메뉴 건너뛰기




Volumn 21, Issue 1, 2011, Pages 29-37

The Nebulin family: An actin support group

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; CYTOSKELETON PROTEIN; NEBULIN; SCAFFOLD PROTEIN;

EID: 78650556675     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2010.09.005     Document Type: Review
Times cited : (96)

References (89)
  • 1
    • 0019028451 scopus 로고
    • Identification of an N2 line protein of striated muscle
    • Wang K., Williamson C.L. Identification of an N2 line protein of striated muscle. Proc. Natl. Acad. Sci. U. S. A. 1980, 77:3254-3258.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 3254-3258
    • Wang, K.1    Williamson, C.L.2
  • 2
    • 0037427450 scopus 로고    scopus 로고
    • The complete mouse nebulin gene sequence and the identification of cardiac nebulin
    • Kazmierski S.T., et al. The complete mouse nebulin gene sequence and the identification of cardiac nebulin. J. Mol. Biol. 2003, 328:835-846.
    • (2003) J. Mol. Biol. , vol.328 , pp. 835-846
    • Kazmierski, S.T.1
  • 3
    • 33745243854 scopus 로고    scopus 로고
    • Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
    • Bang M.L., et al. Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J. Cell Biol. 2006, 173:905-916.
    • (2006) J. Cell Biol. , vol.173 , pp. 905-916
    • Bang, M.L.1
  • 4
    • 77953141955 scopus 로고    scopus 로고
    • Nebulin regulates actin filament lengths by a stabilization mechanism
    • Pappas C.T., et al. Nebulin regulates actin filament lengths by a stabilization mechanism. J. Cell Biol. 2010, 189:859-870.
    • (2010) J. Cell Biol. , vol.189 , pp. 859-870
    • Pappas, C.T.1
  • 5
    • 0025810111 scopus 로고
    • Evidence that nebulin is a protein-ruler in muscle thin filaments
    • Labeit S., et al. Evidence that nebulin is a protein-ruler in muscle thin filaments. FEBS Lett. 1991, 282:313-316.
    • (1991) FEBS Lett. , vol.282 , pp. 313-316
    • Labeit, S.1
  • 6
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit S., Kolmerer B. The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 1995, 248:308-315.
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 7
    • 0030039635 scopus 로고    scopus 로고
    • Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3
    • Wang K., et al. Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem. 1996, 271:4304-4314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4304-4314
    • Wang, K.1
  • 8
    • 39449127146 scopus 로고    scopus 로고
    • A lasp family protein of Ciona intestinalis
    • Terasaki A.G., et al. A lasp family protein of Ciona intestinalis. Biochim. Biophys. Acta 2008, 1779:51-59.
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 51-59
    • Terasaki, A.G.1
  • 9
    • 67449103076 scopus 로고    scopus 로고
    • Structure of the amphioxus nebulin gene and evolution of the nebulin family genes
    • Hanashima A., et al. Structure of the amphioxus nebulin gene and evolution of the nebulin family genes. Gene 2009, 443:76-82.
    • (2009) Gene , vol.443 , pp. 76-82
    • Hanashima, A.1
  • 10
    • 77956170943 scopus 로고    scopus 로고
    • Nebulin: A study of protein repeat evolution
    • Bjorklund A.K., et al. Nebulin: A study of protein repeat evolution. J. Mol. Biol. 2010, 402:38-51.
    • (2010) J. Mol. Biol. , vol.402 , pp. 38-51
    • Bjorklund, A.K.1
  • 11
    • 33748052051 scopus 로고    scopus 로고
    • Expansion of protein domain repeats
    • Bjorklund A.K., et al. Expansion of protein domain repeats. PLoS Comput. Biol. 2006, 2:e114.
    • (2006) PLoS Comput. Biol. , vol.2
    • Bjorklund, A.K.1
  • 12
    • 0036289599 scopus 로고    scopus 로고
    • The bacterial protein SipA polymerizes G-actin and mimics muscle nebulin
    • Galkin V.E., et al. The bacterial protein SipA polymerizes G-actin and mimics muscle nebulin. Nat. Struct. Biol. 2002, 9:518-521.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 518-521
    • Galkin, V.E.1
  • 13
    • 0033605618 scopus 로고    scopus 로고
    • Role of the S. typhimurium actin-binding protein SipA in bacterial internalization
    • Zhou D., et al. Role of the S. typhimurium actin-binding protein SipA in bacterial internalization. Science 1999, 283:2092-2095.
    • (1999) Science , vol.283 , pp. 2092-2095
    • Zhou, D.1
  • 14
    • 24944524470 scopus 로고    scopus 로고
    • Nebulin regulates the assembly and lengths of the thin filaments in striated muscle
    • McElhinny A.S., et al. Nebulin regulates the assembly and lengths of the thin filaments in striated muscle. J. Cell Biol. 2005, 170:947-957.
    • (2005) J. Cell Biol. , vol.170 , pp. 947-957
    • McElhinny, A.S.1
  • 15
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • Witt C.C., et al. 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.C.1
  • 16
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas C.T., et al. Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol. Biol. Cell 2008, 19:1837-1847.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1837-1847
    • Pappas, C.T.1
  • 17
    • 64049087454 scopus 로고    scopus 로고
    • A myopathy-linked desmin mutation perturbs striated muscle actin filament architecture
    • Conover G.M., et al. A myopathy-linked desmin mutation perturbs striated muscle actin filament architecture. Mol. Biol. Cell 2009, 20:834-845.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 834-845
    • Conover, G.M.1
  • 18
    • 65549092824 scopus 로고    scopus 로고
    • A nebulin ruler does not dictate thin filament lengths
    • Castillo A., et al. A nebulin ruler does not dictate thin filament lengths. Biophys. J. 2009, 96:1856-1865.
    • (2009) Biophys. J. , vol.96 , pp. 1856-1865
    • Castillo, A.1
  • 19
    • 0035808418 scopus 로고    scopus 로고
    • The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments
    • McElhinny A.S., et al. The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. J. Biol. Chem. 2001, 276:583-592.
    • (2001) J. Biol. Chem. , vol.276 , pp. 583-592
    • McElhinny, A.S.1
  • 20
    • 0036841312 scopus 로고    scopus 로고
    • Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping
    • Krieger I., et al. Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. Biophys. J. 2002, 83:2716-2725.
    • (2002) Biophys. J. , vol.83 , pp. 2716-2725
    • Krieger, I.1
  • 21
    • 0032508463 scopus 로고    scopus 로고
    • Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs
    • Millevoi S., et al. Characterization of nebulette and nebulin and emerging concepts of their roles for vertebrate Z-discs. J. Mol. Biol. 1998, 282:111-123.
    • (1998) J. Mol. Biol. , vol.282 , pp. 111-123
    • Millevoi, S.1
  • 22
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • Bang M.L., et al. Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J. Struct. Biol. 2002, 137:119-127.
    • (2002) J. Struct. Biol. , vol.137 , pp. 119-127
    • Bang, M.L.1
  • 23
    • 0037031320 scopus 로고    scopus 로고
    • Actin dynamics: tropomyosin provides stability
    • Cooper J.A. Actin dynamics: tropomyosin provides stability. Curr. Biol. 2002, 12:R523-525.
    • (2002) Curr. Biol. , vol.12
    • Cooper, J.A.1
  • 24
    • 67650078502 scopus 로고    scopus 로고
    • Nanomechanics of full-length nebulin: an elastic strain gauge in the skeletal muscle sarcomere
    • Yadavalli V.K., et al. Nanomechanics of full-length nebulin: an elastic strain gauge in the skeletal muscle sarcomere. Langmuir 2009, 25:7496-7505.
    • (2009) Langmuir , vol.25 , pp. 7496-7505
    • Yadavalli, V.K.1
  • 25
    • 76649104716 scopus 로고    scopus 로고
    • Reduced myofibrillar connectivity and increased Z-disk width in nebulin-deficient skeletal muscle
    • Tonino P., et al. Reduced myofibrillar connectivity and increased Z-disk width in nebulin-deficient skeletal muscle. J. Cell Sci. 2010, 123:384-391.
    • (2010) J. Cell Sci. , vol.123 , pp. 384-391
    • Tonino, P.1
  • 26
    • 77951974179 scopus 로고    scopus 로고
    • Differential splicing of the large sarcomeric protein nebulin during skeletal muscle development
    • Buck D., et al. Differential splicing of the large sarcomeric protein nebulin during skeletal muscle development. J. Struct. Biol. 2010, 170:325-333.
    • (2010) J. Struct. Biol. , vol.170 , pp. 325-333
    • Buck, D.1
  • 27
    • 66149095797 scopus 로고    scopus 로고
    • Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties
    • Gokhin D.S., et al. Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties. Am. J. Physiol. Cell Physiol. 2009, 296:C1123-1132.
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Gokhin, D.S.1
  • 28
    • 71449111552 scopus 로고    scopus 로고
    • Nebulin alters cross-bridge cycling kinetics and increases thin filament activation: a novel mechanism for increasing tension and reducing tension cost
    • Chandra M., et al. Nebulin alters cross-bridge cycling kinetics and increases thin filament activation: a novel mechanism for increasing tension and reducing tension cost. J. Biol. Chem. 2009, 284:30889-30896.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30889-30896
    • Chandra, M.1
  • 29
    • 72749126316 scopus 로고    scopus 로고
    • Nebulin plays a direct role in promoting strong actin-myosin interactions
    • Bang M.L., et al. Nebulin plays a direct role in promoting strong actin-myosin interactions. FASEB J. 2009, 23:4117-4125.
    • (2009) FASEB J. , vol.23 , pp. 4117-4125
    • Bang, M.L.1
  • 30
    • 48749123823 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum calcium uptake and speed of relaxation are depressed in nebulin-free skeletal muscle
    • Ottenheijm C.A., et al. Sarcoplasmic reticulum calcium uptake and speed of relaxation are depressed in nebulin-free skeletal muscle. FASEB J. 2008, 22:2912-2919.
    • (2008) FASEB J. , vol.22 , pp. 2912-2919
    • Ottenheijm, C.A.1
  • 31
    • 34249697100 scopus 로고    scopus 로고
    • Muscle intermediate filaments and their links to membranes and membranous organelles
    • Capetanaki Y., et al. Muscle intermediate filaments and their links to membranes and membranous organelles. Exp. Cell Res. 2007, 313:2063-2076.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2063-2076
    • Capetanaki, Y.1
  • 32
    • 0018571673 scopus 로고
    • Desmin and vimentin coexist at the periphery of the myofibril Z disc
    • Granger B.L., Lazarides E. Desmin and vimentin coexist at the periphery of the myofibril Z disc. Cell 1979, 18:1053-1063.
    • (1979) Cell , vol.18 , pp. 1053-1063
    • Granger, B.L.1    Lazarides, E.2
  • 33
    • 0028784365 scopus 로고
    • Nebulette: a 107kD nebulin-like protein in cardiac muscle
    • Moncman C.L., Wang K. Nebulette: a 107kD nebulin-like protein in cardiac muscle. Cell Motil. Cytoskeleton 1995, 32:205-225.
    • (1995) Cell Motil. Cytoskeleton , vol.32 , pp. 205-225
    • Moncman, C.L.1    Wang, K.2
  • 34
    • 0036061465 scopus 로고    scopus 로고
    • Targeted disruption of nebulette protein expression alters cardiac myofibril assembly and function
    • Moncman C.L., Wang K. Targeted disruption of nebulette protein expression alters cardiac myofibril assembly and function. Exp. Cell Res. 2002, 273:204-218.
    • (2002) Exp. Cell Res. , vol.273 , pp. 204-218
    • Moncman, C.L.1    Wang, K.2
  • 35
    • 84954358724 scopus 로고    scopus 로고
    • The nebulette repeat domain is necessary for proper maintenance of tropomyosin with the cardiac sarcomere
    • Bonzo J.R., et al. The nebulette repeat domain is necessary for proper maintenance of tropomyosin with the cardiac sarcomere. Exp. Cell Res. 2008, 314:3519-3530.
    • (2008) Exp. Cell Res. , vol.314 , pp. 3519-3530
    • Bonzo, J.R.1
  • 36
    • 0348030000 scopus 로고    scopus 로고
    • Identification and characterization of LASP2 gene in silico
    • Katoh M. Identification and characterization of LASP2 gene in silico. Int. J. Mol. Med. 2003, 12:405-410.
    • (2003) Int. J. Mol. Med. , vol.12 , pp. 405-410
    • Katoh, M.1
  • 37
    • 0347481319 scopus 로고    scopus 로고
    • A novel LIM and SH3 protein (lasp-2) highly expressing in chicken brain
    • Terasaki A.G., et al. A novel LIM and SH3 protein (lasp-2) highly expressing in chicken brain. Biochem. Biophys. Res. Commun. 2004, 313:48-54.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 48-54
    • Terasaki, A.G.1
  • 38
    • 2442576932 scopus 로고    scopus 로고
    • Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1
    • Li B., et al. 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
  • 39
    • 37549035082 scopus 로고    scopus 로고
    • Lasp-2 expression, localization, and ligand interactions: a new Z-disc scaffolding protein
    • Zieseniss A., et al. 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
  • 40
    • 53049091406 scopus 로고    scopus 로고
    • Ectopic expression of LIM-nebulette (LASP2) reveals roles in cell migration and spreading
    • Deng X.A., et al. Ectopic expression of LIM-nebulette (LASP2) reveals roles in cell migration and spreading. Cell Motil. Cytoskeleton 2008, 65:827-840.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 827-840
    • Deng, X.A.1
  • 41
    • 33845793833 scopus 로고    scopus 로고
    • Linker region of nebulin family members plays an important role in targeting these molecules to cellular structures
    • Panaviene Z., Moncman C.L. Linker region of nebulin family members plays an important role in targeting these molecules to cellular structures. Cell Tissue Res. 2007, 327:353-369.
    • (2007) Cell Tissue Res. , vol.327 , pp. 353-369
    • Panaviene, Z.1    Moncman, C.L.2
  • 42
    • 43049128509 scopus 로고    scopus 로고
    • The LIM and SH3 domain protein family: structural proteins or signal transducers or both?
    • Grunewald T.G., Butt E. The LIM and SH3 domain protein family: structural proteins or signal transducers or both?. Mol. Cancer 2008, 7:31.
    • (2008) Mol. Cancer , vol.7 , pp. 31
    • Grunewald, T.G.1    Butt, E.2
  • 43
    • 33646593154 scopus 로고    scopus 로고
    • Short-term retention of actin filament binding proteins on lamellipodial actin bundles
    • Nakagawa H., et al. Short-term retention of actin filament binding proteins on lamellipodial actin bundles. FEBS Lett. 2006, 580:3223-3228.
    • (2006) FEBS Lett. , vol.580 , pp. 3223-3228
    • Nakagawa, H.1
  • 44
    • 33645214432 scopus 로고    scopus 로고
    • Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells
    • Grunewald T.G., et al. Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. Exp. Cell Res. 2006, 312:974-982.
    • (2006) Exp. Cell Res. , vol.312 , pp. 974-982
    • Grunewald, T.G.1
  • 45
    • 0037115487 scopus 로고    scopus 로고
    • Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo
    • Chew C.S., et al. Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. J. Cell Sci. 2002, 115:4787-4799.
    • (2002) J. Cell Sci. , vol.115 , pp. 4787-4799
    • Chew, C.S.1
  • 46
    • 0028864219 scopus 로고
    • Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains
    • Tomasetto C., et al. Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. FEBS Lett. 1995, 373:245-249.
    • (1995) FEBS Lett. , vol.373 , pp. 245-249
    • Tomasetto, C.1
  • 47
    • 2442474012 scopus 로고    scopus 로고
    • Regulation of cell migration and survival by focal adhesion targeting of Lasp-1
    • Lin Y.H., et al. Regulation of cell migration and survival by focal adhesion targeting of Lasp-1. J. Cell Biol. 2004, 165:421-432.
    • (2004) J. Cell Biol. , vol.165 , pp. 421-432
    • Lin, Y.H.1
  • 48
    • 77956325999 scopus 로고    scopus 로고
    • LIM and SH3 protein-1 modulates CXCR2-mediated cell migration
    • Raman D., et al. LIM and SH3 protein-1 modulates CXCR2-mediated cell migration. PLoS One 2010, 5:e10050.
    • (2010) PLoS One , vol.5
    • Raman, D.1
  • 49
    • 59349096434 scopus 로고    scopus 로고
    • LIM and SH3 protein 1 (Lasp1) is a novel p53 transcriptional target involved in hepatocellular carcinoma
    • Wang B., et al. LIM and SH3 protein 1 (Lasp1) is a novel p53 transcriptional target involved in hepatocellular carcinoma. J. Hepatol. 2009, 50:528-537.
    • (2009) J. Hepatol. , vol.50 , pp. 528-537
    • Wang, B.1
  • 50
    • 33846543020 scopus 로고    scopus 로고
    • Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation
    • Grunewald T.G., et al. Overexpression of LASP-1 mediates migration and proliferation of human ovarian cancer cells and influences zyxin localisation. Br. J. Cancer 2007, 96:296-305.
    • (2007) Br. J. Cancer , vol.96 , pp. 296-305
    • Grunewald, T.G.1
  • 51
    • 68849118742 scopus 로고    scopus 로고
    • Lasp1 gene disruption is linked to enhanced cell migration and tumor formation
    • Zhang H., et al. Lasp1 gene disruption is linked to enhanced cell migration and tumor formation. Physiol. Genomics 2009, 38:372-385.
    • (2009) Physiol. Genomics , vol.38 , pp. 372-385
    • Zhang, H.1
  • 52
    • 37549005081 scopus 로고    scopus 로고
    • Nuclear localization and cytosolic overexpression of LASP-1 correlates with tumor size and nodal-positivity of human breast carcinoma
    • Grunewald T.G., et al. Nuclear localization and cytosolic overexpression of LASP-1 correlates with tumor size and nodal-positivity of human breast carcinoma. BMC Cancer 2007, 7:198.
    • (2007) BMC Cancer , vol.7 , pp. 198
    • Grunewald, T.G.1
  • 53
    • 77952889009 scopus 로고    scopus 로고
    • Nuclear localisation of LASP-1 correlates with poor long-term survival in female breast cancer
    • Frietsch J.J., et al. Nuclear localisation of LASP-1 correlates with poor long-term survival in female breast cancer. Br. J. Cancer 2010, 102:1645-1653.
    • (2010) Br. J. Cancer , vol.102 , pp. 1645-1653
    • Frietsch, J.J.1
  • 54
    • 66149149492 scopus 로고    scopus 로고
    • Myofibril assembly visualized by imaging N-RAP, alpha-actinin, and actin in living cardiomyocytes
    • Manisastry S.M., et al. Myofibril assembly visualized by imaging N-RAP, alpha-actinin, and actin in living cardiomyocytes. Exp. Cell Res. 2009, 315:2126-2139.
    • (2009) Exp. Cell Res. , vol.315 , pp. 2126-2139
    • Manisastry, S.M.1
  • 55
    • 33746674413 scopus 로고    scopus 로고
    • Targeted disruption of N-RAP gene function by RNA interference: a role for N-RAP in myofibril organization
    • Dhume A., et al. Targeted disruption of N-RAP gene function by RNA interference: a role for N-RAP in myofibril organization. Cell Motil. Cytoskeleton 2006, 63:493-511.
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 493-511
    • Dhume, A.1
  • 56
    • 0030820989 scopus 로고    scopus 로고
    • Complete cDNA sequence and tissue localization of N-RAP, a novel nebulin-related protein of striated muscle
    • Luo G., et al. Complete cDNA sequence and tissue localization of N-RAP, a novel nebulin-related protein of striated muscle. Cell Motil. Cytoskeleton 1997, 38:75-90.
    • (1997) Cell Motil. Cytoskeleton , vol.38 , pp. 75-90
    • Luo, G.1
  • 57
    • 0346656820 scopus 로고    scopus 로고
    • N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes
    • Carroll S., et al. N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes. J. Cell Sci. 2004, 117:105-114.
    • (2004) J. Cell Sci. , vol.117 , pp. 105-114
    • Carroll, S.1
  • 58
    • 17444401402 scopus 로고    scopus 로고
    • N-RAP expression during mouse heart development
    • Lu S., et al. N-RAP expression during mouse heart development. Dev. Dyn. 2005, 233:201-212.
    • (2005) Dev. Dyn. , vol.233 , pp. 201-212
    • Lu, S.1
  • 59
    • 57349168177 scopus 로고    scopus 로고
    • Expression and alternative splicing of N-RAP during mouse skeletal muscle development
    • Lu S., et al. Expression and alternative splicing of N-RAP during mouse skeletal muscle development. Cell Motil. Cytoskeleton 2008, 65:945-954.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 945-954
    • Lu, S.1
  • 60
    • 77953517918 scopus 로고    scopus 로고
    • Isolation of nebulin from rabbit skeletal muscle and its interaction with actin
    • Chitose R., et al. Isolation of nebulin from rabbit skeletal muscle and its interaction with actin. J. Biomed. Biotechnol. 2010, 2010:108495.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 108495
    • Chitose, R.1
  • 61
    • 1842858197 scopus 로고    scopus 로고
    • Striated muscle cytoarchitecture: an intricate web of form and function
    • Clark K.A., et al. Striated muscle cytoarchitecture: an intricate web of form and function. Annu. Rev. Cell Dev. Biol. 2002, 18:637-706.
    • (2002) Annu. Rev. Cell Dev. Biol. , vol.18 , pp. 637-706
    • Clark, K.A.1
  • 62
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling
    • Luther P.K. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. J. Muscle Res. Cell Motil. 2009, 30:171-185.
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 171-185
    • Luther, P.K.1
  • 63
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: a nodal point in signalling and disease
    • Frank D., et al. The sarcomeric Z-disc: a nodal point in signalling and disease. J. Mol. Med. 2006, 84:446-468.
    • (2006) J. Mol. Med. , vol.84 , pp. 446-468
    • Frank, D.1
  • 64
    • 33746800269 scopus 로고    scopus 로고
    • Focal adhesions: what's new inside
    • Lo S.H. Focal adhesions: what's new inside. Dev. Biol. 2006, 294:280-291.
    • (2006) Dev. Biol. , vol.294 , pp. 280-291
    • Lo, S.H.1
  • 65
    • 3042799330 scopus 로고    scopus 로고
    • Focal adhesion regulation of cell behavior
    • Wozniak M.A., et al. Focal adhesion regulation of cell behavior. Biochim. Biophys. Acta 2004, 1692:103-119.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 103-119
    • Wozniak, M.A.1
  • 66
    • 0021712727 scopus 로고
    • Length determination in bacteriophage lambda tails
    • Katsura I., Hendrix R.W. Length determination in bacteriophage lambda tails. Cell 1984, 39:691-698.
    • (1984) Cell , vol.39 , pp. 691-698
    • Katsura, I.1    Hendrix, R.W.2
  • 67
    • 0028307501 scopus 로고
    • Tail length determination in bacteriophage T4
    • Abuladze N.K., et al. Tail length determination in bacteriophage T4. Virology 1994, 199:301-310.
    • (1994) Virology , vol.199 , pp. 301-310
    • Abuladze, N.K.1
  • 68
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L., et al. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 2003, 302:1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1
  • 69
    • 0028091960 scopus 로고
    • Titin and nebulin: protein rulers in muscle?
    • Trinick J. Titin and nebulin: protein rulers in muscle?. Trends Biochem. Sci. 1994, 19:405-409.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 405-409
    • Trinick, J.1
  • 70
    • 33644829176 scopus 로고    scopus 로고
    • Nebulin regulation of actin filament lengths: new angles
    • Horowits R. Nebulin regulation of actin filament lengths: new angles. Trends Cell Biol. 2006, 16:121-124.
    • (2006) Trends Cell Biol. , vol.16 , pp. 121-124
    • Horowits, R.1
  • 71
    • 0038353769 scopus 로고    scopus 로고
    • Nebulin: the nebulous, multifunctional giant of striated muscle
    • McElhinny A.S., et al. Nebulin: the nebulous, multifunctional giant of striated muscle. Trends Cardiovasc. Med. 2003, 13:195-201.
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 195-201
    • McElhinny, A.S.1
  • 72
    • 0025840415 scopus 로고
    • Cloning, expression, and protein interaction of human nebulin fragments composed of varying numbers of sequence modules
    • Jin J.P., Wang K. Cloning, expression, and protein interaction of human nebulin fragments composed of varying numbers of sequence modules. J. Biol. Chem. 1991, 266:21215-21223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21215-21223
    • Jin, J.P.1    Wang, K.2
  • 73
    • 0027331352 scopus 로고
    • Nebulin is a full-length template of actin filaments in the skeletal muscle sarcomere: an immunoelectron microscopic study of its orientation and span with site-specific monoclonal antibodies
    • Wright J., et al. Nebulin is a full-length template of actin filaments in the skeletal muscle sarcomere: an immunoelectron microscopic study of its orientation and span with site-specific monoclonal antibodies. J. Muscle Res. Cell Motil. 1993, 14:476-483.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 476-483
    • Wright, J.1
  • 74
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M., et al. Nebulin, a helical actin binding protein. EMBO J. 1994, 13:1782-1789.
    • (1994) EMBO J. , vol.13 , pp. 1782-1789
    • Pfuhl, M.1
  • 75
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile
    • Kruger M., et al. Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile. J. Cell Biol. 1991, 115:97-107.
    • (1991) J. Cell Biol. , vol.115 , pp. 97-107
    • Kruger, M.1
  • 76
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line
    • Wang K., Wright J. Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 1988, 107:2199-2212.
    • (1988) J. Cell Biol. , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 77
    • 0029966287 scopus 로고    scopus 로고
    • Correlation between conformational and binding properties of nebulin repeats
    • Pfuhl M., et al. Correlation between conformational and binding properties of nebulin repeats. J. Mol. Biol. 1996, 257:367-384.
    • (1996) J. Mol. Biol. , vol.257 , pp. 367-384
    • Pfuhl, M.1
  • 78
    • 30044449953 scopus 로고    scopus 로고
    • Nebulin: does it measure up as a ruler?
    • Fowler V.M., et al. Nebulin: does it measure up as a ruler?. Curr. Biol. 2006, 16:R18-20.
    • (2006) Curr. Biol. , vol.16
    • Fowler, V.M.1
  • 79
    • 70349755728 scopus 로고    scopus 로고
    • Core-rod myopathy caused by mutations in the nebulin gene
    • Romero N.B., et al. Core-rod myopathy caused by mutations in the nebulin gene. Neurology 2009, 73:1159-1161.
    • (2009) Neurology , vol.73 , pp. 1159-1161
    • Romero, N.B.1
  • 80
    • 0034906020 scopus 로고    scopus 로고
    • Clinical and genetic heterogeneity in nemaline myopathy--a disease of skeletal muscle thin filaments
    • Sanoudou D., Beggs A.H. Clinical and genetic heterogeneity in nemaline myopathy--a disease of skeletal muscle thin filaments. Trends Mol. Med. 2001, 7:362-368.
    • (2001) Trends Mol. Med. , vol.7 , pp. 362-368
    • Sanoudou, D.1    Beggs, A.H.2
  • 81
    • 34250854550 scopus 로고    scopus 로고
    • Distal myopathy caused by homozygous missense mutations in the nebulin gene
    • Wallgren-Pettersson C., et al. Distal myopathy caused by homozygous missense mutations in the nebulin gene. Brain 2007, 130:1465-1476.
    • (2007) Brain , vol.130 , pp. 1465-1476
    • Wallgren-Pettersson, C.1
  • 82
    • 0036788820 scopus 로고    scopus 로고
    • Nebulin mutations in autosomal recessive nemaline myopathy: an update
    • Pelin K., et al. Nebulin mutations in autosomal recessive nemaline myopathy: an update. Neuromuscul. Disord. 2002, 12:680-686.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 680-686
    • Pelin, K.1
  • 83
    • 67249115136 scopus 로고    scopus 로고
    • Thin filament length dysregulation contributes to muscle weakness in nemaline myopathy patients with nebulin deficiency
    • Ottenheijm C.A., et al. Thin filament length dysregulation contributes to muscle weakness in nemaline myopathy patients with nebulin deficiency. Hum. Mol. Genet. 2009, 18:2359-2369.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2359-2369
    • Ottenheijm, C.A.1
  • 84
    • 77951974414 scopus 로고    scopus 로고
    • Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2)
    • Ottenheijm C.A., et al. Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2). J. Struct. Biol. 2010, 170:334-343.
    • (2010) J. Struct. Biol. , vol.170 , pp. 334-343
    • Ottenheijm, C.A.1
  • 85
    • 77958011915 scopus 로고    scopus 로고
    • Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis
    • Purevjav E., et al. Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis. J. Am. College Cardiol. 2010, 56:1493-1502.
    • (2010) J. Am. College Cardiol. , vol.56 , pp. 1493-1502
    • Purevjav, E.1
  • 86
    • 17744380992 scopus 로고    scopus 로고
    • Characterization of the human nebulette gene: a polymorphism in an actin-binding motif is associated with nonfamilial idiopathic dilated cardiomyopathy
    • Arimura T., et al. Characterization of the human nebulette gene: a polymorphism in an actin-binding motif is associated with nonfamilial idiopathic dilated cardiomyopathy. Hum. Genet. 2000, 107:440-451.
    • (2000) Hum. Genet. , vol.107 , pp. 440-451
    • Arimura, T.1
  • 87
    • 0031985092 scopus 로고    scopus 로고
    • Myofibril degeneration caused by tropomodulin overexpression leads to dilated cardiomyopathy in juvenile mice
    • Sussman M.A., et al. Myofibril degeneration caused by tropomodulin overexpression leads to dilated cardiomyopathy in juvenile mice. J. Clin. Invest. 1998, 101:51-61.
    • (1998) J. Clin. Invest. , vol.101 , pp. 51-61
    • Sussman, M.A.1
  • 88
    • 0035858885 scopus 로고    scopus 로고
    • Alterations at the intercalated disk associated with the absence of muscle LIM protein
    • Ehler E., et al. Alterations at the intercalated disk associated with the absence of muscle LIM protein. J. Cell Biol. 2001, 153:763-772.
    • (2001) J. Cell Biol. , vol.153 , pp. 763-772
    • Ehler, E.1
  • 89
    • 78650553932 scopus 로고    scopus 로고
    • Cover image. In Cell Motil. Cytoskeleton 65, Wiley-Liss
    • Zieseniss, A. (2008) Cover image. In Cell Motil. Cytoskeleton 65, Wiley-Liss.
    • (2008)
    • Zieseniss, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.