Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 289

1.

AGAP1, an endosome-associated, phosphoinositide-dependent ADP-ribosylation factor GTPase-activating protein that affects actin cytoskeleton.

Nie Z, Stanley KT, Stauffer S, Jacques KM, Hirsch DS, Takei J, Randazzo PA.

J Biol Chem. 2002 Dec 13;277(50):48965-75. Epub 2002 Oct 17.

2.

Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site.

Kam JL, Miura K, Jackson TR, Gruschus J, Roller P, Stauffer S, Clark J, Aneja R, Randazzo PA.

J Biol Chem. 2000 Mar 31;275(13):9653-63.

3.

ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.

Jackson TR, Brown FD, Nie Z, Miura K, Foroni L, Sun J, Hsu VW, Donaldson JG, Randazzo PA.

J Cell Biol. 2000 Oct 30;151(3):627-38.

4.

The arf6 GAP centaurin alpha-1 is a neuronal actin-binding protein which also functions via GAP-independent activity to regulate the actin cytoskeleton.

Thacker E, Kearns B, Chapman C, Hammond J, Howell A, Theibert A.

Eur J Cell Biol. 2004 Oct;83(10):541-54.

PMID:
15679100
5.

Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling.

Randazzo PA, Hirsch DS.

Cell Signal. 2004 Apr;16(4):401-13. Review.

PMID:
14709330
6.

Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1.

Yoon HY, Jacques K, Nealon B, Stauffer S, Premont RT, Randazzo PA.

Cell Signal. 2004 Sep;16(9):1033-44.

PMID:
15212764
7.

Substrate specificities and activities of AZAP family Arf GAPs in vivo.

Cuthbert EJ, Davis KK, Casanova JE.

Am J Physiol Cell Physiol. 2008 Jan;294(1):C263-70. Epub 2007 Nov 14.

8.

Arf1 dissociates from the clathrin adaptor GGA prior to being inactivated by Arf GTPase-activating proteins.

Jacques KM, Nie Z, Stauffer S, Hirsch DS, Chen LX, Stanley KT, Randazzo PA.

J Biol Chem. 2002 Dec 6;277(49):47235-41. Epub 2002 Oct 9.

9.

An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization.

Mazaki Y, Hashimoto S, Okawa K, Tsubouchi A, Nakamura K, Yagi R, Yano H, Kondo A, Iwamatsu A, Mizoguchi A, Sabe H.

Mol Biol Cell. 2001 Mar;12(3):645-62.

10.

Analysis of the subcellular distribution of avian p95-APP2, an ARF-GAP orthologous to mammalian paxillin kinase linker.

Paris S, Za L, Sporchia B, de Curtis I.

Int J Biochem Cell Biol. 2002 Jul;34(7):826-37.

PMID:
11950598
11.

The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3.

Nie Z, Fei J, Premont RT, Randazzo PA.

J Cell Sci. 2005 Aug 1;118(Pt 15):3555-66.

12.

GIT proteins, A novel family of phosphatidylinositol 3,4, 5-trisphosphate-stimulated GTPase-activating proteins for ARF6.

Vitale N, Patton WA, Moss J, Vaughan M, Lefkowitz RJ, Premont RT.

J Biol Chem. 2000 May 5;275(18):13901-6.

13.

A novel GTPase-activating protein for ARF6 directly interacts with clathrin and regulates clathrin-dependent endocytosis.

Tanabe K, Torii T, Natsume W, Braesch-Andersen S, Watanabe T, Satake M.

Mol Biol Cell. 2005 Apr;16(4):1617-28. Epub 2005 Jan 19.

15.

Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-associated protein beta.

Mandiyan V, Andreev J, Schlessinger J, Hubbard SR.

EMBO J. 1999 Dec 15;18(24):6890-8.

17.

GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids.

Randazzo PA, Kahn RA.

J Biol Chem. 1994 Apr 8;269(14):10758-63. Erratum in: J Biol Chem 1994 Jun 10;269(23):16519.

18.

DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that enhances cell motility through a GAP-dependent mechanism.

Furman C, Short SM, Subramanian RR, Zetter BR, Roberts TM.

J Biol Chem. 2002 Mar 8;277(10):7962-9. Epub 2001 Dec 31.

19.
20.

Supplemental Content

Support Center