L-thre

28 yses and homology modeling of the Galpha and RGS proteins to address their expansion and its potentia

29 ty of Galpha(i2) deficient (Gnai2 (-/-)) and RGS-insensitive Galpha(i2) (Gnai2 (G184S/G184S)) BMDMs.

30 eraction between the cognate GPCR (Mam2) and RGS (Rgs1), mapping the interaction domains.

31 At neuronal synapses, GPCRs, G proteins, and RGS proteins work in coordination to regulate key aspect

32 ctions between activated Galpha subunits and RGS proteins have yielded a substantial number of inhibi

33 signaling enhances the expression of another RGS domain-containing protein, PDZ-RGS3.

34 es the selectivity of commercially available RGS inhibitors and provides insight into the RGS family

35 onte Carlo simulation of the probe for beta- RGS, the activity that is to be administered for a succe

36 ins compatible with the application of beta- RGS.

37 The application of this beta- RGS to neuroendocrine tumors (NET) requires study of the

38 etermines differences in flexibility between RGS isoforms; mutations either increase or decrease prot

39 s and supports a causal relationship between RGS flexibility and the potency of TDZD inhibitors.

40 ongly suggests a causal relationship between RGS protein flexibility and covalent inhibitor potency.

41 the Galpha subunit, a reaction catalyzed by RGS proteins.

42 15%) infants were perceived to be changed by RGS.

43 retained their ability to be deactivated by RGS.

44 nd signal transduction pathways regulated by RGS proteins in addiction and analgesia circuits.

45 ning the selectivity of Galpha regulation by RGS, we examine the catalytic activity of all canonical

46 Mammalian genomes encode 20 canonical RGS and 16 Galpha genes with key roles in physiology and

47 The soybean genome encodes two chimeric RGS proteins with an N-terminal seven transmembrane doma

48 subcellular localization to compartmentalize RGS activity within a cell, thus highlighting their impo

49 phobic motifs in RH outside of the consensus RGS box are critical for this process.

50 cy mutations spread throughout the conserved RGS domain structure with a slight enrichment at positio

51 merization system that enabled us to control RGS localization independent from R7BP in living cells.

52 ated that viruses rescued from the described RGS resembled the parental viruses in biological and rec

53 ne-driven ON-BCs are determined by different RGS concentrations.

54 cs and inhibitor potency for three different RGS proteins.

55 cytes with a Galphai2 mutation that disables RGS protein binding accumulated in the perivascular chan

56 sis and/or motor dysfunction and dyskinesia: RGSs 4, 6, 9, and 10.

57 s to evaluate the contribution of endogenous RGS proteins to the antinociceptive effects of morphine

58 eins from species with or without endogenous RGS.

59 vity, and provide principles for engineering RGS proteins with defined selectivity.

60 ors have been identified; however, enhancing RGS protein function is often more clinically desirable

61 in meningiomas but was still acceptable for RGS, particularly if further research and development ar

62 s that the tracer can still be effective for RGS.

63 Our results strongly support a role for RGS proteins as negative regulators of opioid supraspina

64 ese findings establish an essential role for RGS proteins in B cell chemoattractant signaling and for

65 ical and cell-based methods to assess Galpha-RGS complex formation and Galpha enzymatic activity, we

66 t for the adaptive coevolution of the Galpha:RGS protein pair based on single amino acid substitution

67 ion-based adaptive coevolution of the Galpha:RGS proteins was proposed to enable the loss of RGS in m

68 Both Gbetagamma and Gbeta5-RGS are obligate dimers that are thought to require the

69 The data reveal rules governing RGS-Galpha recognition, the structural basis of its sele

70 extends previous attempts by including GPCR-RGS interactions.

71 In vivo and in silico data confirm that GPCR-RGS interactions can impose an additional layer of regul

72 a regulator of G protein signaling homology (RGS) domain.

73 This study reveals how RGS proteins modulate Galphai2 signaling to facilitate t

74 proteins, it is important to understand how RGS regulates selective GPCR-G protein signaling.

75 he catalytic activity of all canonical human RGS proteins and their selectivity for a complete set of

76 etection and resection during first-in-human RGS.

77 We further show that changes in RGS concentration differentially impact visually guided-

78 is approach was used to correlate changes in RGS localization and activity in the presence or absence

79 terization of cancer-associated mutations in RGS proteins.

80 turally occurring non-synonymous variants in RGS alter signaling.

81 ain GTP bound, and the loss of an individual RGS protein typically enhances chemokine receptor signal

82 leic acid downregulation of IKACh-inhibiting RGS proteins was present at 16 weeks.

83 Moreover, overexpression of Setaria italica RGS in B. distachyon resulted in phenotypes similar to t

84 endrites by varying the concentration of key RGS proteins and measuring the impact on transmission of

85 Among the over 20 known RGS proteins, RGS2 has received increasing interest as a

86 terations in the PX domains of the mammalian RGS-PX proteins, SNX13, SNX14, SNX19, and SNX25, confer

87 Many RGS proteins also bind additional signaling partners tha

88 tional layer of regulation through mediating RGS subcellular localization to compartmentalize RGS act

89 brane anchoring subunit or further modulates RGS proteins to increase their GAP activity.

90 Several small molecule RGS protein inhibitors have been identified; however, en

91 inhibitors display activity toward multiple RGS family members.

92 epresenting species without or with a native RGS, respectively.

93 in SNc DA neurons (RGS6), striatal neurons (RGSs 4 and 9), or microglia (RGS10), modulate key signal

94 Neutrophil RGS proteins establish a threshold for Galpha(i) activat

95 em (RGS) is urgently needed, but to date, no RGS had been described for IDV.

96 an essential role for modulatory actions of RGS proteins in adult cerebellum.

97 rotein cycle is regulated by the activity of RGS proteins.

98 membrane interactions in spatial control of RGS-PX proteins in cell signaling and trafficking.

99 provide a brief overview of the discovery of RGS proteins and of the gradual and continuing discovery

100 understanding of the molecular diversity of RGS proteins that control MOR signaling, their circuit s

101 With hundreds of GPCRs and dozens of RGS proteins, compartmentalization plays a key role in e

102 , we reveal these differences in dynamics of RGS proteins by partitioning the protein structural spac

103 o the suppression of BdGalpha This effect of RGS overexpression depended on its ability to deactivate

104 The study also explores the evolution of RGS-Galpha selectivity through ancestral reconstruction

105 These results reveal the existence of RGS protein homo-oligomers and show regulation of their

106 Lower or higher expression of RGS proteins results in fewer or more nodules, respectiv

107 r findings reveal that a sizable fraction of RGS protein mutations leads to a loss of function throug

108 nd also reveal a potential novel function of RGS proteins as positive regulators of opioid spinal ant

109 g findings on the regulation and function of RGS proteins in models of analgesia and addiction.

110 ss reports on the regulation and function of RGS proteins in models of psychostimulant addiction.

111 n this paper, we report that the R7 group of RGS regulators is controlled by interaction with two pre

112 Selective inhibition of RGS proteins increases G-protein activity and may provid

113 We propose that the interaction of RGS proteins with orphan GPCRs promotes signaling select

114 matically assess the mutational landscape of RGS GAPs in cancer.

115 s may exist which compensate for the loss of RGS in certain plant species.

116 ese results suggest that despite the loss of RGS in many monocots, the G-protein functional networks

117 proteins was proposed to enable the loss of RGS in monocots.

118 To assess if the loss of RGS in specific plants has resulted in altered G-protein

119 We explore the unique mechanisms of RGS inhibition these chemical tools have revealed and hi

120 ressed levels of Galpha or overexpression of RGS showed significant overlap of differentially regulat

121 urface expression and through recruitment of RGS proteins.

122 indings reveal a hitherto overlooked role of RGS proteins as noise suppressors and demonstrate an abi

123 RGS2 is a member of the R4 subfamily of RGS proteins and is unique in that it is selective for G

124 Members of the RZ subfamily of RGS proteins bind to activated Galpha(o), Galpha(z), and

125 Although the R4 subfamily of RGS proteins generally accepts both Galphai/o and Galpha

126 GS7 and RGS9-2 belong to the R7 subfamily of RGS proteins that form macromolecular complexes with R7-

127 entify RGS6, a member of the R7 subfamily of RGS proteins, as a key regulator of GABA(B)R signaling i

128 Septin organization is dependent on RGS protein activity.

129 one Galpha, one Gbeta, three Ggamma, and one RGS protein.

130 In contrast, only one RGS protein, RGS2, is known to be selective for Galphaq/

131 ed RGS4 inhibitors were active against other RGS members, such as RGS14, with comparable or greater p

132 midbrain expression and trafficking of other RGS proteins such as RGS4 and RGS8.

133 In contrast to other RGS proteins, little is known about RZ subfamily structu

134 Analysis of phosphorylated RGS protein identifies specific amino acids that, when p

135 , while G-proteins are widespread in plants, RGS proteins have been reported to be missing from the e

136 vity toward RhoA, these RhoGEFs also possess RGS homology (RH) domains that interact with activated a

137 s, RGS6-Gbeta5, but not RGS4, is the primary RGS modulator of parasympathetic HR regulation and SAN M

138 used with liver NET metastases, the proposed RGS technique is believed to be feasible by injecting an

139 R7 RGS proteins contain several distinct domains and form o

140 Rgs6(-/-) mice is attributable to another R7 RGS protein whose influence on M2R-IKACh signaling is ma

141 rane compartments, dissociated R7BP-bound R7 RGS complexes from Gi/o-gated G protein-regulated inward

142 ane and facilitating Gi/o deactivation by R7 RGS proteins on GIRK channels.

143 ervous system, is mediated exclusively by R7 RGS proteins.

144 and show regulation of their assembly by R7 RGS-binding partners.

145 , a palmitoylated allosteric modulator of R7 RGS proteins that accelerate deactivation of Gi/o class

146 se findings argue that the association of R7 RGS proteins with the membrane environment provides a ma

147 Rs (MOR and D2R) on the G protein bias of R7 RGS proteins.

148 ta5 complexes under allosteric control of R7 RGS-binding protein (R7BP).

149 Mice lacking all R7-RGS subtypes exhibit diverse neurological phenotypes, an

150 nteraction between activated Galpha13 and R7-RGS heterotrimers, indicating that these effector RhoGEF

151 heterotrimeric complexes with Gbeta5 and R7-RGS-binding protein (R7BP) that regulate G protein-coupl

152 with R7-RGS heterotrimers containing any R7-RGS isoform.

153 R7BP-bound R7-RGS/Gbeta5 complexes and Gbetagamma dimers interact nonc

154 Although each R7-RGS subtype forms heterotrimeric complexes with Gbeta5 a

155 regulator of G protein signaling family (R7-RGS) critically regulates nervous system development and

156 hese effector RhoGEFs can engage Galpha13.R7-RGS complexes.

157 Because Galpha13/R7-RGS interaction required R7BP, we analyzed phenotypes of

158 units, several neurological phenotypes of R7-RGS knock-out mice are not readily explained by dysregul

159 d humans bearing mutations in the retinal R7-RGS isoform RGS9-1 have vision deficits.

160 findings provide the first evidence that R7-RGS heterotrimers interact with Galpha13 to augment sign

161 alpha13 because it had not been linked to R7-RGS complexes before.

162 xpands the diversity of functions whereby R7-RGS complexes regulate critical aspects of nervous syste

163 s active or inactive state interacts with R7-RGS heterotrimers containing any R7-RGS isoform.

164 rch for novel proteins that interact with R7-RGS heterotrimers in the mouse brain.

165 odulation occurs by channel assembly with R7-RGS/Gbeta5 complexes under allosteric control of R7 RGS-

166 anistically link the unusual orphan receptor-RGS complex to a major stress mediator, the cAMP system

167 We show that GPR158/179 recruited RGS complexes to the plasma membrane and augmented their

168 ta, and Ggamma subunits and their regulatory RGS (Regulator of G-protein Signaling) protein are conse

169 After injury, the complex gradually releases RGS proteins, limiting platelet activation and providing

170 dulation by the G12 and G13 proteins via RH (RGS homology) containing RhoGEFs.

171 m Gbetagamma to interact with the PDZ-RhoGEF-RGS domain.

172 RGS-containing RhoGEFs (RGS-RhoGEFs) represent a direct link between the G(12) c

173 itment requires Axin and not APC, and Axin's RGS domain plays an important role.

174 nce (NMR) spectroscopy, relaxed grid search (RGS), molecular dynamics (MD) simulations, and quantum m

175 linical utility of rapid genomic sequencing (RGS).

176 ming residue controls flexibility in several RGS isoforms and supports a causal relationship between

177 nd Gbeta5-regulators of G-protein signaling (RGS) complexes.

178 N-terminal regulator of G protein signaling (RGS) domain binds active Galphai/o-GTP, whereas the C-te

179 The regulator of G protein signaling (RGS) domain proteins generally attenuate heterotrimeric

180 xin1 has a regulator of G-protein signaling (RGS) domain that binds adenomatous polyposis coli and Ga

181 x (PX) and regulator of G protein signaling (RGS) domains.

182 leiotropic regulator of G protein signaling (RGS) family member RGS6 suppresses Ras-induced cellular

183 The regulator of G protein signaling (RGS) family of proteins serves critical roles in G prote

184 ers of the regulator of G protein signaling (RGS) family.

185 Regulators of G protein Signaling (RGS) promote deactivation of heterotrimeric G proteins t

186 etics, the regulator of G-protein signaling (RGS) protein family modulates the timing of GIRK activit

187 truncated regulator of G protein signaling (RGS) protein or a Gbetagamma-sequestering domain to a se

188 The regulator of G protein signaling (RGS) protein Sst2 acts by accelerating GTP hydrolysis an

189 ility of a regulator of G protein signaling (RGS) protein to suppress noise.

190 s, and the REGULATOR OF G-PROTEIN SIGNALING (RGS) protein.

191 R7 family regulators of G protein signaling (RGS) proteins (RGS6, RGS7, RGS9, and RGS11) instead of G

192 Regulator of G-protein signaling (RGS) proteins are an integral part of the G-protein netw

193 Regulator of G-protein signaling (RGS) proteins are critical modulators of GPCR activity,

194 Regulators of G protein signaling (RGS) proteins are critical modulators of GPCR signaling

195 The regulator of G-protein signaling (RGS) proteins are key interactors and critical modulator

196 Regulator of G protein signaling (RGS) proteins are multifunctional proteins expressed in

197 Regulator of G protein signaling (RGS) proteins are negative modulators of G protein signa

198 Regulator of G protein signaling (RGS) proteins are negative regulators of G protein-coupl

199 Regulator of G-protein signaling (RGS) proteins are potent inhibitors of heterotrimeric G-

200 Regulator of G protein signaling (RGS) proteins are signal transduction modulators, expres

201 Regulator of G-protein signaling (RGS) proteins classically function as negative modulator

202 Endogenous regulator of G-protein signaling (RGS) proteins have been implicated as key inhibitors of

203 y, several regulator of G protein signaling (RGS) proteins have emerged as critical modulators of PD

204 mid-1990s, regulator of G protein signaling (RGS) proteins have emerged as key regulators of signalin

205 Regulator of G protein signaling (RGS) proteins interact with activated Galpha subunits vi

206 ized that regulators of G protein signaling (RGS) proteins may be involved.

207 Regulators of G-protein signaling (RGS) proteins modulate receptor signaling by binding to

208 Regulators of G-protein signaling (RGS) proteins play a central role in modulating signalin

209 Regulator of G protein signaling (RGS) proteins play essential roles in the regulation of

210 Regulator of G protein signaling (RGS) proteins represent an exciting class of novel drug

211 ntains two Regulator of G-protein Signaling (RGS) proteins RGS7 and RGS11 that directly act on Go and

212 ded by the regulator of G protein signaling (RGS) proteins that deactivate G protein alpha subunits (

213 These regulators of G-protein signaling (RGS) proteins were viewed by many as nodes downstream of

214 ypothesize Regulator of G-Protein Signaling (RGS) proteins, and specifically RGS5, are endogenous rep

215 ruits the regulators of G-protein signaling (RGS) proteins, RGS7 and RGS11, to the dendritic tips of

216 Regulator of G protein signaling (RGS) proteins, whether primarily expressed in SNc DA neu

217 ns and the regulator of G-protein signaling (RGS) proteins, which accelerate the inherent GTPase acti

218 led by the regulator of G protein signaling (RGS) proteins.

219 led by the regulator of G-protein signaling (RGS) proteins.

220 eract with regulator of G protein signaling (RGS) proteins.

221 e with the regulator of G protein signaling (RGS) Sst2, a GTPase-activating protein that dampens pher

222 studied R7 regulator of G protein signaling (RGS)-binding protein (R7BP), a palmitoylated allosteric

223 t disables regulator of G-protein signaling (RGS)-Galpha(i2) interactions accumulate in the bone marr

224 ) 1 and 2, regulator of G protein signaling (RGS)-homology-RhoGEFs (PDZ domain-containing RhoGEF and

225 tion, and regulators of G protein-signaling (RGS) 4 function in knockout mice.

226 ears ago, regulators of G protein-signaling (RGS) proteins have received considerable attention as po

227 tor of G protein-coupled receptor signaling (RGS) domain that attenuates Galphas-coupled G protein-co

228 amily of "regulator of G protein signaling" (RGS) proteins.

229 on of the regulator of G-protein signalling (RGS) 16, and genetic RGS16 reconstitution reverses the e

230 terize the functions of RgsD, one of the six RGS domain proteins present in the human pathogenic fung

231 evidence has revealed key roles for specific RGS proteins in multiple signaling pathways at neuronal

232 highlight the current knowledge of specific RGS proteins (RGS2, RGS4, RGS7, RGS9-2, and RGS14) that

233 ia-associated RhoGEF (LARG), a RhoA-specific RGS-RhoGEF, is required for abscission, the final stage

234 s of SSRIs, but the identity of the specific RGS proteins involved remains unknown.

235 Specifically, RGS proteins bind to activated Galpha subunits in G-prot

236 We also show that SPL/RGS/SHP1 complexes are present in resting platelets wher

237 blocks cAMP-induced dissociation of the SPL/RGS/SHP-1 complex.

238 Thus, we propose that the role of the SPL/RGS/SHP1 complex in platelets is time and context depend

239 ering dephosphorylation and decay of the SPL/RGS/SHP1 complex.

240 g G protein and GPCR selectivity of striatal RGS proteins.

241 R7 subfamily RGS proteins are stabilized by the G-protein subunit Gbe

242 directly act on Go and two adaptor subunits: RGS Anchor Protein (R9AP) and the orphan receptor, GPR17

243 As such, RGS proteins represent novel therapeutic targets in PD.

244 er injection) and (99m)Tc-PSMA-I&S-supported RGS (16 h after injection) were performed in 1 PCa patie

245 maging and therapy) for radioguided surgery (RGS) of small metastatic prostate cancer (PCa) soft-tiss

246 A novel radioguided surgery (RGS) technique exploiting beta- radiation has been propo

247 A novel radioguided surgery (RGS) technique for cerebral tumors using beta(-) radiati

248 molecular level, a reverse-genetics system (RGS) is urgently needed, but to date, no RGS had been de

249 ior performance as a probe for PSMA-targeted RGS and also hint toward the unexpected potential of (99

250 R7BP targets RGS proteins to the plasma membrane and augments their G

251 seven transmembrane domain and a C-terminal RGS box.

252 regulator of Hh-mediated signaling and that RGS proteins are potential targets for novel therapeutic

253 Our results collectively demonstrated that RGS-derived viruses resembled the parental viruses for t

254 istic regression models, the likelihood that RGS was perceived as useful increased 6.7-fold when asso

255 Strikingly, we observed that RGS activity is augmented by membrane recruitment, in an

256 primary end-point-clinician perception that RGS was useful- was met for 154 (77%) of 201 infants.

257 Physicians reported that RGS changed clinical management in 57 (28%) infants, par

258 In this study, we show that RGS protein/Galphai2 interactions are essential for norm

259 Our results show that RGS proteins are widely distributed in the monocot linea

260 The RGS domain of RGS6, known only for its GTPase-activating

261 communication between the GPR motif and the RGS domain upon G protein binding and examined whether R

262 hibitor binding sites and terminating at the RGS/Galpha protein-protein interface.

263 rovide evidence of an essential role for the RGS-containing RhoGEF family in signaling to Rho by Galp

264 erged as potential candidates to inhibit the RGS/Galpha protein-protein interaction and enhance GPCR

265 RGS inhibitors and provides insight into the RGS family members for which drug discovery efforts may

266 eraction required the DEP domain but not the RGS and DHEX domains or the Gbeta5 subunit.

267 acts can be maintained between alpha6 of the RGS domain and Switch III of Galphaq, regions of high se

268 reclinical work suggests that members of the RGS family act by unique mechanisms in specific brain re

269 Since RGS4 is a member of the RGS family of proteins that act to reduce the lifetime o

270 , preclinical work identified members of the RGS family with unique and critical roles in intracellul

271 olecule inhibitors targeting a subset of the RGS proteins.

272 liomas (HGGs) and a feasibility study of the RGS technique in these types of tumor.

273 In terms of feasibility of the RGS technique, we estimated that by administering a 3 MB

274 ight into the mechanism of regulation of the RGS-RhoGEF and broadens our understanding of G protein s

275 We found that the RGS protein Sst2 limits variability in transcription and

276 For example, Galpha(13) binding to the RGS-homology (RH) domains of several RH-RhoGEFs alloster

277 modification of cysteine residues within the RGS domain that are located distal to the Galpha-binding

278 ine residues are highly conserved within the RGS family, many of these inhibitors display activity to

279 although slight differences exist within the RGS homology (RH) bundle subdomain, substrate-binding si

280 conferred by a conserved domain dubbed the "RGS-box." Here, we developed an experimental pipeline to

281 act with activated Galpha subunits via their RGS domains and accelerate the hydrolysis of GTP.

282 Accordingly, these RGS proteins represent novel therapeutic targets for the

283 lineate the structural organization of these RGS-PX proteins, revealing a protein family with a modul

284 ties, thereby supporting the utility of this RGS to study IDV infection biology.

285 information on the biological roles of this RGS-containing family of RhoGEFs in vivo.

286 embryonic fibroblasts defective in all three RGS-containing RhoGEFs.

287 Thus, RGSs 4, 6, 9, and 10 are critical modulators of cell sig

288 y and low likelihood of harm with first-tier RGS of infants in ICUs with diseases of unknown etiology

289 to cholinergic stimulation, possibly due to RGS protein downregulation.

290 In neurons of the striatum, two RGS proteins, RGS7 and RGS9-2, regulate signaling by mu-

291 is mammalian SNX19, which lacks the typical RGS structure but preserves all other domains.

292 In vitro, RGS proteins have been shown to inhibit signaling by ago

293 When RGS activity is abrogated, septins are partially disorga

294 Despite many investigations, whether RGS proteins modulate GIRK activity in neurons by mechan

295 we highlight the diverse mechanisms by which RGS protein complexes control plasticity in response to

296 ummarize findings on the mechanisms by which RGS proteins modulate functional responses to opioids in

297 ation has emerged on the mechanisms by which RGS proteins modulate the efficacy of opioid analgesics

298 d G-protein networks and the extent to which RGS function is conserved across contrasting monocots, w

299 RhoA/Rho kinase has not been associated with RGS molecules.

300 NFR1 interacts with RGS proteins and phosphorylates them.