scholarly article | Q13442814 |
review article | Q7318358 |
P356 | DOI | 10.1016/S0076-6879(04)89006-2 |
P698 | PubMed publication ID | 15313561 |
P2093 | author name string | Yaping Tu | |
Thomas M Wilkie | |||
P2860 | cites work | Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity | Q22253430 |
RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha | Q24316172 | ||
The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro | Q24655997 | ||
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis | Q27736041 | ||
Modulation of the affinity and selectivity of RGS protein interaction with G alpha subunits by a conserved asparagine/serine residue | Q28138422 | ||
Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10 | Q28141136 | ||
GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins | Q28145018 | ||
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 | Q28184243 | ||
RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation | Q28198826 | ||
G proteins: transducers of receptor-generated signals | Q29547519 | ||
Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits | Q34444567 | ||
Analyses of RGS protein control of agonist-evoked Ca2+ signaling | Q35864203 | ||
Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-activating proteins | Q36424021 | ||
Regulators of G-protein signaling (RGS) 4, insertion into model membranes and inhibition of activity by phosphatidic acid | Q38358455 | ||
Binding of regulator of G protein signaling (RGS) proteins to phospholipid bilayers. Contribution of location and/or orientation to Gtpase-activating protein activity | Q43556709 | ||
RGS4 binds to membranes through an amphipathic alpha -helix. | Q52538794 | ||
Expression of G-protein alpha subunits in Escherichia coli. | Q54645309 | ||
Purification of Recombinant G Proteins from Sf9 Cells by Hexahistidine Tagging of Associated Subunits | Q56593501 | ||
Dynamic Regulation of RGS2 Suggests a Novel Mechanism in G-Protein Signaling and Neuronal Plasticity | Q61893595 | ||
Recognition and characterization of calmodulin-binding sequences in peptides and proteins | Q69032811 | ||
Mutational analysis of the Asn residue essential for RGS protein binding to G-proteins | Q74326003 | ||
The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling | Q77696554 | ||
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 89-105 | |
P577 | publication date | 2004-01-01 | |
P1433 | published in | Methods in Enzymology | Q2076903 |
P1476 | title | Allosteric regulation of GAP activity by phospholipids in regulators of G-protein signaling | |
P478 | volume | 389 |
Q42578482 | Evaluating modulators of "Regulator of G-protein Signaling" (RGS) proteins |
Q41671424 | Functional cooperation of of IL-1β and RGS4 in the brachial plexus avulsion mediated brain reorganization |
Q36061579 | G-protein signaling: back to the future |
Q38978553 | Phosphatidic acid binding inhibits RGS1 activity to affect specific signaling pathways in Arabidopsis |
Q57372759 | Regulation of RGS2 and Second Messenger Signaling in Vascular Smooth Muscle Cells by cGMP-dependent Protein Kinase |
Q34198530 | Regulators of G-protein signaling and their Gα substrates: promises and challenges in their use as drug discovery targets |
Q48160738 | Three regulators of G protein signaling differentially affect mating, morphology and virulence in the smut fungus Ustilago maydis. |
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