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Items: 1 to 20 of 138


The unusual dynamics of parasite actin result from isodesmic polymerization.

Skillman KM, Ma CI, Fremont DH, Diraviyam K, Cooper JA, Sept D, Sibley LD.

Nat Commun. 2013;4:2285. doi: 10.1038/ncomms3285.


Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.

Skillman KM, Daher W, Ma CI, Soldati-Favre D, Sibley LD.

Biochemistry. 2012 Mar 27;51(12):2486-95. doi: 10.1021/bi201704y.


Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites.

Skillman KM, Diraviyam K, Khan A, Tang K, Sept D, Sibley LD.

PLoS Pathog. 2011 Oct;7(10):e1002280. doi: 10.1371/journal.ppat.1002280.


Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.

Mehta S, Sibley LD.

J Biol Chem. 2010 Feb 26;285(9):6835-47. doi: 10.1074/jbc.M109.068155.


Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii.

Mehta S, Sibley LD.

Mol Biol Cell. 2011 Apr 15;22(8):1290-9. doi: 10.1091/mbc.E10-12-0939.


Actin filament polymerization regulates gliding motility by apicomplexan parasites.

Wetzel DM, Håkansson S, Hu K, Roos D, Sibley LD.

Mol Biol Cell. 2003 Feb;14(2):396-406.


Structure of Toxoplasma gondii coronin, an actin-binding protein that relocalizes to the posterior pole of invasive parasites and contributes to invasion and egress.

Salamun J, Kallio JP, Daher W, Soldati-Favre D, Kursula I.

FASEB J. 2014 Nov;28(11):4729-47. doi: 10.1096/fj.14-252569.


Molecular characterization of Toxoplasma gondii formin 3, an actin nucleator dispensable for tachyzoite growth and motility.

Daher W, Klages N, Carlier MF, Soldati-Favre D.

Eukaryot Cell. 2012 Mar;11(3):343-52. doi: 10.1128/EC.05192-11.


Role of formins in actin assembly: nucleation and barbed-end association.

Pruyne D, Evangelista M, Yang C, Bi E, Zigmond S, Bretscher A, Boone C.

Science. 2002 Jul 26;297(5581):612-5.


A novel actin-binding motif in Las17/WASP nucleates actin filaments independently of Arp2/3.

Urbanek AN, Smith AP, Allwood EG, Booth WI, Ayscough KR.

Curr Biol. 2013 Feb 4;23(3):196-203. doi: 10.1016/j.cub.2012.12.024.


Actin hydrophobic loop 262-274 and filament nucleation and elongation.

Shvetsov A, Galkin VE, Orlova A, Phillips M, Bergeron SE, Rubenstein PA, Egelman EH, Reisler E.

J Mol Biol. 2008 Jan 18;375(3):793-801.


Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion.

Delorme-Walker V, Abrivard M, Lagal V, Anderson K, Perazzi A, Gonzalez V, Page C, Chauvet J, Ochoa W, Volkmann N, Hanein D, Tardieux I.

J Cell Sci. 2012 Sep 15;125(Pt 18):4333-42. doi: 10.1242/jcs.103648.


Toxofilin, a novel actin-binding protein from Toxoplasma gondii, sequesters actin monomers and caps actin filaments.

Poupel O, Boleti H, Axisa S, Couture-Tosi E, Tardieux I.

Mol Biol Cell. 2000 Jan;11(1):355-68.


Kinetic analysis of actin polymerization.

Nishida E, Sakai H.

J Biochem. 1983 Apr;93(4):1011-20.


Tension modulates actin filament polymerization mediated by formin and profilin.

Courtemanche N, Lee JY, Pollard TD, Greene EC.

Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9752-7. doi: 10.1073/pnas.1308257110.


Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends.

Murray JW, Edmonds BT, Liu G, Condeelis J.

J Cell Biol. 1996 Dec;135(5):1309-21.


Polymerization of G-actin by myosin subfragment 1.

Miller L, Phillips M, Reisler E.

J Biol Chem. 1988 Feb 5;263(4):1996-2002.


Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii.

Daher W, Plattner F, Carlier MF, Soldati-Favre D.

PLoS Pathog. 2010 Oct 7;6(10):e1001132. doi: 10.1371/journal.ppat.1001132.


Microtubules as platforms for assaying actin polymerization in vivo.

Oelkers JM, Vinzenz M, Nemethova M, Jacob S, Lai FP, Block J, Szczodrak M, Kerkhoff E, Backert S, Schlüter K, Stradal TE, Small JV, Koestler SA, Rottner K.

PLoS One. 2011;6(5):e19931. doi: 10.1371/journal.pone.0019931.

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