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Items: 1 to 20 of 178

1.

The proline-rich protein palladin is a binding partner for profilin.

Boukhelifa M, Moza M, Johansson T, Rachlin A, Parast M, Huttelmaier S, Roy P, Jockusch BM, Carpen O, Karlsson R, Otey CA.

FEBS J. 2006 Jan;273(1):26-33.

2.

Palladin is a novel binding partner for Ena/VASP family members.

Boukhelifa M, Parast MM, Bear JE, Gertler FB, Otey CA.

Cell Motil Cytoskeleton. 2004 May;58(1):17-29.

PMID:
14983521
3.
4.

The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins.

Reinhard M, Giehl K, Abel K, Haffner C, Jarchau T, Hoppe V, Jockusch BM, Walter U.

EMBO J. 1995 Apr 18;14(8):1583-9.

5.

High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP.

Kursula P, Kursula I, Massimi M, Song YH, Downer J, Stanley WA, Witke W, Wilmanns M.

J Mol Biol. 2008 Jan 4;375(1):270-90. Epub 2007 Oct 24.

PMID:
18001770
6.
7.

Molecular analysis of the interaction between palladin and alpha-actinin.

Rönty M, Taivainen A, Moza M, Otey CA, Carpén O.

FEBS Lett. 2004 May 21;566(1-3):30-4.

8.

The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences.

Lambrechts A, Verschelde JL, Jonckheere V, Goethals M, Vandekerckhove J, Ampe C.

EMBO J. 1997 Feb 3;16(3):484-94.

9.

Characterization of human palladin, a microfilament-associated protein.

Mykkänen OM, Grönholm M, Rönty M, Lalowski M, Salmikangas P, Suila H, Carpén O.

Mol Biol Cell. 2001 Oct;12(10):3060-73.

10.
11.

Complex formation between the postsynaptic scaffolding protein gephyrin, profilin, and Mena: a possible link to the microfilament system.

Giesemann T, Schwarz G, Nawrotzki R, Berhörster K, Rothkegel M, Schlüter K, Schrader N, Schindelin H, Mendel RR, Kirsch J, Jockusch BM.

J Neurosci. 2003 Sep 10;23(23):8330-9.

12.

cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains.

Lambrechts A, Kwiatkowski AV, Lanier LM, Bear JE, Vandekerckhove J, Ampe C, Gertler FB.

J Biol Chem. 2000 Nov 17;275(46):36143-51.

13.

The palladin/myotilin/myopalladin family of actin-associated scaffolds.

Otey CA, Rachlin A, Moza M, Arneman D, Carpen O.

Int Rev Cytol. 2005;246:31-58. Review.

PMID:
16164966
15.

Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin.

Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S.

J Biol Chem. 2000 Oct 6;275(40):30817-25.

16.

X-ray structure determination of human profilin II: A comparative structural analysis of human profilins.

Nodelman IM, Bowman GD, Lindberg U, Schutt CE.

J Mol Biol. 1999 Dec 17;294(5):1271-85.

PMID:
10600384
17.

VASP interaction with vinculin: a recurring theme of interactions with proline-rich motifs.

Reinhard M, Rüdiger M, Jockusch BM, Walter U.

FEBS Lett. 1996 Dec 9;399(1-2):103-7.

18.

RIAM, an Ena/VASP and Profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion.

Lafuente EM, van Puijenbroek AA, Krause M, Carman CV, Freeman GJ, Berezovskaya A, Constantine E, Springer TA, Gertler FB, Boussiotis VA.

Dev Cell. 2004 Oct;7(4):585-95.

19.

Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin.

Dixon RD, Arneman DK, Rachlin AS, Sundaresan NR, Costello MJ, Campbell SL, Otey CA.

J Biol Chem. 2008 Mar 7;283(10):6222-31. doi: 10.1074/jbc.M707694200. Epub 2008 Jan 7. Erratum in: J Biol Chem. 2008 Oct 3;283(40):27344.

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