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Volumn 402, Issue 1, 2010, Pages 38-51

Nebulin: A Study of Protein Repeat Evolution

Author keywords

Evolution; Nebulin; Protein domain repeat; Repeat duplication; Segmental duplication

Indexed keywords

ACTIN; LIM KINASE 1; NEBULIN; PROTEIN; PROTEIN NEBULETTE; PROTEIN SH3; TROPOMYOSIN; TROPONIN; UNCLASSIFIED DRUG; MUSCLE PROTEIN;

EID: 77956170943     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.011     Document Type: Article
Times cited : (45)

References (44)
  • 1
    • 0035816218 scopus 로고    scopus 로고
    • Domain combinations in archaeal, eubacterial and eukaryotic proteomes
    • Apic G., Gough J., Teichmann S.A. Domain combinations in archaeal, eubacterial and eukaryotic proteomes. J. Mol. Biol. 2001, 310:311-325.
    • (2001) J. Mol. Biol. , vol.310 , pp. 311-325
    • Apic, G.1    Gough, J.2    Teichmann, S.A.3
  • 2
    • 12344261833 scopus 로고    scopus 로고
    • The relationship between domain duplication and recombination
    • Vogel C., Teichmann S., Pereira-Leal J. The relationship between domain duplication and recombination. J. Mol. Biol. 2005, 346:355-365.
    • (2005) J. Mol. Biol. , vol.346 , pp. 355-365
    • Vogel, C.1    Teichmann, S.2    Pereira-Leal, J.3
  • 4
    • 33646268799 scopus 로고    scopus 로고
    • Domain deletions and substitutions in the modular protein evolution
    • Weiner J., Beaussart F., Bornberg-Bauer E. Domain deletions and substitutions in the modular protein evolution. FEBS J. 2006, 273:2037-2047.
    • (2006) FEBS J. , vol.273 , pp. 2037-2047
    • Weiner, J.1    Beaussart, F.2    Bornberg-Bauer, E.3
  • 5
    • 16244423379 scopus 로고    scopus 로고
    • Multi-domain proteins in the three kingdoms of like-orphan domains and other unassigned regions
    • Ekman D., Björklund Å.K., Frey-Skött J., Elofsson A. Multi-domain proteins in the three kingdoms of like-orphan domains and other unassigned regions. J. Mol. Biol. 2005, 348:231-243.
    • (2005) J. Mol. Biol. , vol.348 , pp. 231-243
    • Ekman, D.1    Björklund, Å.K.2    Frey-Skött, J.3    Elofsson, A.4
  • 8
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman D., Light S., Björklund Å.K., Elofsson A. What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?. Genome Biol. 2006, 7:R45.
    • (2006) Genome Biol. , vol.7
    • Ekman, D.1    Light, S.2    Björklund, Å.K.3    Elofsson, A.4
  • 10
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M., Winder S., Pastore A. Nebulin, a helical actin binding protein. EMBO J. 1994, 13:1782-1789.
    • (1994) EMBO J. , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.2    Pastore, A.3
  • 12
    • 0035814795 scopus 로고    scopus 로고
    • High-affinity actin-binding nebulin fragments influence the actoS1 complex
    • Root D., Wang K. High-affinity actin-binding nebulin fragments influence the actoS1 complex. Biochemistry 2001, 40:1171-1186.
    • (2001) Biochemistry , vol.40 , pp. 1171-1186
    • Root, D.1    Wang, K.2
  • 13
    • 4644306059 scopus 로고    scopus 로고
    • Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts
    • Donner K., Sandbacka M., Lehtokari V., Wallgren-Pettersson C., Pelin K. Complete genomic structure of the human nebulin gene and identification of alternatively spliced transcripts. Eur. J. Hum. Genet. 2004, 12:744-751. 10.1038/sj.ejhg.5201242.
    • (2004) Eur. J. Hum. Genet. , vol.12 , pp. 744-751
    • Donner, K.1    Sandbacka, M.2    Lehtokari, V.3    Wallgren-Pettersson, C.4    Pelin, K.5
  • 14
    • 0036061465 scopus 로고    scopus 로고
    • Targeted disruption of Nebulette protein expression alters cardiac myofibril assembly and function
    • Moncman C., Wang K. Targeted disruption of Nebulette protein expression alters cardiac myofibril assembly and function. Exp. Cell Res. 2002, 273:204-218. 10.1006/excr.2001.5423.
    • (2002) Exp. Cell Res. , vol.273 , pp. 204-218
    • Moncman, C.1    Wang, K.2
  • 15
    • 2442576932 scopus 로고    scopus 로고
    • Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-Nebulette and Lasp-1
    • Li B., Zhuang L., Trueb B. Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-Nebulette and Lasp-1. J. Biol. Chem. 2004, 279:20401-20410.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20401-20410
    • Li, B.1    Zhuang, L.2    Trueb, B.3
  • 16
    • 37549035082 scopus 로고    scopus 로고
    • Lasp-2 expression, localization, and ligand interactions: a new Z-disc scaffolding protein
    • Zieseniss A., Terasaki A.G., Gregorio C.C. Lasp-2 expression, localization, and ligand interactions: a new Z-disc scaffolding protein. Cell Motil. Cytoskeleton 2008, 65:59-72.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 59-72
    • Zieseniss, A.1    Terasaki, A.G.2    Gregorio, C.C.3
  • 17
    • 62849089983 scopus 로고    scopus 로고
    • Characterization of amphioxus nebulin and its similarity to human nebulin
    • Hanashima A., Kubokawa K., Kimura S. Characterization of amphioxus nebulin and its similarity to human nebulin. J. Exp. Biol. 2009, 212:668-672. 10.1242/jeb.022681.
    • (2009) J. Exp. Biol. , vol.212 , pp. 668-672
    • Hanashima, A.1    Kubokawa, K.2    Kimura, S.3
  • 18
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: a comprehensive database of protein domain families based on seed alignments
    • Sonnhammer E., Eddy S., Durbin R. Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins Struct. Funct. Genet. 1997, 28:405-420.
    • (1997) Proteins Struct. Funct. Genet. , vol.28 , pp. 405-420
    • Sonnhammer, E.1    Eddy, S.2    Durbin, R.3
  • 20
    • 0031962157 scopus 로고    scopus 로고
    • Expression and purification of large nebulin fragments and their interaction with actin
    • Zhang J., Weisberg A., Horowits R. Expression and purification of large nebulin fragments and their interaction with actin. Biophys J. 1998, 74:349-359.
    • (1998) Biophys J. , vol.74 , pp. 349-359
    • Zhang, J.1    Weisberg, A.2    Horowits, R.3
  • 22
    • 0034831138 scopus 로고    scopus 로고
    • Segmental duplications: organization and impact within the current human genome project assembly
    • Bailey J., Yavor A., Massa H., Trask B., Eichler E. Segmental duplications: organization and impact within the current human genome project assembly. Genome Res. 2001, 11:1005-1017. 10.1101/gr.187101.
    • (2001) Genome Res. , vol.11 , pp. 1005-1017
    • Bailey, J.1    Yavor, A.2    Massa, H.3    Trask, B.4    Eichler, E.5
  • 26
    • 77950461601 scopus 로고    scopus 로고
    • Origins and functional impact of copy number variation in the human genome
    • Conrad D., Pinto D., Redon R., Feuk L., Gokcumen O., Zhang Y., et al. Origins and functional impact of copy number variation in the human genome. Nature 2010, 464:704-712. 10.1038/nature08516.
    • (2010) Nature , vol.464 , pp. 704-712
    • Conrad, D.1    Pinto, D.2    Redon, R.3    Feuk, L.4    Gokcumen, O.5    Zhang, Y.6
  • 27
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas C., Bhattacharya N., Cooper J., Gregorio C. Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol. Biol. Cell 2008, 5:1837-1847.
    • (2008) Mol. Biol. Cell , vol.5 , pp. 1837-1847
    • Pappas, C.1    Bhattacharya, N.2    Cooper, J.3    Gregorio, C.4
  • 28
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • Witt C., Burkart C., Labeit D., McNabb M., Wu Y., Granzier H., Labeit S. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J. 2006, 25:3843-3855.
    • (2006) EMBO J. , vol.25 , pp. 3843-3855
    • Witt, C.1    Burkart, C.2    Labeit, D.3    McNabb, M.4    Wu, Y.5    Granzier, H.6    Labeit, S.7
  • 29
    • 61549130938 scopus 로고    scopus 로고
    • A prominent role for segmental duplications in modeling eukaryotic genomes
    • Koszul R., Fischer G. A prominent role for segmental duplications in modeling eukaryotic genomes. C. R. Biol. 2009, 332:254-266.
    • (2009) C. R. Biol. , vol.332 , pp. 254-266
    • Koszul, R.1    Fischer, G.2
  • 30
    • 0142059650 scopus 로고    scopus 로고
    • An Alu transposition model for the origin and expansion of human segmental duplications
    • Bailey J., Liu G., Eichler E. An Alu transposition model for the origin and expansion of human segmental duplications. Am. J. Hum. Genet. 2003, 73:823-834.
    • (2003) Am. J. Hum. Genet. , vol.73 , pp. 823-834
    • Bailey, J.1    Liu, G.2    Eichler, E.3
  • 31
    • 0032478140 scopus 로고    scopus 로고
    • The partial tandem duplication of ALL1 (MLL) is consistently generated by Alu-mediated homologous recombination in acute myeloid leukemia
    • Strout M.P., Marcucci G., Bloomfield C.D., Caligiuri M.A. The partial tandem duplication of ALL1 (MLL) is consistently generated by Alu-mediated homologous recombination in acute myeloid leukemia. Proc. Natl Acad. Sci. 1998, 95:2390.
    • (1998) Proc. Natl Acad. Sci. , vol.95 , pp. 2390
    • Strout, M.P.1    Marcucci, G.2    Bloomfield, C.D.3    Caligiuri, M.A.4
  • 32
    • 0031857253 scopus 로고    scopus 로고
    • Analysis of two duplications of the LDL receptor gene affecting intracellular transport, catabolism, and surface binding of the LDL receptor
    • Patel D. Analysis of two duplications of the LDL receptor gene affecting intracellular transport, catabolism, and surface binding of the LDL receptor. J. Lipid Res. 1998, 39:1466.
    • (1998) J. Lipid Res. , vol.39 , pp. 1466
    • Patel, D.1
  • 33
    • 0031026976 scopus 로고    scopus 로고
    • Duplication of seven exons in the lysyl hydroxylase gene is associated with longer forms of a repetitive sequence within the gene and is a common cause for the type VI variant of Ehlers-Danlos syndrome
    • Heikkinen J., Toppinen T., Yeowell H., Krieg T., Steinmann B., Kivirikko K., Myllylä R. Duplication of seven exons in the lysyl hydroxylase gene is associated with longer forms of a repetitive sequence within the gene and is a common cause for the type VI variant of Ehlers-Danlos syndrome. Am. J. Hum. Genet. 1997, 60:48.
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 48
    • Heikkinen, J.1    Toppinen, T.2    Yeowell, H.3    Krieg, T.4    Steinmann, B.5    Kivirikko, K.6    Myllylä, R.7
  • 34
    • 36248946195 scopus 로고    scopus 로고
    • Identification of an Alu-mediated tandem duplication of exons 8 and 9 in a patient with mitochondrial acetoacetyl-CoA thiolase (T2) deficiency
    • Fukao T., Zhang G., Rolland M.O., Zabot M.T., Guffon N., Aoki Y., Kondo N. Identification of an Alu-mediated tandem duplication of exons 8 and 9 in a patient with mitochondrial acetoacetyl-CoA thiolase (T2) deficiency. Mol. Genet. Metab. 2007, 92:375-378.
    • (2007) Mol. Genet. Metab. , vol.92 , pp. 375-378
    • Fukao, T.1    Zhang, G.2    Rolland, M.O.3    Zabot, M.T.4    Guffon, N.5    Aoki, Y.6    Kondo, N.7
  • 38
    • 45749086679 scopus 로고    scopus 로고
    • The amphioxus genome and the evolution of the chordate karyotype
    • Putnam N., Butts T., Ferrier D., Furlong R., Hellsten U., Kawashima T., et al. The amphioxus genome and the evolution of the chordate karyotype. Nature 2008, 453:1064-1071.
    • (2008) Nature , vol.453 , pp. 1064-1071
    • Putnam, N.1    Butts, T.2    Ferrier, D.3    Furlong, R.4    Hellsten, U.5    Kawashima, T.6
  • 39
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European Molecular Biology Open Software Suite
    • Rice P., Longden I., Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 2000, 16:276-277.
    • (2000) Trends Genet. , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 40
    • 63349085641 scopus 로고    scopus 로고
    • Kalign2: high-performance multiple alignment of protein and nucleotide sequences allowing external features
    • Lassmann T., Frings O., Sonnhammer E. Kalign2: high-performance multiple alignment of protein and nucleotide sequences allowing external features. Nucleic Acids Res. 2009, 37:858-865. 10.1093/nar/gkn1006.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 858-865
    • Lassmann, T.1    Frings, O.2    Sonnhammer, E.3
  • 42
    • 0029654258 scopus 로고
    • A dot-matrix program with dynamic threshold control suited for genomic DNA and protein sequence analysis
    • Sonnhammer E., Durbin R. A dot-matrix program with dynamic threshold control suited for genomic DNA and protein sequence analysis. Gene 1995, 167:1-2.
    • (1995) Gene , vol.167 , pp. 1-2
    • Sonnhammer, E.1    Durbin, R.2
  • 43
    • 0003437299 scopus 로고    scopus 로고
    • Department of Genome Sciences, University of Washington, Seattle, WA, distributed by the author
    • Felsenstein J. PHYLIP (Phylogeny Inference Package) Version 3.6 2004, Department of Genome Sciences, University of Washington, Seattle, WA, distributed by the author.
    • (2004) PHYLIP (Phylogeny Inference Package) Version 3.6
    • Felsenstein, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.