The PH domain of Ras-GAP is sufficient for in vitro binding to beta gamma subunits of heterotrimeric G proteins. (Q30192652)

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17 October 2019

title

The PH domain of Ras-GAP is sufficient for in vitro binding to beta gamma subunits of heterotrimeric G proteins (English)

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17 October 2019

7

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17 October 2019

author name string

N Xu

1

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17 October 2019

O Coso

2

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17 October 2019

D Mahadevan

3

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17 October 2019

A De Blasi

4

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17 October 2019

P K Goldsmith

5

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17 October 2019

W F Simonds

6

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17 October 2019

publication date

1 February 1996

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Cellular and Molecular Neurobiology

17 October 2019

published in

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17 October 2019

volume

16

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17 October 2019

issue

1

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17 October 2019

page(s)

51-59

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

17 October 2019

cites work

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G-protein beta gamma dimers. Membrane targeting requires subunit coexpression and intact gamma C-A-A-X domain

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The PH domain: a common piece in the structural patchwork of signalling proteins

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Recombinant G-protein beta gamma-subunits activate the muscarinic-gated atrial potassium channel

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PH domain: the first anniversary

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A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP

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ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channels

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GAP domains responsible for ras p21-dependent inhibition of muscarinic atrial K+ channel currents

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A putative modular domain present in diverse signaling proteins

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The non-catalytic domain of ras-GAP inhibits transformation induced by G protein coupled receptors

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High expression of beta-adrenergic receptor kinase in human peripheral blood leukocytes. Isoproterenol and platelet activating factor can induce kinase translocation

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12 December 2020