ライフサイエンスコーパス: G-alpha-12

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1 tes the intrinsic GTP hydrolysis activity of G alpha 12/13 subunits and acts as an effector for G13-c

2 G alpha 12/13-mediated pathways have been shown to be in

3 Thus, the G alpha 12/13-RhoGEF pathway is likely to be involved in

4 tream of gpa-12, the C. elegans homologue of G alpha 12/13.

5 alpha subfamilies, G alpha s, G alpha q, and G alpha 12/13.

6 ase completely restored normal attachment in G alpha 12-activated cells, and there was partial recove

7 G alpha 12 activation led to decreased phosphorylation o

8 the RGS box of LARG interacts not only with G alpha 12 and G alpha 13 but also with G alpha q.

9 Activated G alpha q, as well as G alpha 12 and G alpha 13, cooperated with LARG and caus

10 transition state mimetic forms of G alpha q, G alpha 12, and G alpha 13.

11 y pertussis toxin as well as deficiencies in G alpha 12, chemokine receptor 2 (CCR2), CCR5, chemokine

12 MDCK cell 3D-tubulogenesis assay, activated G alpha 12 inhibited tubulogenesis and led to the format

13 Herein, we demonstrate that G alpha 12 inhibits interaction of MDCK cells with colla

14 r, these studies provide direct evidence for G alpha 12-integrin regulation of epithelial cell spread

15 ese RhoGEFs interact with activated forms of G alpha 12 or G alpha 13 through their RGS domains.

16 blishes a requirement for G alpha 13 but not G alpha 12 or G alpha q/11 in G2A-induced actin rearrang

17 Activating G alpha 12 (QL point mutation or stimulating endogenous

18 Consistent with G alpha 12-regulated attachment to collagen-I, G alpha 1

19 These results proved conservation of the G alpha 12-RhoGEF pathway in C. elegans.

20 eceptors and G proteins in COS-7 cells, that G alpha 12 selectively couples the thrombin receptor to

21 alpha 12-regulated attachment to collagen-I, G alpha 12-silenced MDCK cells revealed a more adherent

22 Furthermore, G alpha 12-silenced MDCK cells were resistant to thrombi

23 (QL point mutation or stimulating endogenous G alpha 12 with thrombin) inhibited focal adhesions and

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