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Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics.

Poukkula M, Kremneva E, Serlachius M, Lappalainen P.

Cytoskeleton (Hoboken). 2011 Sep;68(9):471-90. doi: 10.1002/cm.20530. Epub 2011 Sep 13. Review.


Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins.

Hellman M, Paavilainen VO, Naumanen P, Lappalainen P, Annila A, Permi P.

FEBS Lett. 2004 Oct 8;576(1-2):91-6.


Structure of the actin-depolymerizing factor homology domain in complex with actin.

Paavilainen VO, Oksanen E, Goldman A, Lappalainen P.

J Cell Biol. 2008 Jul 14;182(1):51-9. doi: 10.1083/jcb.200803100.


Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin.

Paavilainen VO, Merckel MC, Falck S, Ojala PJ, Pohl E, Wilmanns M, Lappalainen P.

J Biol Chem. 2002 Nov 8;277(45):43089-95. Epub 2002 Aug 30.


NMR solution structures of actin depolymerizing factor homology domains.

Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S.

Protein Sci. 2009 Nov;18(11):2384-92. doi: 10.1002/pro.248.


GMF is an evolutionarily developed Adf/cofilin-super family protein involved in the Arp2/3 complex-mediated organization of the actin cytoskeleton.

Nakano K, Kuwayama H, Kawasaki M, Numata O, Takaine M.

Cytoskeleton (Hoboken). 2010 Jun;67(6):373-82. doi: 10.1002/cm.20451.


Regulation of cytoskeletal dynamics by actin-monomer-binding proteins.

Paavilainen VO, Bertling E, Falck S, Lappalainen P.

Trends Cell Biol. 2004 Jul;14(7):386-94. Review.


Coordinated regulation of actin filament turnover by a high-molecular-weight Srv2/CAP complex, cofilin, profilin, and Aip1.

Balcer HI, Goodman AL, Rodal AA, Smith E, Kugler J, Heuser JE, Goode BL.

Curr Biol. 2003 Dec 16;13(24):2159-69.


Structural basis and evolutionary origin of actin filament capping by twinfilin.

Paavilainen VO, Hellman M, Helfer E, Bovellan M, Annila A, Carlier MF, Permi P, Lappalainen P.

Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3113-8. Epub 2007 Feb 20.


Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility.

Carlier MF, Laurent V, Santolini J, Melki R, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D.

J Cell Biol. 1997 Mar 24;136(6):1307-22.


Architecture dependence of actin filament network disassembly.

Gressin L, Guillotin A, Guérin C, Blanchoin L, Michelot A.

Curr Biol. 2015 Jun 1;25(11):1437-47. doi: 10.1016/j.cub.2015.04.011. Epub 2015 Apr 23.


GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation.

Gandhi M, Smith BA, Bovellan M, Paavilainen V, Daugherty-Clarke K, Gelles J, Lappalainen P, Goode BL.

Curr Biol. 2010 May 11;20(9):861-7. doi: 10.1016/j.cub.2010.03.026. Epub 2010 Apr 1.


Oryza sativa actin-interacting protein 1 is required for rice growth by promoting actin turnover.

Shi M, Xie Y, Zheng Y, Wang J, Su Y, Yang Q, Huang S.

Plant J. 2013 Mar;73(5):747-60. doi: 10.1111/tpj.12065. Epub 2013 Jan 17.


The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics.

Vartiainen MK, Mustonen T, Mattila PK, Ojala PJ, Thesleff I, Partanen J, Lappalainen P.

Mol Biol Cell. 2002 Jan;13(1):183-94.


The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers.

Ojala PJ, Paavilainen VO, Vartiainen MK, Tuma R, Weeds AG, Lappalainen P.

Mol Biol Cell. 2002 Nov;13(11):3811-21.

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