Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members. (Q40082365)

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scientific article published on 11 September 2007

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English	Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members.	scientific article published on 11 September 2007

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7 January 2020

Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members (English)

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Ramanathan Natesh

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Steven Gu

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Janet He

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Wing-Ting Ho

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Suneela Ramineni

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John R Hepler

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Scott P Heximer

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11 September 2007

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7 January 2020

Journal of Biological Chemistry

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33064-33075

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7 January 2020

GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits

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RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits

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RGS10 is a selective activator of G alpha i GTPase activity

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GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins

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21 January 2018

RGSZ1 and Ret RGS: two of several splice variants from the gene RGS20.

1 reference

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21 January 2018

RGSZ1, a Gz-selective regulator of G protein signaling whose action is sensitive to the phosphorylation state of Gzalpha

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Measurement of histone-DNA interaction free energy in nucleosomes

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Cellular regulation of RGS proteins: modulators and integrators of G protein signaling

1 reference

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21 January 2018

RGS4 binds to membranes through an amphipathic alpha -helix.

1 reference

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Mechanisms governing subcellular localization and function of human RGS2

1 reference

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Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gq-mediated signaling in vivo.

1 reference

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21 January 2018

G protein selectivity is a determinant of RGS2 function.

1 reference

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21 January 2018

Single-cell imaging of intracellular Ca2+ and phospholipase C activity reveals that RGS 2, 3, and 4 differentially regulate signaling via the Galphaq/11-linked muscarinic M3 receptor

1 reference

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21 January 2018

RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling

1 reference

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21 January 2018

RGS3 inhibits G protein-mediated signaling via translocation to the membrane and binding to Galpha11

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Determinants of translational fidelity and efficiency in vertebrate mRNAs

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Identification of determinants in the alpha-subunit of Gq required for phospholipase C activation

1 reference

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21 January 2018

RGS2-mediated regulation of Gqalpha

1 reference

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Identification of small-molecule inhibitors of RGS4 using a high-throughput flow cytometry protein interaction assay

1 reference

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21 January 2018

Selective inhibition of alpha1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop

1 reference

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21 January 2018

Spinophilin regulates Ca2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors

1 reference

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21 January 2018

Receptor-selective effects of endogenous RGS3 and RGS5 to regulate mitogen-activated protein kinase activation in rat vascular smooth muscle cells

1 reference

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21 January 2018

Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling

1 reference

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21 January 2018

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

1 reference

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10.1074/JBC.M702685200

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17848575%20AND%20SRC:MED&resulttype=core&format=json

7 January 2020

PubMed publication ID

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17848575%20AND%20SRC:MED&resulttype=core&format=json

7 January 2020

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