(Q44149497)

English

Unique isoform of Galpha -interacting protein (RGS-GAIP) selectively discriminates between two Go-mediated pathways that inhibit Ca2+ channels

scientific article published on 20 September 2002

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Unique isoform of Galpha -interacting protein (RGS-GAIP) selectively discriminates between two Go-mediated pathways that inhibit Ca2+ channels (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

object named as

Timothy Turner

2

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author name string

Patrizia Tosetti

1

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Qiang Lu

3

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Kathleen Dunlap

4

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

language of work or name

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publication date

20 September 2002

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

30 November 2017

277

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

48

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

46001-46009

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

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The regulator of G protein signaling family

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Regulators of G protein signaling attenuate the G protein-mediated inhibition of N-type Ca channels

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RGS proteins: more than just GAPs for heterotrimeric G proteins

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Novel form of crosstalk between G protein and tyrosine kinase pathways

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Structural Basis for the Selectivity of the RGS Protein, GAIP, for G i Family Members: IDENTIFICATION OF A SINGLE AMINO ACID DETERMINANT FOR SELECTIVE INTERACTION OF G i SUBUNITS WITH GAIP

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A novel 7-nucleotide motif located in 3' untranslated sequences of the immediate-early gene set mediates platelet-derived growth factor induction of the JE gene

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Divergence of RGS proteins: evidence for the existence of six mammalian RGS subfamilies

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RGS4 binds to membranes through an amphipathic alpha -helix.

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Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs

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Two types of gamma-aminobutyric acid receptor on embryonic sensory neurones

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Control of the expression and activity of the Galpha-interacting protein (GAIP) in human intestinal cells

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Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles

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Identifiers

10.1074/JBC.M207874200

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

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