PUBLICATIONS

2017

Wioland H, Guichard B, Senju Y, Myram S, Lappalainen P, Jegou A, Romet-Lemonne G (2017): ADF/cofilin accelerates actin dynamics by severing filaments and promoting their depolymerization at both ends. Curr. Biol. (in press).

Stefani C, Gonzalez-Rodriguez D, Senju Y, Doye A, Efimova N, Janel S, Lipuna J, Tsai MC, Hamaoui D, Maddugoda M, Cochet-Escartin O, Prevost C, Lafont F, Svitkina T, Lappalainen P, Bassereau P, Lemichez E (2017): Ezrin enhances line tension along transcellular tunnel edges via NMIIa driven actomyosin cable formation. Nat. Commun. (in press).

Gateva G, Kremneva E, Reindl T, Kotila T, Kogan K, Gressin L, Gunning PW, Manstein DJ, Michelot A, Lappalainen P (2017): Tropomyosin isoforms specify functionally distinct actin filament populations in vitro. Curr. Biol.27, 705-713.

Pfisterer S, Gateva G, Horvath P, Pirhonen J, Salo V, Karhinen L, Varjosalo M, Ryhänen S, Lappalainen P, Ikonen E (2017): Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage. Nature Commun.8:14858.

Jiu Y, Peränen J, Schaible N, Cheng F, Eriksson JE, Krishnan R, Lappalainen P (2017): Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA. J Cell Sci.130: 892-902.

 

2016

Lappalainen P (2016): Actin-binding proteins: the long road to understanding the dynamic landscape of cellular actin networks. Mol Biol Cell.,27:2519-2522.

Lehtimäki J, Hakala M, Lappalainen P (2016): Actin Filament Structures in Migrating Cells. Handb Exp Pharmacol., 2016 Jul 29. [Epub ahead of print]

 

2015

Tojkander S, Gateva G, Husain A, Krishnan R, Lappalainen P (2015): Generation of contractile actomyosin bundles depends on mechanosensitive actin filament assembly and disassembly. eLife, 4:e06126.

Boczkowska M, Rebowski G, Kremneva E, Lappalainen P, Dominguez R (2015): How leiomodin and tropomodulin use a common fold for different actin assembly functions. Nat. Commun. 15;6:8314.

Prévost C, Zhao H, Manzi J, Lemichez E, Lappalainen P, Callan-Jones A,  Bassereau P (2015): IRSp53 senses negative membrane curvature and phase separates along membrane tubules. Nat. Commun. 15:6:8529.

Gunning PW, Hardeman EC, Lappalainen P, Mulvihill DP (2015):  Tropomyosin: Master regulator of actin filament function in the cytoskeleton. J. Cell Sci. 128: 2965-74.

Jiu Y, Lehtimäki J, Tojkander S, Cheng F, Jäälinoja H, Liu X, Varjosalo M, Eriksson JE, Lappalainen P (2015). Bidirectional interplay between vimentin intermediate filaments and contractile actin stress fibers. Cell Reports 11: 1511-1518.

Saarikangas J, Kourdougli N, Senju Y, Chazal G, Segerstråle M, Minkeviciene R, Kuurne J, Mattila PK, Garrett L, Hölter SM, Becker L, Racz I, Hans W, Klopstock T, Wurst W, Zimmer A, Fuchs H, Gailus-Durner V, Hrabě de Angelis M, von Ossowski L, Taira T, Lappalainen P, Rivera C, Hotulainen P (2015): MIM-induced membrane bending promotes dendritic spine initiation. Dev. Cell 33: 644-659.

 

2014

Poukkula M, Hakala M, Pentinmikko N, Sweeney MO, Jansen S, Mattila J, Hietakangas V, Goode BL, Lappalainen P (2014): GMF promotes leading edge dynamics and collective cell migration in vivo. Curr. Biol. 24: 2533-2540.

Kremneva E, Makkonen MH, Skwarek-Maruszewska A, Gateva G, Michelot A, Dominguez R, Lappalainen P (2014): Cofilin-2 controls actin filament length in muscle sarcomeres. Dev. Cell. 31: 215-226.

Kostan J, Salzer U, Orlova A, Törö I, Hodnik V, Senju Y, Zou J, Schreiner C, Steiner J, Meriläinen J, Nikki M, Virtanen I, Carugo O, Rappsilber J, Lappalainen P, Lehto V-P, Anderluh G, Egelman EH, Djinović-Carugo K (2014): Direct interaction of actin filaments with F-BAR protein pacsin2. EMBO Rep. 15: 1154-1162.

Gateva G, Tojkander S, Koho S, Carpen O, Lappalainen P (2014): Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment.J. Cell Sci. 127: 1887-98.

Mertz KD, Pathria G, Wagner C, Saarikangas J, Sboner A, Romanov J, Gschaider M, Lenz F, Neumann F, Schreiner W, Nemethova M, Glassmann A, Lappalainen P, Stingl G, Small JV, Fink D, Chin L, Wagner SN (2014): MTSS1 is a metastasis driver in a subset of human melanomas. Nat. Commun. 5:3465.

Talma V., Gateva G., Ekokoski E, Lappalainen P, Tuominen RK (2014): Evidence for a role of MRCK in mediating HeLa cell elongation induced by the C1 domain ligand HMI-1a3.  Eur. J. Pharm. Sci. 55: 46-57.

Linkner J, Witte G, Zhao H, Junemann A, Nordholz B, Runge-Wollmann P, Lappalainen P, Faix J (2014): The inverse BAR-domain protein IBARa drives membrane remodelling to control osmoregulation, phagocytosis and cytokinesis.J. Cell Sci. 127: 1279-1292.

 

2013

Kanerva K, Uronen R, Blom T, Li S, Bittman R, Lappalainen P, Peränen J, Raposo G, Ikonen E (2013): LDL-cholesterol is recycled to the plasma membrane via Rab8a-Myosin5b-actin dependent membrane transport. Dev. Cell 27: 249-262.

Zhao H, Michelot A, Koskela EV, Tkach V, Stamou D, Drubin DG, Lappalainen P (2013): Memebrane-sculptingBin-Amphiphysin-Rvs (BAR) domains generate stable lipid microdomains.Cell Reports 6: 1213-1223.

Makkonen M, Bertling E, Chebotareva NA, Baum J, Lappalainen P (2013): Mammalian and malaria parasite cyclase-associated proteins catalyze nucleotide exchange on G-actin through a conserved mechanism. J. Biol. Chem. 288: 984-994.

Pivovarova AV, Chebotareva NA, Kremneva EV, Lappalainen P, Levitsky DI. (2013): The effects of Actin-Binding Proteins on the Thermal Stability of Monomeric Actin. Biochemistry 52: 152-160.

Weber-Boyvat M, Zhao H, Aro N, Yuan Q, Chernov K, Peränen J, Lappalainen P, Jäntti J (2013): A conserved regulatory mode in exocytic membrane fusion revealed by Mso1p membrane interactions. Mol. Biol. Cell 24: 331-341.

 

2012

Lehtonen HJ, Sipponen T, Tojkander S, Karikoski R, Järvinen H, Laing NG, Lappalainen P, Aaltonen LA, Tuupanen S. (2012). Segregation of a Missense Variant in Enteric Smooth Muscle Actin γ-2 with Autosomal Dominant Familial Visceral Myopathy Gastroenterology. 143:1482-1491.

Zhao H, Lappalainen P. (2012). A simple guide to biochemical approaches for analyzing protein-lipid interaction. Mol Biol Cell. 23(15):2823-30.

Kotiadis V, Leadsham J, Bastow E, Gheeraert A, Whybrew J, Bard M, Lappalainen P, Gourlay C (2012): Identification of new surfaces of cofilin that link mitochondrial function to the control of multi-drug resistance. J. Cell Sci. ;125:2288-2299.

Tojkander S, Gateva G, Lappalainen P (2012): Actin stress fibers: assembly, dynamics and biological roles. J. Cell Sci. 125:1855-1864.

2011

Maddugoda MP, Stefani C, Gonzalez-Rodriguez D, Saarikangas J, Torrino S, Janel S, Prodon F, Doye A, Goossens PL, Lafont F, Bassereau P, Lappalainen P, Brochard F, Lemichez E (2011): cAMP signaling by Anthrax edema toxin induces transendothelial cell tunnels, which are resealed by MIM via Arp2/3-driven actin polymerization. Cell Host & Microbe 10:
464-474.

Nevalainen EM, Braun A, Vartiainen MK, Serlachius M, Andersson LC, Moser M, Lappalainen P.(2011). Twinfilin-2a is dispensable for mouse development. PLoS One. 2011;6(8):e22894. Epub 2011 Aug 18.

Poukkula M, Kremneva E, Serlachius M, Lappalainen P. (2011).Actin-depolymerizing factor homology domain: A conserved fold performing diverse roles in cytoskeletal dynamics.Cytoskeleton (Hoboken). 68:471-490.

Pykäläinen A, Boczkowska M, Zhao H, Saarikangas J, Rebowski G, Jansen  M, Hakanen J,  Koskela  E V, Peränen J, Vihinen H, Jokitalo E, Salminen  M, Ikonen E, Dominguez R, Lappalainen P (2011): Pinkbar is an epithelial-specific BAR domain protein that generates planar membrane structures. Nat Struct Mol Biol. 18:902-907.

Tojkander S, Gateva G, Schevzov G, Hotulainen P, Naumanen P, Martin C, Gunning PW, Lappalainen P (2011): A Molecular Pathway for Myosin II Recruitment to Stress Fibers, Current Biology. 21:539-550.

Saarikangas J, Mattila PK, Varjosalo M, Bovellan M, Hakanen J, Calzada-Wack J, Tost M, Jennen L, Rathkolb B, Hans W, Horsch M, Hyvönen ME, Perälä N, Fuchs H, Gailus-Durner V, Esposito I, Wolf E, de Angelis MH, Frilander MJ, Savilahti H, Sariola H, Sainio K, Lehtonen S, Taipale J, Salminen M, Lappalainen P. (2011): Missing-in-metastasis MIM/MTSS1 promotes actin assembly at intercellular junctions and is required for integrity of kidney epithilia. J Cell Sci. 124:1245-1255.

Zhao H, Pykäläinen A, Lappalainen P (2011): I-BAR domain proteins: linking actin and plasma membrane dynamics. Curr Opin Cell Biol. 23:14-21.

2010


Skwarek-Maruszewska A, Boczkowska M, Zajac AL, Kremneva E, Svitkina T, Dominguez R, Lappalainen P (2010): Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeres. Mol. Biol. Cell. 21:3352-3361.

Ramalingam N, Zhao H, Breitsprecher D, Lappalainen P, Faix J, Schleicher M. (2010): Phospholipids regulate localization and activity of mDia1 formin. Eur. J. Cell Biol. 89:723-732.

Saarikangas J , Zhao H , Lappalainen P (2010): Regulation of the interplay between the actin cytoskeleton and plasma membrane by phosphpinositides. Physiol. Rev. 90: 259-289.

Gandhi M, Smith BA, Bovellan M , Paavilainen V , Daugherty-Clarke K, Gelles J, Lappalainen P , Goode BL (2010): GMF is a cofilin homologue that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation. Curr. Biol. 20: 861-867.

Zhao H , Hakala M , Lappalainen P (2010): ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP 2 -density sensor. Biophys. J . 98: 2327-2336.

Monfregola J, Napolitano G, D'Urso M, Lappalainen P , Ursini MV (2010): Functional characterization of Wiscott Aldrich Syndrome protein and scar homolog (WASH), a bi-modular nucleation promoting factor (NPF) able to interact with biogenesis of lysosome related organelle subunit 2 (BLOS-2) and g-tubulin. J. Biol.Chem. 285: 16951-16957.

Li Q, Song X-W, Zou J, Wang G-K, Kremneva E , Zhu N, Li X-Q, Lappalainen P , Yuan W-J, Qin Y-W, and Jing Q (2010): Attenuation of microRNA-1 de-represses the cytoskeleton regulatory protein twinfilin-1 to provoke cardiac hypertrophy. J. Cell Sci. . 123: 2444-2452.

 

2009

Rzadzinska AK, Nevalainen EM, Prosser HM, Lappalainen P, Steel KP (2009). MyosinVIIa interacts withTwinfilin-2 at the tips of mechanosensory stereocilia in the inner ear. PLoS One. 4:e7097.

Hotulainen P , Llano O, Smirnov S, Tanhuanpää K, Faix J, Rivera C, Lappalainen P (2009): Defining mechanisms of actin polymerization and depolymerization during dendritic spine morphogenesis. J. Cell Biol.185:323-329.

Skwarek-Maruszewska A, Hotulainen P, Mattila PK , Lappalainen P (2009): Contractility-dependent actin dynamics in cardiomyocyte sarcomeres. J. Cell Sci.122:2119-2126 .

Quintero-Monzon O, Jonasson EM, Bertling E, Talarico L, Chaudhry F, Sihvo M, Lappalainen P, Goode BL (2009): The roles of Srv2/CAP oligomerization and binding to cofilin-actin complexes in actin turnover in vivo. J. Biol. Chem. 284:10923-10934.

Kardos R, Pozsonyi K, Nevalainen E, Lappalainen P, Nyitrai M, Hild G (2009): The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin. Biophys. J. 96: 2335-43.

Bach CTT, Creed S, Zhong J, Mahmassani M, Schevzov G, Stehn J, Cowell LN, Naumanen P, Lappalainen P, Gunning PW and O'Neill GM. (2009): Tropomyosin isoform expression regulates the transition of adhesions to determine cell speed and direction. Mol. Cell. Biol. 29: 1506-14.

Saarikangas J, Zhao H, Pykäläinen A, Laurinmäki P, Mattila PK, Kinnunen P, Butcher SJ, Lappalainen P (2009): Molecular mechanisms of membrane deformation by I-BAR domain proteins. Curr. Biol. 19: 95-107.

Nevalainen EM, Skwarek-Maruszewska A, Braun A, Moser M, Lappalainen P (2009): Two biochemically distinct and tissue-specific twinfilin isoforms are generated from mouse twinfilin-2 gene by alternative promoter usage. Biochem. J. 417: 593-600.

 

2008

Paavilainen VO, Oksanen E, Goldman A, Lappalainen P (2008): Structure of the actin-depolymerizing factor homology domain in complex with actin. J Cell Biol.  182: 51-59. (Article)

Mattila PK, Lappalainen P (2008): Filopodia: molecular architecture and cellular functions. Nat. Rev. Mol. Cell Biol. 9: 446-454. (Article)

Naumanen P, Lappalainen P, Hotulainen P (2008): Mechanisms of actin stress fibre assembly. J. Microscopy 231: 446-454. (Article)

Creed SJ, Bryce N, Naumanen P, Weinberger R, Lappalainen P, Stehn J, Gunning P. (2008) Tropomyosin isoforms define distinct microfilament populations with different drug susceptibility. Eur. J Cell Biol. 87: 709-720. (Article)

Chereau D, Boczkowska M, Skwarek-Maruszewska A, Fujiwara I, Hayes DB, Renowski G, Lappalainen P, Pollard TD, Dominguez R (2008): Leiomodin is an actin filament nucleator in muscle cells. Science 320: 239-243. (Article)

Saarikangas J, Hakanen J, Mattila PK, Grumet M, Salminen M, Lappalainen P (2008): ABBA regulates plasma-membrane and actin dynamics to promote radial glia extension. J. Cell Sci. 121: 1444-1454. (Article)

Scita G, Confalonieri S, Lappalainen P, Suetsugu S (2008): IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol. 18: 52-60. (Article)

 

2007

Mattila PK, Pykäläinen A, Saarikangas J, Paavilainen V, Vihinen H, Jokitalo E, Lappalainen P (2007): Missing-In-Metastasis (MIM) and IRSp53 deform PI(4,5)P2-rich membranes by an inverse BAR domain like mechanism. J. Cell Biol. 176: 953-964. (Article)

Bertling E, Quintero-Monzon O, Mattila PK, Goode BL, Lappalainen P (2007): Mechanism and biological role of profilin - Srv2/CAP interaction. J. Cell. Sci. 120: 1225-1234. (Article)

Paavilainen VO, Hellman M, Helfer E, Koskinen M, Didry D, Annila A, Carlier M-F, Permi P, Lappalainen P (2007): Structural basis and evolutionary origin of actin filament capping by twinfilin. Proc. Natl. Acad. Sci. 104: 3113-3118. (Article)

 

2006

Hellman M, Paavilainen VO, Annila A, Lappalainen P, Permi P (2006): 1H, 13C and 15N resonance assignments of C-terminal domain of an actin monomer binding protein twinfilin. J. Biomol. NMR, Suppl. 5: 66. (Article)

Hotulainen P, Lappalainen P (2006): Stress-fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173: 383-394. (Article)

Bugyi  B, Papp G, Hild G, Lőrinczy D, Nevalainen EM, Lappalainen P, Somogyi B, Nyitrai M (2006): Formins regulate actin filament flexibility through long-range allosteric interactions. J. Biol. Chem. 281: 10727-10736. (Article)

Helfer E, Nevalainen EM, Naumanen P, Romero S, Didry D, Pantaloni D, Lappalainen P, Carlier M-F (2006): Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility. EMBO Journal. 25: 1184–1195. (Article)

Nevalainen EM, Paavilainen VO, Lappalainen P (2006): Regulation of cellular actin monomer pool by twinfilin. In Actin Monomer Binding Proteins. Springer Science + Business Media. New York, NY, and Landes Bioscience. Georgetown, TX (in press).

Skwarek-Maruszewska A, Hotulainen P, Lappalainen P (2006): Regulation of the actin cytoskeleton by phospholipids. In Advances in Molecular and Cell Biology. Elsevier. Burlington, MA,. vol. 37: 201-219.

 

2005

Hotulainen P, Paunola E, Vartiainen MK, Lappalainen P (2005): ADF and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian non-muscle cells. Mol. Biol. Cell 16: 649-664.

Hellman M, Paavilainen VO, Annila A, Lappalainen P, Permi P. (2005): 1H, 13C and 15N resonance assignments of coactosin, a cytoskeletal regulatory protein. J. Biomol. NMR 30: 365-366.

 

2004

Mattila PK, Quintero-Monzon O, Kugler J, Moseley JB, Almo SC, Lappalainen P, Goode BL (2004) A high affinity interaction with ADP-G-actin underlies the mechanism and in vivo function of Srv2/cyclase-associated protein (CAP). Mol. Biol. Cell 15: 5158-5171.

Hellman M, Paavilainen VO, Naumanen P, Lappalainen P, Annila A, Permi P (2004): Solution structure of coactosin reveals structural homology to ADF/cofilin family proteins. FEBS Letters  576: 91-96.

Falck S, Paavilainen VO, Wear MA, Grossmann JG, Cooper JA, Lappalainen P (2004): Biological role and structural mechanism of twinfilin – capping protein interaction. EMBO Journal. 23: 3010–3019.

Bertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, Lappalainen P (2004): Cyclase-associated-protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian non-muscle cells. Mol. Biol. Cell 15: 2312-2323.

Paavilainen VO, Bertling E, Falck S, Lappalainen P (2004): Regulation of cytoskeletal dynamics by actin monomer binding proteins. Trends Cell Biol. 14: 386-394.

Hilpelä P, Vartiainen MK, Lappalainen P (2004): Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. Current Topics in Microbiology and Immunology 282: 117-163.

 

2003

Vartiainen MK, Sarkkinen EM, Matilainen T, Salminen M, Lappalainen P (2003): Mammals have two twinfilin isoforms whose sub-cellular localizations and tissue distributions are differentially regulated. J. Biol. Chem. 278: 34347-34355.

Mattila PK, Salminen M, Yamashiro T, Lappalainen P (2003): Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its carboxyl-terminal WH2 domain. J. Biol. Chem.  278: 8452-8459.

Salmikangas P, van der Ven PFM, Lalowski M, Taivainen A, Zhao F, Suila H, Schröder R, Lappalainen P, Fürst DO, Carpen O (2003): Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly. Hum. Mol. Genetics 12: 189-203.

 

2002

Ojala PJ, Paavilainen VO, Vartiainen MK, Tuma R, Weeds AG, Lappalainen P (2002): The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers. Mol. Biol. Cell 13: 3811-3821.

Paavilainen VO, Merckel MC, Falck S, Ojala PJ, Pohl E, Wilmanns M, Lappalainen P (2002): Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolyerizing factor (ADF)/cofilin. J. Biol. Chem. 277: 43089-43095.

Band AM, Ali H, Vartiainen MK, Welti S, Lappalainen P, Olkkonen VM, Kuismanen E. (2002): Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. FEBS Lett. 531, 513-9.

Vartiainen MK, Mustonen T, Mattila PK, Ojala PJ, Thesleff I, Partanen J, Lappalainen P (2002): The three mouse actin-depolymerization factor/cofilins evolved to fulfill cell-type specific requirements for actin dynamics. Mol. Biol. Cell 13: 183-194.

Palmgren S, Vartiainen MK, Lappalainen P (2002): Twinfilin, a molecular mailman for actin monomers. J.Cell Sci. 115: 881-886.

Paunola E, Mattila PK, Lappalainen P (2002): WH2 domain: a small, versatile adapter for actin monomers. FEBS Letters 513: 92-97.

 

2001

Wahlström G, Vartiainen MK, Yamamoto L, Mattila PK, Lappalainen P, Heino TI (2001): Twinfilin is required for actin-dependent developmental processes in Drosophila. J. Cell Biol.  155: 787-795.

Palmgren S, Ojala PJ, Wear MA, Cooper JA, Lappalainen P (2001): Interactions with PIP2, ADP-actin monomers and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155: 251-260.

Ojala PJ, Paavilainen V, Lappalainen P (2001): Identification of yeast cofilin residues specific for actin monomer and PIP2-binding. Biochemistry 40: 15562-15569.

 

2000

Vartiainen M, Ojala PJ, Auvinen P, Peränen J, Lappalainen P (2000): Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol. Cell. Biol. 20: 1772-1783.

 

1997-1999 (at UC Berkeley)

Rodal AR, Tetreault JW, Lappalainen P, Drubin DG, Amberg DC (1999): Aip1p interacts with cofilin to disassemble actin filaments. J. Cell Biol. 145: 1251-1264.

Goode BL, Drubin DG, Lappalainen P (1998): Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. J. Cell Biol. 142: 723-733.

Lappalainen P, Kessels MM, Cope MJTV, Drubin DG (1998): The ADF homology (ADF-H) domain, a highly exploited actin-binding module. Mol. Biol. Cell 9: 1951-1959.

Lappalainen P, Fedorov EV, Fedorov AA, Almo SC, Drubin DG (1997): Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO Journal 16: 5520-5530.

Lappalainen P, Drubin DG (1997): Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82.

Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC (1997): Structure determination of yeast cofilin. Nature Struct. Biol. 4: 366-369.

 

 

Contact info

Mailing address:
Biocenter 2, room 2016
Viikinkaari 5D, 00790 Helsinki, Finland
Pekka Lappalainen tel: +358-50-4155433
Office:
Lab: +358-50-4484609
All e-mails:
firstname.lastname -at- helsinki.fi

University of Helsinki