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Volumn 6, Issue 7, 2011, Pages

Structural and functional evaluation of C. elegans filamins FLN-1 and FLN-2

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FILAMIN; FILAMIN 2; FILAMIN A; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; CAENORHABDITIS ELEGANS PROTEIN; CONTRACTILE PROTEIN; FILAMINS; IMMUNOGLOBULIN;

EID: 79960745771     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022428     Document Type: Article
Times cited : (13)

References (70)
  • 2
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: a versatile molecular scaffold for cell motility and signalling
    • Feng Y, Walsh CA, (2004) The many faces of filamin: a versatile molecular scaffold for cell motility and signalling. Nat Cell Biol 6: 1034-1038.
    • (2004) Nat Cell Biol , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 3
    • 62849095585 scopus 로고    scopus 로고
    • Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations
    • Nakamura F, Heikkinen O, Pentikainen OT, Osborn TM, Kasza KE, et al. (2009) Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations. PLoS One 4: e4928.
    • (2009) PLoS One , vol.4
    • Nakamura, F.1    Heikkinen, O.2    Pentikainen, O.T.3    Osborn, T.M.4    Kasza, K.E.5
  • 4
    • 34548447703 scopus 로고    scopus 로고
    • Structure of three tandem filamin domains reveals auto-inhibition of ligand binding
    • Lad Y, Kiema T, Jiang P, Pentikainen OT, Coles CH, et al. (2007) Structure of three tandem filamin domains reveals auto-inhibition of ligand binding. EMBO J 26: 3993-4004.
    • (2007) EMBO J , vol.26 , pp. 3993-4004
    • Lad, Y.1    Kiema, T.2    Jiang, P.3    Pentikainen, O.T.4    Coles, C.H.5
  • 5
    • 31544465231 scopus 로고    scopus 로고
    • The molecular basis of filamin binding to integrins and competition with talin
    • Kiema T, Lad Y, Jiang P, Oxley CL, Baldassarre M, et al. (2006) The molecular basis of filamin binding to integrins and competition with talin. Mol Cell 21: 337-347.
    • (2006) Mol Cell , vol.21 , pp. 337-347
    • Kiema, T.1    Lad, Y.2    Jiang, P.3    Oxley, C.L.4    Baldassarre, M.5
  • 9
    • 0025184841 scopus 로고
    • Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring
    • Gorlin JB, Yamin R, Egan S, Stewart M, Stossel TP, et al. (1990) Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J Cell Biol 111: 1089-1105.
    • (1990) J Cell Biol , vol.111 , pp. 1089-1105
    • Gorlin, J.B.1    Yamin, R.2    Egan, S.3    Stewart, M.4    Stossel, T.P.5
  • 10
    • 25444458853 scopus 로고    scopus 로고
    • Ca2+ and calmodulin regulate the binding of filamin A to actin filaments
    • Nakamura F, Hartwig JH, Stossel TP, Szymanski PT, (2005) Ca2+ and calmodulin regulate the binding of filamin A to actin filaments. J Biol Chem 280: 32426-32433.
    • (2005) J Biol Chem , vol.280 , pp. 32426-32433
    • Nakamura, F.1    Hartwig, J.H.2    Stossel, T.P.3    Szymanski, P.T.4
  • 11
    • 0028833396 scopus 로고
    • Utrophin actin binding domain: analysis of actin binding and cellular targeting
    • Winder SJ, Hemmings L, Maciver SK, Bolton SJ, Tinsley JM, et al. (1995) Utrophin actin binding domain: analysis of actin binding and cellular targeting. J Cell Sci 108 (Pt 1): 63-71.
    • (1995) J Cell Sci , vol.108 , Issue.PT 1 , pp. 63-71
    • Winder, S.J.1    Hemmings, L.2    Maciver, S.K.3    Bolton, S.J.4    Tinsley, J.M.5
  • 13
    • 0344522713 scopus 로고    scopus 로고
    • Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans
    • Robertson SP, Twigg SR, Sutherland-Smith AJ, Biancalana V, Gorlin RJ, et al. (2003) Localized mutations in the gene encoding the cytoskeletal protein filamin A cause diverse malformations in humans. Nat Genet 33: 487-491.
    • (2003) Nat Genet , vol.33 , pp. 487-491
    • Robertson, S.P.1    Twigg, S.R.2    Sutherland-Smith, A.J.3    Biancalana, V.4    Gorlin, R.J.5
  • 14
    • 71749121849 scopus 로고    scopus 로고
    • Identification and characterization of multiple similar ligand-binding repeats in filamin: IMPLICATION ON FILAMIN-MEDIATED RECEPTOR CLUSTERING AND CROSS-TALK
    • Ithychanda SS, Hsu D, Li H, Yan L, Liu D, et al. (2009) Identification and characterization of multiple similar ligand-binding repeats in filamin: IMPLICATION ON FILAMIN-MEDIATED RECEPTOR CLUSTERING AND CROSS-TALK. J Biol Chem 284: 35113-35121.
    • (2009) J Biol Chem , vol.284 , pp. 35113-35121
    • Ithychanda, S.S.1    Hsu, D.2    Li, H.3    Yan, L.4    Liu, D.5
  • 15
    • 0032483459 scopus 로고    scopus 로고
    • Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction
    • Loo DT, Kanner SB, Aruffo A, (1998) Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction. J Biol Chem 273: 23304-23312.
    • (1998) J Biol Chem , vol.273 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 16
    • 0142210175 scopus 로고    scopus 로고
    • Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking
    • Onoprishvili I, Andria ML, Kramer HK, Ancevska-Taneva N, Hiller JM, et al. (2003) Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking. Mol Pharmacol 64: 1092-1100.
    • (2003) Mol Pharmacol , vol.64 , pp. 1092-1100
    • Onoprishvili, I.1    Andria, M.L.2    Kramer, H.K.3    Ancevska-Taneva, N.4    Hiller, J.M.5
  • 18
    • 0030614745 scopus 로고    scopus 로고
    • Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells
    • Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, et al. (1997) Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells. J Biol Chem 272: 2620-2628.
    • (1997) J Biol Chem , vol.272 , pp. 2620-2628
    • Marti, A.1    Luo, Z.2    Cunningham, C.3    Ohta, Y.4    Hartwig, J.5
  • 20
    • 0023899761 scopus 로고
    • Actin-binding and dimerization domains of HeLa cell filamin
    • Weihing RR, (1988) Actin-binding and dimerization domains of HeLa cell filamin. Biochemistry 27: 1865-1869.
    • (1988) Biochemistry , vol.27 , pp. 1865-1869
    • Weihing, R.R.1
  • 21
    • 59449085097 scopus 로고    scopus 로고
    • Filamin B serves as a molecular scaffold for type I interferon-induced c-Jun NH2-terminal kinase signaling pathway
    • Jeon YJ, Choi JS, Lee JY, Yu KR, Ka SH, et al. (2008) Filamin B serves as a molecular scaffold for type I interferon-induced c-Jun NH2-terminal kinase signaling pathway. Mol Biol Cell 19: 5116-5130.
    • (2008) Mol Biol Cell , vol.19 , pp. 5116-5130
    • Jeon, Y.J.1    Choi, J.S.2    Lee, J.Y.3    Yu, K.R.4    Ka, S.H.5
  • 22
    • 0038607443 scopus 로고    scopus 로고
    • The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha
    • Tigges U, Koch B, Wissing J, Jockusch BM, Ziegler WH, (2003) The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha. J Biol Chem 278: 23561-23569.
    • (2003) J Biol Chem , vol.278 , pp. 23561-23569
    • Tigges, U.1    Koch, B.2    Wissing, J.3    Jockusch, B.M.4    Ziegler, W.H.5
  • 23
    • 33750615553 scopus 로고    scopus 로고
    • A biochemist's guide to Caenorhabditis elegans
    • Corsi AK, (2006) A biochemist's guide to Caenorhabditis elegans. Anal Biochem 359: 1-17.
    • (2006) Anal Biochem , vol.359 , pp. 1-17
    • Corsi, A.K.1
  • 24
    • 0028990430 scopus 로고
    • Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans
    • Gettner SN, Kenyon C, Reichardt LF, (1995) Characterization of beta pat-3 heterodimers, a family of essential integrin receptors in C. elegans. J Cell Biol 129: 1127-1141.
    • (1995) J Cell Biol , vol.129 , pp. 1127-1141
    • Gettner, S.N.1    Kenyon, C.2    Reichardt, L.F.3
  • 25
    • 0142106350 scopus 로고    scopus 로고
    • Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans
    • Cram EJ, Clark SG, Schwarzbauer JE, (2003) Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans. J Cell Sci 116: 3871-3878.
    • (2003) J Cell Sci , vol.116 , pp. 3871-3878
    • Cram, E.J.1    Clark, S.G.2    Schwarzbauer, J.E.3
  • 26
    • 2942514673 scopus 로고    scopus 로고
    • Sticky worms: adhesion complexes in C. elegans
    • Cox EA, Hardin J, (2004) Sticky worms: adhesion complexes in C. elegans. J Cell Sci 117: 1885-1897.
    • (2004) J Cell Sci , vol.117 , pp. 1885-1897
    • Cox, E.A.1    Hardin, J.2
  • 27
    • 38449099645 scopus 로고    scopus 로고
    • Small GTPases
    • Lundquist EA, (2006) Small GTPases. WormBook pp. 1-18.
    • (2006) WormBook , pp. 1-18
    • Lundquist, E.A.1
  • 28
    • 77957907446 scopus 로고    scopus 로고
    • FLN-1/filamin is required for maintenance of actin and exit of fertilized oocytes from the spermatheca in C. elegans
    • Kovacevic I, Cram EJ, (2010) FLN-1/filamin is required for maintenance of actin and exit of fertilized oocytes from the spermatheca in C. elegans. Dev Biol 347: 247-257.
    • (2010) Dev Biol , vol.347 , pp. 247-257
    • Kovacevic, I.1    Cram, E.J.2
  • 29
    • 0037448540 scopus 로고    scopus 로고
    • Systematic functional analysis of the Caenorhabditis elegans genome using RNAi
    • Kamath RS, Fraser AG, Dong Y, Poulin G, Durbin R, et al. (2003) Systematic functional analysis of the Caenorhabditis elegans genome using RNAi. Nature 421: 231-237.
    • (2003) Nature , vol.421 , pp. 231-237
    • Kamath, R.S.1    Fraser, A.G.2    Dong, Y.3    Poulin, G.4    Durbin, R.5
  • 30
    • 26444458292 scopus 로고    scopus 로고
    • Functional genomic analysis of C. elegans molting
    • Frand AR, Russel S, Ruvkun G, (2005) Functional genomic analysis of C. elegans molting. PLoS Biol 3: e312.
    • (2005) PLoS Biol , vol.3
    • Frand, A.R.1    Russel, S.2    Ruvkun, G.3
  • 31
    • 0026078472 scopus 로고
    • Insertion of part of an intron into the 5′ untranslated region of a Caenorhabditis elegans gene converts it into a trans-spliced gene
    • Conrad R, Thomas J, Spieth J, Blumenthal T, (1991) Insertion of part of an intron into the 5′ untranslated region of a Caenorhabditis elegans gene converts it into a trans-spliced gene. Mol Cell Biol 11: 1921-1926.
    • (1991) Mol Cell Biol , vol.11 , pp. 1921-1926
    • Conrad, R.1    Thomas, J.2    Spieth, J.3    Blumenthal, T.4
  • 32
    • 38549105096 scopus 로고    scopus 로고
    • Trans-splicing and operons
    • WormBook
    • Blumenthal T, (2005) Trans-splicing and operons. WormBook pp. 1-9.
    • (2005) , pp. 1-9
    • Blumenthal, T.1
  • 33
    • 69949142750 scopus 로고    scopus 로고
    • Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin
    • Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, et al. (2009) Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284: 25450-25458.
    • (2009) J Biol Chem , vol.284 , pp. 25450-25458
    • Heikkinen, O.K.1    Ruskamo, S.2    Konarev, P.V.3    Svergun, D.I.4    Iivanainen, T.5
  • 34
    • 78650410139 scopus 로고    scopus 로고
    • Integrative analysis of the Caenorhabditis elegans genome by the modENCODE project
    • Gerstein MB, Lu ZJ, Van Nostrand EL, Cheng C, Arshinoff BI, et al. (2010) Integrative analysis of the Caenorhabditis elegans genome by the modENCODE project. Science 330: 1775-1787.
    • (2010) Science , vol.330 , pp. 1775-1787
    • Gerstein, M.B.1    Lu, Z.J.2    van Nostrand, E.L.3    Cheng, C.4    Arshinoff, B.I.5
  • 35
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N, Nei M, (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 36
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 37
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • Letunic I, Doerks T, Bork P, (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37: D229-232.
    • (2009) Nucleic Acids Res , vol.37 , pp. 229-232
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 38
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J, Milpetz F, Bork P, Ponting CP, (1998) SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A 95: 5857-5864.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 39
    • 34247146251 scopus 로고    scopus 로고
    • Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer
    • Sjekloca L, Pudas R, Sjoblom B, Konarev P, Carugo O, et al. (2007) Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368: 1011-1023.
    • (2007) J Mol Biol , vol.368 , pp. 1011-1023
    • Sjekloca, L.1    Pudas, R.2    Sjoblom, B.3    Konarev, P.4    Carugo, O.5
  • 41
  • 42
    • 40549141792 scopus 로고    scopus 로고
    • QMEAN: A comprehensive scoring function for model quality assessment
    • Benkert P, Tosatto SC, Schomburg D, (2008) QMEAN: A comprehensive scoring function for model quality assessment. Proteins 71: 261-277.
    • (2008) Proteins , vol.71 , pp. 261-277
    • Benkert, P.1    Tosatto, S.C.2    Schomburg, D.3
  • 43
    • 67649846288 scopus 로고    scopus 로고
    • Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains
    • Sawyer GM, Clark AR, Robertson SP, Sutherland-Smith AJ, (2009) Disease-associated substitutions in the filamin B actin binding domain confer enhanced actin binding affinity in the absence of major structural disturbance: Insights from the crystal structures of filamin B actin binding domains. J Mol Biol 390: 1030-1047.
    • (2009) J Mol Biol , vol.390 , pp. 1030-1047
    • Sawyer, G.M.1    Clark, A.R.2    Robertson, S.P.3    Sutherland-Smith, A.J.4
  • 44
    • 0038022666 scopus 로고    scopus 로고
    • The Caenorhabditis elegans vab-10 spectraplakin isoforms protect the epidermis against internal and external forces
    • Bosher JM, Hahn BS, Legouis R, Sookhareea S, Weimer RM, et al. (2003) The Caenorhabditis elegans vab-10 spectraplakin isoforms protect the epidermis against internal and external forces. J Cell Biol pp. 757-768.
    • (2003) J Cell Biol , pp. 757-768
    • Bosher, J.M.1    Hahn, B.S.2    Legouis, R.3    Sookhareea, S.4    Weimer, R.M.5
  • 47
    • 79960671344 scopus 로고    scopus 로고
    • Assembly of a filamin four domain fragment and the influence of splicing variant-1 on the structure
    • in press
    • Pentikainen U, Jiang P, Takala H, Ruskamo S, Campbell ID, et al. (2011) Assembly of a filamin four domain fragment and the influence of splicing variant-1 on the structure. J Biol Chem in press.
    • (2011) J Biol Chem
    • Pentikainen, U.1    Jiang, P.2    Takala, H.3    Ruskamo, S.4    Campbell, I.D.5
  • 48
    • 17444372666 scopus 로고    scopus 로고
    • Seizure suppression by gain-of-function escargot mutations
    • Hekmat-Scafe DS, Dang KN, Tanouye MA, (2005) Seizure suppression by gain-of-function escargot mutations. Genetics 169: 1477-1493.
    • (2005) Genetics , vol.169 , pp. 1477-1493
    • Hekmat-Scafe, D.S.1    Dang, K.N.2    Tanouye, M.A.3
  • 49
    • 33748279281 scopus 로고    scopus 로고
    • Mutations in the K+/Cl- cotransporter gene kazachoc (kcc) increase seizure susceptibility in Drosophila
    • Hekmat-Scafe DS, Lundy MY, Ranga R, Tanouye MA, (2006) Mutations in the K+/Cl- cotransporter gene kazachoc (kcc) increase seizure susceptibility in Drosophila. J Neurosci 26: 8943-8954.
    • (2006) J Neurosci , vol.26 , pp. 8943-8954
    • Hekmat-Scafe, D.S.1    Lundy, M.Y.2    Ranga, R.3    Tanouye, M.A.4
  • 50
    • 33644854752 scopus 로고    scopus 로고
    • Seizure suppression by shakB2, a gap junction mutation in Drosophila
    • Song J, Tanouye MA, (2006) Seizure suppression by shakB2, a gap junction mutation in Drosophila. J Neurophysiol 95: 627-635.
    • (2006) J Neurophysiol , vol.95 , pp. 627-635
    • Song, J.1    Tanouye, M.A.2
  • 51
    • 79651475674 scopus 로고    scopus 로고
    • Intertissue mechanical stress affects frizzled-mediated planar cell polarity in the Drosophila notum epidermis
    • Olguin P, Glavic A, Mlodzik M, (2011) Intertissue mechanical stress affects frizzled-mediated planar cell polarity in the Drosophila notum epidermis. Curr Biol 21: 236-242.
    • (2011) Curr Biol , vol.21 , pp. 236-242
    • Olguin, P.1    Glavic, A.2    Mlodzik, M.3
  • 52
    • 0033523942 scopus 로고    scopus 로고
    • Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals
    • Sokol NS, Cooley L, (1999) Drosophila filamin encoded by the cheerio locus is a component of ovarian ring canals. Curr Biol 9: 1221-1230.
    • (1999) Curr Biol , vol.9 , pp. 1221-1230
    • Sokol, N.S.1    Cooley, L.2
  • 53
    • 0032824776 scopus 로고    scopus 로고
    • Filamin is required for ring canal assembly and actin organization during Drosophila oogenesis
    • Li MG, Serr M, Edwards K, Ludmann S, Yamamoto D, et al. (1999) Filamin is required for ring canal assembly and actin organization during Drosophila oogenesis. J Cell Biol 146: 1061-1074.
    • (1999) J Cell Biol , vol.146 , pp. 1061-1074
    • Li, M.G.1    Serr, M.2    Edwards, K.3    Ludmann, S.4    Yamamoto, D.5
  • 54
    • 0042845810 scopus 로고    scopus 로고
    • Drosophila filamin is required for follicle cell motility during oogenesis
    • Sokol NS, Cooley L, (2003) Drosophila filamin is required for follicle cell motility during oogenesis. Dev Biol 260: 260-272.
    • (2003) Dev Biol , vol.260 , pp. 260-272
    • Sokol, N.S.1    Cooley, L.2
  • 55
    • 22044435648 scopus 로고    scopus 로고
    • A novel filamin A D203Y mutation in a female patient with otopalatodigital type 1 syndrome and extremely skewed X chromosome inactivation
    • Hidalgo-Bravo A, Pompa-Mera EN, Kofman-Alfaro S, Gonzalez-Bonilla CR, Zenteno JC, (2005) A novel filamin A D203Y mutation in a female patient with otopalatodigital type 1 syndrome and extremely skewed X chromosome inactivation. Am J Med Genet A 136: 190-193.
    • (2005) Am J Med Genet A , vol.136 , pp. 190-193
    • Hidalgo-Bravo, A.1    Pompa-Mera, E.N.2    Kofman-Alfaro, S.3    Gonzalez-Bonilla, C.R.4    Zenteno, J.C.5
  • 56
    • 0032422555 scopus 로고    scopus 로고
    • Mutations in filamin 1 prevent migration of cerebral cortical neurons in human periventricular heterotopia
    • Fox JW, Lamperti ED, Eksioglu YZ, Hong SE, Feng Y, et al. (1998) Mutations in filamin 1 prevent migration of cerebral cortical neurons in human periventricular heterotopia. Neuron 21: 1315-1325.
    • (1998) Neuron , vol.21 , pp. 1315-1325
    • Fox, J.W.1    Lamperti, E.D.2    Eksioglu, Y.Z.3    Hong, S.E.4    Feng, Y.5
  • 58
    • 0026683647 scopus 로고
    • Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin
    • Furuhashi K, Inagaki M, Hatano S, Fukami K, Takenawa T, (1992) Inositol phospholipid-induced suppression of F-actin-gelating activity of smooth muscle filamin. Biochem Biophys Res Commun 184: 1261-1265.
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1261-1265
    • Furuhashi, K.1    Inagaki, M.2    Hatano, S.3    Fukami, K.4    Takenawa, T.5
  • 59
    • 0032832619 scopus 로고    scopus 로고
    • Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod
    • McCoy AJ, Fucini P, Noegel AA, Stewart M, (1999) Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod. Nat Struct Biol 6: 836-841.
    • (1999) Nat Struct Biol , vol.6 , pp. 836-841
    • McCoy, A.J.1    Fucini, P.2    Noegel, A.A.3    Stewart, M.4
  • 62
    • 0035370113 scopus 로고    scopus 로고
    • Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy
    • Furuike S, Ito T, Yamazaki M, (2001) Mechanical unfolding of single filamin A (ABP-280) molecules detected by atomic force microscopy. FEBS Lett 498: 72-75.
    • (2001) FEBS Lett , vol.498 , pp. 72-75
    • Furuike, S.1    Ito, T.2    Yamazaki, M.3
  • 63
    • 0038583855 scopus 로고    scopus 로고
    • Mechanical response of single filamin A (ABP-280) molecules and its role in the actin cytoskeleton
    • Yamazaki M, Furuike S, Ito T, (2002) Mechanical response of single filamin A (ABP-280) molecules and its role in the actin cytoskeleton. J Muscle Res Cell Motil 23: 525-534.
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 525-534
    • Yamazaki, M.1    Furuike, S.2    Ito, T.3
  • 65
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff S, Henikoff JG, (1992) Amino acid substitution matrices from protein blocks. Proc Natl Acad Sci U S A 89: 10915-10919.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 66
    • 0034800374 scopus 로고    scopus 로고
    • InterProScan-an integration platform for the signature-recognition methods in InterPro
    • Zdobnov EM, Apweiler R, (2001) InterProScan-an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17: 847-848.
    • (2001) Bioinformatics , vol.17 , pp. 847-848
    • Zdobnov, E.M.1    Apweiler, R.2
  • 67
    • 61449229355 scopus 로고    scopus 로고
    • Protein structure homology modeling using SWISS-MODEL workspace
    • Bordoli L, Kiefer F, Arnold K, Benkert P, Battey J, et al. (2009) Protein structure homology modeling using SWISS-MODEL workspace. Nat Protoc 4: 1-13.
    • (2009) Nat Protoc , vol.4 , pp. 1-13
    • Bordoli, L.1    Kiefer, F.2    Arnold, K.3    Benkert, P.4    Battey, J.5
  • 69
    • 0025942107 scopus 로고
    • Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences
    • Mello CC, Kramer JM, Stinchcomb D, Ambros V, (1991) Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences. EMBO J 10: 3959-3970.
    • (1991) EMBO J , vol.10 , pp. 3959-3970
    • Mello, C.C.1    Kramer, J.M.2    Stinchcomb, D.3    Ambros, V.4
  • 70
    • 0016063911 scopus 로고
    • The genetics of Caenorhabditis elegans
    • Brenner S, (1974) The genetics of Caenorhabditis elegans. Genetics 77: 71-94.
    • (1974) Genetics , vol.77 , pp. 71-94
    • Brenner, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.