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Volumn 12, Issue 2, 2012, Pages 203-225

The interactome of LIM domain proteins: The contributions of LIM domain proteins to heart failure and heart development

Author keywords

Bioinformatics; Heart development; Heart failure; Interactome; LIM domain proteins; Multi protein complex

Indexed keywords

ACTIN BINDING LIM 3 PROTEIN; ATRIAL NATRIURETIC FACTOR; CYSTEINE; DYXIN; F BOX ONLY PROTEIN 20; F BOX PROTEIN; FOUR AND A HALF LIM DOMAINS PROTEIN 1; FOUR AND A HALF LIM DOMAINS PROTEIN 2; GLYCINE RICH PROTEIN 1; GLYCINE RICH PROTEIN 2; HYDROGEN PEROXIDE INDUCIBLE CLONE 5 PROTEIN; INSULIN GENE ENHANCER PROTEIN 1; LIM DOMAIN BINDING PROTEIN 3; LIM DOMAIN PROTEIN 5; LIM DOMAIN PROTEIN 7; LIM HOMEOBOX PROTEIN 9; LIM KINASE 1; LIM KINASE 2; LIM PROTEIN; MIGFILIN; MUSCLE LIM PROTEIN; NEBULIN; NEBULIN RELATED ANCHORING PROTEIN; PAXILLIN; PDZ PROTEIN; PROTEIN SH3; RHOMBOTIN 2; THYMOSIN BETA4; UNCLASSIFIED DRUG; ZYXIN; ZYXIN RELATED PROTEIN 1;

EID: 84855981967     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100492     Document Type: Review
Times cited : (45)

References (193)
  • 1
    • 0025328511 scopus 로고
    • Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin-II
    • Freyd, G., Kim, S. K., Horvitz, H. R., Novel cysteine-rich motif and homeodomain in the product of the Caenorhabditis elegans cell lineage gene lin-II. Nature 1990, 344, 876-879.
    • (1990) Nature , vol.344 , pp. 876-879
    • Freyd, G.1    Kim, S.K.2    Horvitz, H.R.3
  • 2
    • 0031966041 scopus 로고    scopus 로고
    • LIM domains: Multiple roles as adapters and functional modifiers in protein interactions
    • Dawid, I. B., Breen, J., Toyama, R., LIM domains: Multiple roles as adapters and functional modifiers in protein interactions. Trends Genet. 1998, 14, 56-62.
    • (1998) Trends Genet. , vol.14 , pp. 56-62
    • Dawid, I.B.1    Breen, J.2    Toyama, R.3
  • 3
    • 34548420681 scopus 로고    scopus 로고
    • The diverse biofunctions of LIM domain proteins: determined by subcellular localization and protein-protein interaction
    • Zheng, Q., Zhao, Y., The diverse biofunctions of LIM domain proteins: determined by subcellular localization and protein-protein interaction. Biol. Cell 2007, 099, 489-502.
    • (2007) Biol. Cell , vol.99 , pp. 489-502
    • Zheng, Q.1    Zhao, Y.2
  • 4
    • 8444240109 scopus 로고    scopus 로고
    • The LIM domain: From the cytoskeleton to the nucleus
    • Kadrmas, J. L., Beckerle, M. C., The LIM domain: From the cytoskeleton to the nucleus. Nat. Rev. Mol. Cell. Biol. 2004, 5, 920-931.
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 920-931
    • Kadrmas, J.L.1    Beckerle, M.C.2
  • 5
    • 0028279782 scopus 로고
    • Mutational analysis of the metal sites in an Lim domain
    • Michelsen, J. W., Sewell, A. K., Louis, H. A., Olsen, J. I. et al., Mutational analysis of the metal sites in an Lim domain. J. Biol. Chem. 1994, 269, 11108-11113.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11108-11113
    • Michelsen, J.W.1    Sewell, A.K.2    Louis, H.A.3    Olsen, J.I.4
  • 6
    • 0027439276 scopus 로고
    • The cysteine-rich Lim domains inhibit DNA-binding by the associated homeodomain in Isl-1
    • Sanchezgarcia, I., Osada, H., Forster, A., Rabbitts, T. H., The cysteine-rich Lim domains inhibit DNA-binding by the associated homeodomain in Isl-1. EMBO J. 1993, 12, 4243-4250.
    • (1993) EMBO J. , vol.12 , pp. 4243-4250
    • Sanchezgarcia, I.1    Osada, H.2    Forster, A.3    Rabbitts, T.H.4
  • 7
    • 0027892020 scopus 로고
    • Cooperative interactions between the Caenorhabditis elegans homeoproteins Unc-86 and Mec-3
    • Xue, D., Tu, Y., Chalfie, M., Cooperative interactions between the Caenorhabditis elegans homeoproteins Unc-86 and Mec-3. Science 1993, 261, 1324-1328.
    • (1993) Science , vol.261 , pp. 1324-1328
    • Xue, D.1    Tu, Y.2    Chalfie, M.3
  • 8
    • 0036008284 scopus 로고    scopus 로고
    • LIM proteins: Association with the actin cytoskeleton
    • Khurana, T., Khurana, B., Noegel, A. A., LIM proteins: Association with the actin cytoskeleton. Protoplasma 2002, 219, 1-12.
    • (2002) Protoplasma , vol.219 , pp. 1-12
    • Khurana, T.1    Khurana, B.2    Noegel, A.A.3
  • 9
    • 78651319979 scopus 로고    scopus 로고
    • Ongoing and future developments at the Universal Protein Resource
    • Consortium, T. U., Ongoing and future developments at the Universal Protein Resource. Nucleic Acid Res. 2011, 39, D214-D219.
    • (2011) Nucleic Acid Res. , vol.39
    • Consortium, T.U.1
  • 10
    • 0038110087 scopus 로고    scopus 로고
    • Genomic organization, alternative splicing, and expression of human and mouse N-RAP, a nebulin-related LIM protein of striated muscle
    • Mohiddin, S. A., Lu, S., Cardoso, J.-P., Carroll, S. et al., Genomic organization, alternative splicing, and expression of human and mouse N-RAP, a nebulin-related LIM protein of striated muscle. Cell Motil. Cytoskeleton 2003, 55, 200-212.
    • (2003) Cell Motil. Cytoskeleton , vol.55 , pp. 200-212
    • Mohiddin, S.A.1    Lu, S.2    Cardoso, J.-P.3    Carroll, S.4
  • 11
    • 0035858885 scopus 로고    scopus 로고
    • Alterations at the intercalated disk associated with the absence of muscle Lim protein
    • Ehler, E., Horowits, R., Zuppinger, C., Price, R. L. 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    Horowits, R.2    Zuppinger, C.3    Price, R.L.4
  • 12
    • 0035846582 scopus 로고    scopus 로고
    • Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart
    • Zhang, J. Q., Elzey, B., Williams, G., Lu, S. et al., Ultrastructural and biochemical localization of N-RAP at the interface between myofibrils and intercalated disks in the mouse heart. Biochemistry 2001, 40, 14898-14906.
    • (2001) Biochemistry , vol.40 , pp. 14898-14906
    • Zhang, J.Q.1    Elzey, B.2    Williams, G.3    Lu, S.4
  • 13
    • 84855913811 scopus 로고    scopus 로고
    • Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle
    • Crawford, G., Horowits, R., Scaffolds and chaperones in myofibril assembly: putting the striations in striated muscle. Biophys. Rev. 2011, 3, 25-32.
    • (2011) Biophys. Rev. , vol.3 , pp. 25-32
    • Crawford, G.1    Horowits, R.2
  • 14
    • 50649110727 scopus 로고    scopus 로고
    • Role of nonmuscle myosin IIB and N-RAP in cell spreading and myofibril assembly in primary mouse cardiomyocytes
    • Lu, S., Horowits, R., Role of nonmuscle myosin IIB and N-RAP in cell spreading and myofibril assembly in primary mouse cardiomyocytes. Cell Motil. Cytoskeleton 2008, 65, 747-761.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 747-761
    • Lu, S.1    Horowits, R.2
  • 15
    • 0037672668 scopus 로고    scopus 로고
    • New N-RAP-binding partners α-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly
    • Lu, S., Carroll, S. L., Herrera, A. H., Ozanne, B., Horowits, R., New N-RAP-binding partners α-actinin, filamin and Krp1 detected by yeast two-hybrid screening: implications for myofibril assembly. J. Cell Sci. 2003, 116, 2169-2178.
    • (2003) J. Cell Sci. , vol.116 , pp. 2169-2178
    • Lu, S.1    Carroll, S.L.2    Herrera, A.H.3    Ozanne, B.4    Horowits, R.5
  • 16
    • 0346656820 scopus 로고    scopus 로고
    • N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes
    • Carroll, S., Lu, S., Herrera, A. H., Horowits, R., 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    Lu, S.2    Herrera, A.H.3    Horowits, R.4
  • 17
    • 0037237653 scopus 로고    scopus 로고
    • Dilated cardiomyopathy: a disease of the intercalated disc?
    • Perriard, J.-C., Hirschy, A., Ehler, E., Dilated cardiomyopathy: a disease of the intercalated disc? Trends Cardiovasc. Med. 2003, 13, 30-38.
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 30-38
    • Perriard, J.-C.1    Hirschy, A.2    Ehler, E.3
  • 18
    • 79953091335 scopus 로고    scopus 로고
    • Cardiac-specific NRAP overexpression causes right ventricular dysfunction in mice
    • Lu, S., Crawford, G. L., Dore, J., Anderson, S. A. et al., Cardiac-specific NRAP overexpression causes right ventricular dysfunction in mice. Exp. Cell Res. 2011, 317, 1226-1237.
    • (2011) Exp. Cell Res. , vol.317 , pp. 1226-1237
    • Lu, S.1    Crawford, G.L.2    Dore, J.3    Anderson, S.A.4
  • 19
    • 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 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
  • 23
    • 84954358724 scopus 로고    scopus 로고
    • The nebulette repeat domain is necessary for proper maintenance of tropomyosin with the cardiac sarcomere
    • Bonzo, J. R., Norris, A. A., Esham, M., Moncman, C. L., 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    Norris, A.A.2    Esham, M.3    Moncman, C.L.4
  • 24
    • 0032860929 scopus 로고    scopus 로고
    • Functional dissection of nebulette demonstrates actin binding of nebulin-like repeats and Z-line targeting of SH3 and linker domains
    • Moncman, C. L., Wang, K., Functional dissection of nebulette demonstrates actin binding of nebulin-like repeats and Z-line targeting of SH3 and linker domains. Cell Motil. Cytoskeleton 1999, 44, 1-22.
    • (1999) Cell Motil. Cytoskeleton , vol.44 , pp. 1-22
    • Moncman, C.L.1    Wang, K.2
  • 25
    • 77958011915 scopus 로고    scopus 로고
    • Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis
    • Purevjav, E., Varela, J., Morgado, M., Kearney, D. L. et al., Nebulette mutations are associated with dilated cardiomyopathy and endocardial fibroelastosis. J. Am. Coll. Cardiol. 2010, 56, 1493-1502.
    • (2010) J. Am. Coll. Cardiol. , vol.56 , pp. 1493-1502
    • Purevjav, E.1    Varela, J.2    Morgado, M.3    Kearney, D.L.4
  • 26
    • 77957976010 scopus 로고    scopus 로고
    • Nebulette mutations in cardiac remodeling: big effects from a small mechanosensor
    • Ram, R., Blaxall, B. C., Nebulette mutations in cardiac remodeling: big effects from a small mechanosensor. J. Am. Coll. Cardiol. 2010, 56, 1503-1505.
    • (2010) J. Am. Coll. Cardiol. , vol.56 , pp. 1503-1505
    • Ram, R.1    Blaxall, B.C.2
  • 27
    • 33845793833 scopus 로고    scopus 로고
    • Linker region of nebulin family members plays an important role in targeting these molecules to cellular structures
    • Moncman, C. L., Panaviene, Z., 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
    • Moncman, C.L.1    Panaviene, Z.2
  • 28
    • 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., Chen, X., Parente, J. A., Tarrer, 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    Chen, X.2    Parente, J.A.3    Tarrer, S.4
  • 29
    • 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., 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.2
  • 31
    • 33751359975 scopus 로고    scopus 로고
    • Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes
    • Holaska, J. M., Rais-Bahrami, S., Wilson, K. L., Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes. Human Mol. Genetics 2006, 15, 3459-3472.
    • (2006) Human Mol. Genetics , vol.15 , pp. 3459-3472
    • Holaska, J.M.1    Rais-Bahrami, S.2    Wilson, K.L.3
  • 33
    • 0038683341 scopus 로고    scopus 로고
    • An engineered 800 kilobase deletion of Uchl3 and Lmo7 on mouse chromosome 14 causes defects in viability, postnatal growth and degeneration of muscle and retina
    • Semenova, E., Wang, X., Jablonski, M. M., Levorse, J., Tilghman, S. M., An engineered 800 kilobase deletion of Uchl3 and Lmo7 on mouse chromosome 14 causes defects in viability, postnatal growth and degeneration of muscle and retina. Human Mol. Genetics 2003, 12, 1301-1312.
    • (2003) Human Mol. Genetics , vol.12 , pp. 1301-1312
    • Semenova, E.1    Wang, X.2    Jablonski, M.M.3    Levorse, J.4    Tilghman, S.M.5
  • 34
    • 33645729418 scopus 로고    scopus 로고
    • Notch1b and neuregulin are required for specification of central cardiac conduction tissue
    • Milan, D. J., Giokas, A. C., Serluca, F. C., Peterson, R. T., MacRae, C. A., Notch1b and neuregulin are required for specification of central cardiac conduction tissue. Development 2006, 133, 1125-1132.
    • (2006) Development , vol.133 , pp. 1125-1132
    • Milan, D.J.1    Giokas, A.C.2    Serluca, F.C.3    Peterson, R.T.4    MacRae, C.A.5
  • 35
    • 48049085684 scopus 로고    scopus 로고
    • Emerin and the nuclear lamina in muscle and cardiac disease
    • Holaska, J. M., Emerin and the nuclear lamina in muscle and cardiac disease. Circ. Res. 2008, 103, 16-23.
    • (2008) Circ. Res. , vol.103 , pp. 16-23
    • Holaska, J.M.1
  • 36
    • 0033555309 scopus 로고    scopus 로고
    • Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1)
    • Kotaka, M., Ngai, S.-M., Garcia-Barcelo, M., Tsui, S. K. W. et al., Characterization of the human 36-kDa carboxyl terminal LIM domain protein (hCLIM1). J. Cell. Biochem. 1999, 72, 279-285.
    • (1999) J. Cell. Biochem. , vol.72 , pp. 279-285
    • Kotaka, M.1    Ngai, S.-M.2    Garcia-Barcelo, M.3    Tsui, S.K.W.4
  • 37
    • 0033897296 scopus 로고    scopus 로고
    • Interaction of hCLIM1, an Enigma family protein, with α-actinin 2
    • Kotaka, M., Kostin, S., Ngai, S.-M., Chan, K.-K. et al., Interaction of hCLIM1, an Enigma family protein, with α-actinin 2. J. Cell. Biochem. 2000, 78, 558-565.
    • (2000) J. Cell. Biochem. , vol.78 , pp. 558-565
    • Kotaka, M.1    Kostin, S.2    Ngai, S.-M.3    Chan, K.-K.4
  • 38
  • 39
    • 0028073676 scopus 로고
    • Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation
    • Arber, S., Halder, G., Caroni, P., Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation. Cell 1994, 79, 221-231.
    • (1994) Cell , vol.79 , pp. 221-231
    • Arber, S.1    Halder, G.2    Caroni, P.3
  • 40
    • 0002764856 scopus 로고    scopus 로고
    • A possible role for novel LIM domain proteins in dilated cardiomyopathy
    • Zimmermann, R., Kostin, S., Kotaka, M., Waye, M. M. et al., A possible role for novel LIM domain proteins in dilated cardiomyopathy. Circulation 1999, 100, 565-565.
    • (1999) Circulation , vol.100 , pp. 565-565
    • Zimmermann, R.1    Kostin, S.2    Kotaka, M.3    Waye, M.M.4
  • 41
    • 0035033212 scopus 로고    scopus 로고
    • Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy
    • Pashmforoush, M., Pomies, P., Peterson, K. L., Kubalak, S. et al., Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy. Nat. Med. 2001, 7, 591-597.
    • (2001) Nat. Med. , vol.7 , pp. 591-597
    • Pashmforoush, M.1    Pomies, P.2    Peterson, K.L.3    Kubalak, S.4
  • 42
    • 33947593150 scopus 로고    scopus 로고
    • Mutations in PDLIM3 and MYOZ1 encoding myocyte Z line proteins are infrequently found in idiopathic dilated cardiomyopathy
    • Arola, A. M., Sanchez, X., Murphy, R. T., Hasle, E. et al., Mutations in PDLIM3 and MYOZ1 encoding myocyte Z line proteins are infrequently found in idiopathic dilated cardiomyopathy. Mol. Genet. Metab. 2007, 90, 435-440.
    • (2007) Mol. Genet. Metab. , vol.90 , pp. 435-440
    • Arola, A.M.1    Sanchez, X.2    Murphy, R.T.3    Hasle, E.4
  • 43
    • 78649909959 scopus 로고    scopus 로고
    • Analysis of the Z-disc genes PDLIM3 and MYPN in patients with hypertrophic cardiomyopathy
    • Bagnall, R. D., Yeates, L., Semsarian, C., Analysis of the Z-disc genes PDLIM3 and MYPN in patients with hypertrophic cardiomyopathy. Int. J. Cardiol. 2010, 145, 601-602.
    • (2010) Int. J. Cardiol. , vol.145 , pp. 601-602
    • Bagnall, R.D.1    Yeates, L.2    Semsarian, C.3
  • 44
    • 33749361499 scopus 로고    scopus 로고
    • Gene regulatory networks in the evolution and development of the heart
    • Olson, E. N., Gene regulatory networks in the evolution and development of the heart. Science 2006, 313, 1922-1927.
    • (2006) Science , vol.313 , pp. 1922-1927
    • Olson, E.N.1
  • 45
    • 0346783332 scopus 로고    scopus 로고
    • Isl1 identifies a cardiac progenitor population that proliferates prior to differentiation and contributes a majority of cells to the heart
    • Cai, C. L., Liang, X., Shi, Y., Chu, P. H. et al., Isl1 identifies a cardiac progenitor population that proliferates prior to differentiation and contributes a majority of cells to the heart. Dev. Cell 2003, 5, 877-889.
    • (2003) Dev. Cell , vol.5 , pp. 877-889
    • Cai, C.L.1    Liang, X.2    Shi, Y.3    Chu, P.H.4
  • 46
    • 4544236360 scopus 로고    scopus 로고
    • Mef2c is a direct transcriptional target of ISL1 and GATA factors in the anterior heart field during mouse embryonic development
    • Dodou, E., Verzi, M. P., Anderson, J. P., Xu, S.-M., Black, B. L., Mef2c is a direct transcriptional target of ISL1 and GATA factors in the anterior heart field during mouse embryonic development. Development 2004, 131, 3931-3942.
    • (2004) Development , vol.131 , pp. 3931-3942
    • Dodou, E.1    Verzi, M.P.2    Anderson, J.P.3    Xu, S.-M.4    Black, B.L.5
  • 47
    • 67650071028 scopus 로고    scopus 로고
    • Human ISL1 heart progenitors generate diverse multipotent cardiovascular cell lineages
    • Bu, L., Jiang, X., Martin-Puig, S., Caron, L. et al., Human ISL1 heart progenitors generate diverse multipotent cardiovascular cell lineages. Nature 2009, 460, 113-117.
    • (2009) Nature , vol.460 , pp. 113-117
    • Bu, L.1    Jiang, X.2    Martin-Puig, S.3    Caron, L.4
  • 48
    • 13544272476 scopus 로고    scopus 로고
    • Postnatal isl1+cardioblasts enter fully differentiated cardiomyocyte lineages
    • Laugwitz, K.-L., Moretti, A., Lam, J., Gruber, P. et al., Postnatal isl1+cardioblasts enter fully differentiated cardiomyocyte lineages. Nature 2005, 433, 647-653.
    • (2005) Nature , vol.433 , pp. 647-653
    • Laugwitz, K.-L.1    Moretti, A.2    Lam, J.3    Gruber, P.4
  • 49
    • 33947519989 scopus 로고    scopus 로고
    • Cardiovascular development: towards biomedical applicability
    • Moretti, A., Lam, J., Evans, S., Laugwitz, K., Cardiovascular development: towards biomedical applicability. Cell. Mol. Life Sci. 2007, 64, 674-682.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 674-682
    • Moretti, A.1    Lam, J.2    Evans, S.3    Laugwitz, K.4
  • 50
    • 74249116579 scopus 로고    scopus 로고
    • A potential role for islet-1 in post-natal angiogenesis and vasculogenesis
    • Barzelay, A., Ben-Shoshan, J., Entin-Meer, M., Maysel-Auslender, S. et al., A potential role for islet-1 in post-natal angiogenesis and vasculogenesis. Thromb. Haemost. 2010, 103, 188-197.
    • (2010) Thromb. Haemost. , vol.103 , pp. 188-197
    • Barzelay, A.1    Ben-Shoshan, J.2    Entin-Meer, M.3    Maysel-Auslender, S.4
  • 52
    • 79957850422 scopus 로고    scopus 로고
    • Distinction between two populations of islet-1-positive cells in hearts of different murine strains
    • Khattar, P., Friedrich, F. W., Bonne, G., Carrier, L. et al., Distinction between two populations of islet-1-positive cells in hearts of different murine strains. Stem Cells Dev. 2011, 20, 1043-1052.
    • (2011) Stem Cells Dev. , vol.20 , pp. 1043-1052
    • Khattar, P.1    Friedrich, F.W.2    Bonne, G.3    Carrier, L.4
  • 54
    • 0032080146 scopus 로고    scopus 로고
    • LIM domains of cysteine-rich protein 1 (CRP1) are essential for its zyxin-binding function
    • Beckerle, M. C., Schmeichel, K. L., LIM domains of cysteine-rich protein 1 (CRP1) are essential for its zyxin-binding function. Biochem. J. 1998, 331, 885-892.
    • (1998) Biochem. J. , vol.331 , pp. 885-892
    • Beckerle, M.C.1    Schmeichel, K.L.2
  • 55
    • 28844455092 scopus 로고    scopus 로고
    • Cysteine-rich protein 1 (CRP1) regulates actin filament bundling
    • Tran, T. C., Singleton, C., Fraley, T. S., Greenwood, J. A., Cysteine-rich protein 1 (CRP1) regulates actin filament bundling. BMC Cell Biol 2005, 6, 45.
    • (2005) BMC Cell Biol , vol.6 , pp. 45
    • Tran, T.C.1    Singleton, C.2    Fraley, T.S.3    Greenwood, J.A.4
  • 56
    • 34547426803 scopus 로고    scopus 로고
    • Csrp1 regulates dynamic cell movements of the mesendoderm and cardiac mesoderm through interactions with Dishevelled and Diversin
    • Ogura, T., Miyasaka, K. Y., Kida, Y. S., Sato, T., Minarni, M., Csrp1 regulates dynamic cell movements of the mesendoderm and cardiac mesoderm through interactions with Dishevelled and Diversin. Proc. Natl. Acad. Sci. USA 2007, 104, 11274-11279.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 11274-11279
    • Ogura, T.1    Miyasaka, K.Y.2    Kida, Y.S.3    Sato, T.4    Minarni, M.5
  • 57
    • 0037242185 scopus 로고    scopus 로고
    • Cysteine-rich LIM-only proteins CRP1 and CRP2 are potent smooth muscle differentiation cofactors
    • Chang, D. F., Belaguli, N. S., Iyer, D., Roberts, W. B. et al., Cysteine-rich LIM-only proteins CRP1 and CRP2 are potent smooth muscle differentiation cofactors. Dev. Cell 2003, 4, 107-118.
    • (2003) Dev. Cell , vol.4 , pp. 107-118
    • Chang, D.F.1    Belaguli, N.S.2    Iyer, D.3    Roberts, W.B.4
  • 58
    • 0028811671 scopus 로고
    • The cysteine-rich protein family of highly related LIM domain proteins
    • Weiskirchen, R., Pino, J. D., Macalma, T., Bister, K., Beckerle, M. C., The cysteine-rich protein family of highly related LIM domain proteins. J. Biol. Chem. 1995, 270, 28946-28954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28946-28954
    • Weiskirchen, R.1    Pino, J.D.2    Macalma, T.3    Bister, K.4    Beckerle, M.C.5
  • 59
    • 51249117801 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Csrp2 gene encoding the cysteine- and glycine-rich LIM domain protein CRP2 result in subtle alteration of cardiac ultrastructure
    • Sagave, J., Moser, M., Ehler, E., Weiskirchen, S. et al., Targeted disruption of the mouse Csrp2 gene encoding the cysteine- and glycine-rich LIM domain protein CRP2 result in subtle alteration of cardiac ultrastructure. BMC Dev. Biol. 2008, 8, 80.
    • (2008) BMC Dev. Biol. , vol.8 , pp. 80
    • Sagave, J.1    Moser, M.2    Ehler, E.3    Weiskirchen, S.4
  • 61
    • 15844405223 scopus 로고    scopus 로고
    • Molecular cloning and characterization of SmLIM, a developmentally regulated LIM protein preferentially expressed in aortic smooth muscle cells
    • Jain, M. K., Fujita, K. P., Hsieh, C.-M., Endege, W. O. et al., Molecular cloning and characterization of SmLIM, a developmentally regulated LIM protein preferentially expressed in aortic smooth muscle cells. J. Biol. Chem. 1996, 271, 10194-10199.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10194-10199
    • Jain, M.K.1    Fujita, K.P.2    Hsieh, C.-M.3    Endege, W.O.4
  • 62
    • 0032538947 scopus 로고    scopus 로고
    • Embryonic expression suggests an important role for CRP2/SmLIM in the developing cardiovascular system
    • Jain, M. K., Kashiki, S., Hsieh, C.-M., Layne, M. D. et al., Embryonic expression suggests an important role for CRP2/SmLIM in the developing cardiovascular system. Circ. Res. 1998, 83, 980-985.
    • (1998) Circ. Res. , vol.83 , pp. 980-985
    • Jain, M.K.1    Kashiki, S.2    Hsieh, C.-M.3    Layne, M.D.4
  • 63
    • 80052183371 scopus 로고    scopus 로고
    • Expression of Crip2, a LIM-domain-only protein, in the mouse cardiovascular system under physiological and pathological conditions
    • Wei, T.-C., Lin, H.-Y., Lu, C.-C., Chen, C.-M., You, L.-R., Expression of Crip2, a LIM-domain-only protein, in the mouse cardiovascular system under physiological and pathological conditions. Gene Expr. Patterns. 2011, 11, 384-394.
    • (2011) Gene Expr. Patterns , vol.11 , pp. 384-394
    • Wei, T.-C.1    Lin, H.-Y.2    Lu, C.-C.3    Chen, C.-M.4    You, L.-R.5
  • 65
    • 40749088154 scopus 로고    scopus 로고
    • hhLIM is a novel F-actin binding protein involved in actin cytoskeleton remodeling
    • Zheng, B., Wen, J.-K., Han, M., hhLIM is a novel F-actin binding protein involved in actin cytoskeleton remodeling. FEBS J. 2008, 275, 1568-1578.
    • (2008) FEBS J. , vol.275 , pp. 1568-1578
    • Zheng, B.1    Wen, J.-K.2    Han, M.3
  • 66
    • 41749123888 scopus 로고    scopus 로고
    • Human heart LIM protein has transcription activation ability related to LIM domain 1
    • Zheng, B., Han, M., Wen, J.-K., Human heart LIM protein has transcription activation ability related to LIM domain 1. Biochemistry (Moscow) 2008, 73, 353-357.
    • (2008) Biochemistry (Moscow) , vol.73 , pp. 353-357
    • Zheng, B.1    Han, M.2    Wen, J.-K.3
  • 67
    • 38949151033 scopus 로고    scopus 로고
    • Human heart LIM protein activates atrial-natriuretic-factor gene expression by interacting with the cardiac-restricted transcription factor Nkx2. 5
    • Zheng, B., Han, M., Wen, J.-K., Zhang, R., Human heart LIM protein activates atrial-natriuretic-factor gene expression by interacting with the cardiac-restricted transcription factor Nkx2. 5. Biochem. J. 2008, 409, 683-690.
    • (2008) Biochem. J. , vol.409 , pp. 683-690
    • Zheng, B.1    Han, M.2    Wen, J.-K.3    Zhang, R.4
  • 68
    • 33646168238 scopus 로고    scopus 로고
    • hhLIM is involved in cardiomyogenesis of embryonic stem cells
    • Zheng, B., Wen, J.-K., Han, M., hhLIM is involved in cardiomyogenesis of embryonic stem cells. Biochemistry (Moscow) 2006, 71, S71-S76.
    • (2006) Biochemistry (Moscow) , vol.71
    • Zheng, B.1    Wen, J.-K.2    Han, M.3
  • 69
    • 0035996981 scopus 로고    scopus 로고
    • The heart LIM protein gene (Hlp), expressed in the developing and adult heart, defines a new tissue-specific LIM-only protein family
    • Yu, T.-S., Moctezuma-Anaya, M., Kubo, A., Keller, G., Robertson, S., The heart LIM protein gene (Hlp), expressed in the developing and adult heart, defines a new tissue-specific LIM-only protein family. Mech. Dev. 2002, 116, 187-192.
    • (2002) Mech. Dev. , vol.116 , pp. 187-192
    • Yu, T.-S.1    Moctezuma-Anaya, M.2    Kubo, A.3    Keller, G.4    Robertson, S.5
  • 70
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Caroni, P., Arber, S., Barbayannis, F. A., Hanser, H. et al., Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 1998, 393, 805-809.
    • (1998) Nature , vol.393 , pp. 805-809
    • Caroni, P.1    Arber, S.2    Barbayannis, F.A.3    Hanser, H.4
  • 71
    • 79953056392 scopus 로고    scopus 로고
    • Tissue specific characterisation of Lim-kinase 1 expression during mouse embryogenesis
    • Lindstrom, N. O. L. N. O., Neves, C., McIntosh, R., Miedzybrodzka, Z. et al., Tissue specific characterisation of Lim-kinase 1 expression during mouse embryogenesis. Gene Expr. Patterns 2011, 11, 221-232.
    • (2011) Gene Expr. Patterns , vol.11 , pp. 221-232
    • Lindstrom, N.1    Neves, C.2    McIntosh, R.3    Miedzybrodzka, Z.4
  • 72
    • 34249870137 scopus 로고    scopus 로고
    • Acute inhibition of Rho-kinase improves cardiac contractile function in streptozotocin-diabetic rats
    • Lin, G., Craig, G. P., Zhang, L., Yuen, V. G. et al., Acute inhibition of Rho-kinase improves cardiac contractile function in streptozotocin-diabetic rats. Cardiovasc. Res. 2007, 75, 51-58.
    • (2007) Cardiovasc. Res. , vol.75 , pp. 51-58
    • Lin, G.1    Craig, G.P.2    Zhang, L.3    Yuen, V.G.4
  • 74
    • 77956179490 scopus 로고    scopus 로고
    • Lmcd1/Dyxin, a novel Z-disc associated LIM protein, mediates cardiac hypertrophy in vitro and in vivo
    • Frank, D., Frauen, R., Hanselmann, C., Kuhn, C. et al., Lmcd1/Dyxin, a novel Z-disc associated LIM protein, mediates cardiac hypertrophy in vitro and in vivo. J. Mol. Cell. Cardiol. 2010, 49, 673-682.
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 673-682
    • Frank, D.1    Frauen, R.2    Hanselmann, C.3    Kuhn, C.4
  • 75
    • 74949112895 scopus 로고    scopus 로고
    • LIM and cysteine-rich domains 1 regulates cardiac hypertrophy by targeting calcineurin/nuclear factor of activated T cells signaling
    • Bian, Z.-Y., Huang, H., Jiang, H., Shen, D.-F. et al., LIM and cysteine-rich domains 1 regulates cardiac hypertrophy by targeting calcineurin/nuclear factor of activated T cells signaling. Hypertension 2010, 55, 257-263.
    • (2010) Hypertension , vol.55 , pp. 257-263
    • Bian, Z.-Y.1    Huang, H.2    Jiang, H.3    Shen, D.-F.4
  • 76
    • 0038390128 scopus 로고    scopus 로고
    • Roles of cardiac transcription factors in cardiac hypertrophy
    • Akazawa, H., Komuro, I., Roles of cardiac transcription factors in cardiac hypertrophy. Circ. Res. 2003, 92, 1079-1088.
    • (2003) Circ. Res. , vol.92 , pp. 1079-1088
    • Akazawa, H.1    Komuro, I.2
  • 77
    • 33847261472 scopus 로고    scopus 로고
    • Re-employment of developmental transcription factors in adult heart disease
    • Oka, T., Xu, J., Molkentin, J. D., Re-employment of developmental transcription factors in adult heart disease. Semin. Cell Dev. Biol. 2007, 18, 117-131.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 117-131
    • Oka, T.1    Xu, J.2    Molkentin, J.D.3
  • 78
    • 77649112626 scopus 로고    scopus 로고
    • A novel p38 MAPK target dyxin is rapidly induced by mechanical load in the heart
    • Luosujärvi, H., Aro, J., Tokola, H., Leskinen, H. et al., A novel p38 MAPK target dyxin is rapidly induced by mechanical load in the heart. Blood Pressure 2010, 19, 54-63.
    • (2010) Blood Pressure , vol.19 , pp. 54-63
    • Luosujärvi, H.1    Aro, J.2    Tokola, H.3    Leskinen, H.4
  • 79
    • 0034643946 scopus 로고    scopus 로고
    • Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure
    • Zolk, O., Caroni, P., Bohm, M., Decreased expression of the cardiac LIM domain protein MLP in chronic human heart failure. Circulation 2000, 101, 2674-2677.
    • (2000) Circulation , vol.101 , pp. 2674-2677
    • Zolk, O.1    Caroni, P.2    Bohm, M.3
  • 80
    • 69249246979 scopus 로고    scopus 로고
    • Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein
    • Boateng, S. Y., Senyo, S. E., Qi, L., Goldspink, P. H., Russell, B., Myocyte remodeling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein. J. Mol. Cell. Cardiol. 2009, 47, 426-435.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 426-435
    • Boateng, S.Y.1    Senyo, S.E.2    Qi, L.3    Goldspink, P.H.4    Russell, B.5
  • 81
    • 39349108340 scopus 로고    scopus 로고
    • Evaluation of 15 candidate genes for dilated cardiomyopathy in the newfoundland dog
    • Wiersma, A. C., Stabej, P., Leegwater, P. A. J., Van Oost, B. A. et al., Evaluation of 15 candidate genes for dilated cardiomyopathy in the newfoundland dog. J. Hered. 2008, 99, 73-80.
    • (2008) J. Hered. , vol.99 , pp. 73-80
    • Wiersma, A.C.1    Stabej, P.2    Leegwater, P.A.J.3    Van Oost, B.A.4
  • 82
    • 22244486626 scopus 로고    scopus 로고
    • Young MLP deficient mice show diastolic dysfunction before the onset of dilated cardiomyopathy
    • Lorenzen-Schmidt, I., Stuyvers, B. D., ter Keurs, H. E. D. J., Date, M.-O. et al., Young MLP deficient mice show diastolic dysfunction before the onset of dilated cardiomyopathy. J. Mol. Cell. Cardiol. 2005, 39, 241-250.
    • (2005) J. Mol. Cell. Cardiol. , vol.39 , pp. 241-250
    • Lorenzen-Schmidt, I.1    Stuyvers, B.D.2    ter Keurs, H.E.D.J.3    Date, M.-O.4
  • 83
    • 70349665019 scopus 로고    scopus 로고
    • Intercalated discs: multiple proteins perform multiple functions in non-failing and failing human hearts
    • Estigoy, C., Pontén, F., Odeberg, J., Herbert, B. et al., Intercalated discs: multiple proteins perform multiple functions in non-failing and failing human hearts. Biophys. Rev. 2009, 1, 43-49.
    • (2009) Biophys. Rev. , vol.1 , pp. 43-49
    • Estigoy, C.1    Pontén, F.2    Odeberg, J.3    Herbert, B.4
  • 84
    • 77951620985 scopus 로고    scopus 로고
    • Mechanical stress-induced sarcomere assembly for cardiac muscle growth in length and width
    • Russell, B., Curtis, M. W., Koshman, Y. E., Samarel, A. M., Mechanical stress-induced sarcomere assembly for cardiac muscle growth in length and width. J. Mol. Cell. Cardiol. 2010, 48, 817-823.
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 817-823
    • Russell, B.1    Curtis, M.W.2    Koshman, Y.E.3    Samarel, A.M.4
  • 85
    • 30944435503 scopus 로고    scopus 로고
    • Sarcomeric protein mutations in dilated cardiomyopathy
    • Chang, A., Potter, J., Sarcomeric protein mutations in dilated cardiomyopathy. Heart Failure Rev. 2005, 10, 225-235.
    • (2005) Heart Failure Rev. , vol.10 , pp. 225-235
    • Chang, A.1    Potter, J.2
  • 86
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • Knöll, R., Hoshijima, M., Hoffman, H. M., Person, V. et al., The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 2002, 111, 943-955.
    • (2002) Cell , vol.111 , pp. 943-955
    • Knöll, R.1    Hoshijima, M.2    Hoffman, H.M.3    Person, V.4
  • 87
    • 79958824015 scopus 로고    scopus 로고
    • MLP (muscle LIM protein) as a stress sensor in the heart
    • Buyandelger, B., Ng, K.-E., Miocic, S., Piotrowska, I. et al., MLP (muscle LIM protein) as a stress sensor in the heart. Pflug. Arch. 2011, 462, 135-142.
    • (2011) Pflug. Arch , vol.462 , pp. 135-142
    • Buyandelger, B.1    Ng, K.-E.2    Miocic, S.3    Piotrowska, I.4
  • 88
    • 77949379473 scopus 로고    scopus 로고
    • A common MLP (muscle LIM protein) variant is associated with cardiomyopathy
    • Knoll, R., Kostin, S., Klede, S., Savvatis, K. et al., A common MLP (muscle LIM protein) variant is associated with cardiomyopathy. Circ. Res. 2010, 106, 695-704.
    • (2010) Circ. Res. , vol.106 , pp. 695-704
    • Knoll, R.1    Kostin, S.2    Klede, S.3    Savvatis, K.4
  • 89
    • 0037453074 scopus 로고    scopus 로고
    • Mutations in the human muscle LIM protein gene in families with hypertrophic cardiomyopathy
    • Geier, C., Perrot, A., Özcelik, C., Binner, P. et al., Mutations in the human muscle LIM protein gene in families with hypertrophic cardiomyopathy. Circulation 2003, 107, 1390-1395.
    • (2003) Circulation , vol.107 , pp. 1390-1395
    • Geier, C.1    Perrot, A.2    Özcelik, C.3    Binner, P.4
  • 90
    • 50849138457 scopus 로고    scopus 로고
    • Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy
    • Geier, C., Gehmlich, K., Ehler, E., Hassfeld, S. et al., Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy. Human Mol. Genet. 2008, 17, 2753-2765.
    • (2008) Human Mol. Genet. , vol.17 , pp. 2753-2765
    • Geier, C.1    Gehmlich, K.2    Ehler, E.3    Hassfeld, S.4
  • 91
    • 4043152847 scopus 로고    scopus 로고
    • Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and α-actinin and their implication for hypertrophic cardiomyopathy
    • Gehmlich, K., Geier, C., Osterziel, K. J., Van der Ven, P. F. M., Fürst, D. O., Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and α-actinin and their implication for hypertrophic cardiomyopathy. Cell Tissue Res. 2004, 317, 129-136.
    • (2004) Cell Tissue Res. , vol.317 , pp. 129-136
    • Gehmlich, K.1    Geier, C.2    Osterziel, K.J.3    Van der Ven, P.F.M.4    Fürst, D.O.5
  • 92
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • Arber, S., Hunter, J. J., Ross, J., Jr., Hongo, M. et al., MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 1997, 88, 393-403.
    • (1997) Cell , vol.88 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross Jr, J.3    Hongo, M.4
  • 95
    • 74149086177 scopus 로고    scopus 로고
    • quot;MLP: a stress sensor goes nuclear" By Sylvia Gunkel, Jörg Heineke, Denise Hilfiker-Kleiner, Ralph Knöll, J. Mol. Cell. Cardiol. 2009, 47, 423-425. J. Mol. Cell. Cardiol.
    • Gehmlich, K., Ehler, E., Perrot, A., Fürst, D. O., Geier, C., "MLP: a stress sensor goes nuclear" By Sylvia Gunkel, Jörg Heineke, Denise Hilfiker-Kleiner, Ralph Knöll, J. Mol. Cell. Cardiol. 2009, 47, 423-425. J. Mol. Cell. Cardiol. 2010, 48, 424-425.
    • (2010) , vol.48 , pp. 424-425
    • Gehmlich, K.1    Ehler, E.2    Perrot, A.3    Fürst, D.O.4    Geier, C.5
  • 96
    • 79958838357 scopus 로고    scopus 로고
    • Conformation-regulated mechanosensory control via titin domains in cardiac muscle
    • Voelkel, T., Linke, W. A., Conformation-regulated mechanosensory control via titin domains in cardiac muscle. Pflug. Arch. 2011, 462, 143-154.
    • (2011) Pflug. Arch. , vol.462 , pp. 143-154
    • Voelkel, T.1    Linke, W.A.2
  • 97
    • 46749137221 scopus 로고    scopus 로고
    • GATA4/FOG2 transcriptional complex regulates Lhx9 gene expression in murine heart development
    • Smagulova, F., Manuylov, N., Leach, L., Tevosian, S., GATA4/FOG2 transcriptional complex regulates Lhx9 gene expression in murine heart development. BMC Dev. Biol. 2008, 8, 67.
    • (2008) BMC Dev. Biol. , vol.8 , pp. 67
    • Smagulova, F.1    Manuylov, N.2    Leach, L.3    Tevosian, S.4
  • 98
    • 0034602651 scopus 로고    scopus 로고
    • The oncogenic LIM-only transcription factor Lmo2 regulates angiogenesis but not vasculogenesis in mice
    • Yamada, Y., Pannell, R., Forster, A., Rabbitts, T. H., The oncogenic LIM-only transcription factor Lmo2 regulates angiogenesis but not vasculogenesis in mice. Proc. Natl. Acad. Sci. USA 2000, 97, 320-324.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 320-324
    • Yamada, Y.1    Pannell, R.2    Forster, A.3    Rabbitts, T.H.4
  • 99
    • 79551539901 scopus 로고    scopus 로고
    • Loss of migfilin expression has no overt consequences on murine development and homeostasis
    • Moik, D. V., Janbandhu, V. C., Fässler, R., Loss of migfilin expression has no overt consequences on murine development and homeostasis. J. Cell Sci. 2011, 124, 414-421.
    • (2011) J. Cell Sci. , vol.124 , pp. 414-421
    • Moik, D.V.1    Janbandhu, V.C.2    Fässler, R.3
  • 100
    • 41949127144 scopus 로고    scopus 로고
    • Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function
    • Dowling, J. J., Gibbs, E., Russell, M., Goldman, D. et al., Kindlin-2 is an essential component of intercalated discs and is required for vertebrate cardiac structure and function. Circ. Res. 2008, 102, 423-431.
    • (2008) Circ. Res. , vol.102 , pp. 423-431
    • Dowling, J.J.1    Gibbs, E.2    Russell, M.3    Goldman, D.4
  • 101
    • 41949101971 scopus 로고    scopus 로고
    • Disrupted intercalated discs
    • Hatcher, C. J., Basson, C. T., Disrupted intercalated discs. Circ. Res. 2008, 102, 392-394.
    • (2008) Circ. Res. , vol.102 , pp. 392-394
    • Hatcher, C.J.1    Basson, C.T.2
  • 102
    • 14944370105 scopus 로고    scopus 로고
    • Migfilin and its binding partners: from cell biology to human diseases
    • Wu, C., Migfilin and its binding partners: from cell biology to human diseases. J. Cell Sci. 2005, 118, 659-664.
    • (2005) J. Cell Sci. , vol.118 , pp. 659-664
    • Wu, C.1
  • 103
    • 0842288224 scopus 로고    scopus 로고
    • A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5
    • Akazawa, H., Kudoh, S., Mochizuki, N., Takekoshi, N. et al., A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5. J. Cell Biol. 2004, 164, 395-405.
    • (2004) J. Cell Biol. , vol.164 , pp. 395-405
    • Akazawa, H.1    Kudoh, S.2    Mochizuki, N.3    Takekoshi, N.4
  • 104
    • 33646529418 scopus 로고    scopus 로고
    • Integrin signalling: the tug-of-war in heart hypertrophy
    • Brancaccio, M., Hirsch, E., Notte, A., Selvetella, G. et al., Integrin signalling: the tug-of-war in heart hypertrophy. Cardiovasc. Res. 2006, 70, 422-433.
    • (2006) Cardiovasc. Res. , vol.70 , pp. 422-433
    • Brancaccio, M.1    Hirsch, E.2    Notte, A.3    Selvetella, G.4
  • 105
    • 0032479573 scopus 로고    scopus 로고
    • Congenital heart disease caused by mutations in the transcription factor NKX2-5
    • Schott, J.-J., Benson, D. W., Basson, C. T., Pease, W. et al., Congenital heart disease caused by mutations in the transcription factor NKX2-5. Science 1998, 281, 108-111.
    • (1998) Science , vol.281 , pp. 108-111
    • Schott, J.-J.1    Benson, D.W.2    Basson, C.T.3    Pease, W.4
  • 106
    • 0031861927 scopus 로고    scopus 로고
    • Upregulation of the cardiac homeobox gene Nkx2-5 (CSX) in feline right ventricular pressure overload
    • Thompson, J. T., Rackley, M. S., O'Brien, T. X., Upregulation of the cardiac homeobox gene Nkx2-5 (CSX) in feline right ventricular pressure overload. Am. J. Physiol. - Heart Circ. Physiol. 1998, 274, H1569-H1573.
    • (1998) Am. J. Physiol. - Heart Circ. Physiol. , vol.274
    • Thompson, J.T.1    Rackley, M.S.2    O'Brien, T.X.3
  • 107
    • 77952395282 scopus 로고    scopus 로고
    • Splice variants of Enigma homolog, differentially expressed during heart development, promote or prevent hypertrophy
    • Yamazaki, T., Wälchli, S., Fujita, T., Ryser, S. et al., Splice variants of Enigma homolog, differentially expressed during heart development, promote or prevent hypertrophy. Cardiovasc. Res. 2010, 86, 374-382.
    • (2010) Cardiovasc. Res. , vol.86 , pp. 374-382
    • Yamazaki, T.1    Wälchli, S.2    Fujita, T.3    Ryser, S.4
  • 108
    • 77956634211 scopus 로고    scopus 로고
    • Unraveling Enigma in the Z-disks
    • Wang, X., Su, H., Unraveling Enigma in the Z-disks. Circ. Res. 2010, 107, 321-323.
    • (2010) Circ. Res. , vol.107 , pp. 321-323
    • Wang, X.1    Su, H.2
  • 109
    • 79951850381 scopus 로고    scopus 로고
    • LIM domains regulate protein kinase C activity: A novel molecular function
    • Maturana, A. D., Nakagawa, N., Yoshimoto, N., Tatematsu, K. et al., LIM domains regulate protein kinase C activity: A novel molecular function. Cell. Signal. 2011, 23, 928-934.
    • (2011) Cell. Signal. , vol.23 , pp. 928-934
    • Maturana, A.D.1    Nakagawa, N.2    Yoshimoto, N.3    Tatematsu, K.4
  • 110
    • 33646081053 scopus 로고    scopus 로고
    • Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures
    • Hoshijima, M., Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures. Am. J. Physiol. - Heart Circ. Physiol. 2006, 290, H1313-H1325.
    • (2006) Am. J. Physiol. - Heart Circ. Physiol. , vol.290
    • Hoshijima, M.1
  • 111
    • 44449137885 scopus 로고    scopus 로고
    • Enigma homolog 1 scaffolds protein kinase D1 to regulate the activity of the cardiac L-type voltage-gated calcium channel
    • Maturana, A. D., Walchli, S., Iwata, M., Ryser, S. et al., Enigma homolog 1 scaffolds protein kinase D1 to regulate the activity of the cardiac L-type voltage-gated calcium channel. Cardiovasc. Res. 2008, 78, 458-465.
    • (2008) Cardiovasc. Res. , vol.78 , pp. 458-465
    • Maturana, A.D.1    Walchli, S.2    Iwata, M.3    Ryser, S.4
  • 112
    • 77956645736 scopus 로고    scopus 로고
    • Loss of Enigma homolog protein results in dilated cardiomyopathy/novelty and significance
    • Cheng, H., Kimura, K., Peter, A. K., Cui, L. et al., Loss of Enigma homolog protein results in dilated cardiomyopathy/novelty and significance. Circ. Res. 2010, 107, 348-356.
    • (2010) Circ. Res. , vol.107 , pp. 348-356
    • Cheng, H.1    Kimura, K.2    Peter, A.K.3    Cui, L.4
  • 113
    • 33846232336 scopus 로고    scopus 로고
    • Differential regulation of Tbx5 protein expression and sub-cellular localization during heart development
    • Bimber, B., Dettman, R. W., Simon, H.-G., Differential regulation of Tbx5 protein expression and sub-cellular localization during heart development. Dev. Biol. 2007, 302, 230-242.
    • (2007) Dev. Biol. , vol.302 , pp. 230-242
    • Bimber, B.1    Dettman, R.W.2    Simon, H.-G.3
  • 114
    • 72649083705 scopus 로고    scopus 로고
    • Pdlim7 (LMP4) regulation of Tbx5 specifies zebrafish heart atrio-ventricular boundary and valve formation
    • Camarata, T., Krcmery, J., Snyder, D., Park, S. et al., Pdlim7 (LMP4) regulation of Tbx5 specifies zebrafish heart atrio-ventricular boundary and valve formation. Dev. Biol. 2010, 337, 233-245.
    • (2010) Dev. Biol. , vol.337 , pp. 233-245
    • Camarata, T.1    Krcmery, J.2    Snyder, D.3    Park, S.4
  • 115
    • 0345491828 scopus 로고    scopus 로고
    • REST/NRSF-interacting LIM domain protein, a putative nuclear translocation receptor
    • Shimojo, M., Hersh, L. B., REST/NRSF-interacting LIM domain protein, a putative nuclear translocation receptor. Mol. Cell. Biol. 2003, 23, 9025-9031.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 9025-9031
    • Shimojo, M.1    Hersh, L.B.2
  • 116
    • 33646366606 scopus 로고    scopus 로고
    • Refinement and prediction of protein prenylation motifs
    • Maurer-Stroh, S., Eisenhaber, F., Refinement and prediction of protein prenylation motifs. Genome Biol. 2005, 6, R55.
    • (2005) Genome Biol. , vol.6
    • Maurer-Stroh, S.1    Eisenhaber, F.2
  • 117
    • 33645106218 scopus 로고    scopus 로고
    • Characterization of the REST/NRSF-interacting LIM domain protein (RILP): localization and interaction with REST/NRSF
    • Shimojo, M., Hersh, L. B., Characterization of the REST/NRSF-interacting LIM domain protein (RILP): localization and interaction with REST/NRSF. J. Neurochem. 2006, 96, 1130-1138.
    • (2006) J. Neurochem. , vol.96 , pp. 1130-1138
    • Shimojo, M.1    Hersh, L.B.2
  • 118
    • 0037901028 scopus 로고    scopus 로고
    • Minireview: Natriuretic peptides during development of the fetal heart and circulation
    • Cameron, V. A., Ellmers, L. J., Minireview: Natriuretic peptides during development of the fetal heart and circulation. Endocrinology 2003, 144, 2191-2194.
    • (2003) Endocrinology , vol.144 , pp. 2191-2194
    • Cameron, V.A.1    Ellmers, L.J.2
  • 119
    • 78650644716 scopus 로고    scopus 로고
    • RE1-silencing transcription factor (REST) and REST-interacting LIM domain protein (RILP) affect P19CL6 differentiation
    • Shimojo, M., RE1-silencing transcription factor (REST) and REST-interacting LIM domain protein (RILP) affect P19CL6 differentiation. Genes Cells 2011, 16, 90-100.
    • (2011) Genes Cells , vol.16 , pp. 90-100
    • Shimojo, M.1
  • 120
    • 0033606789 scopus 로고    scopus 로고
    • ZASP: a new Z-band alternatively spliced PDZ-motif protein
    • Faulkner, G., Pallavicini, A., Formentin, E., Comelli, A. et al., ZASP: a new Z-band alternatively spliced PDZ-motif protein. J. Cell Biol. 1999, 146, 465-475.
    • (1999) J. Cell Biol. , vol.146 , pp. 465-475
    • Faulkner, G.1    Pallavicini, A.2    Formentin, E.3    Comelli, A.4
  • 121
    • 33646069003 scopus 로고    scopus 로고
    • Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with [α]-actinin - analysis of patient mutations
    • Klaavuniemi, T., Ylänne, J., Zasp/Cypher internal ZM-motif containing fragments are sufficient to co-localize with [α]-actinin - analysis of patient mutations. Exp. Cell Res. 2006, 312, 1299-1311.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1299-1311
    • Klaavuniemi, T.1    Ylänne, J.2
  • 122
    • 84924110084 scopus 로고    scopus 로고
    • Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy
    • Zhou, Q., Chu, P.-H., Huang, C., Cheng, C.-F. et al., Ablation of Cypher, a PDZ-LIM domain Z-line protein, causes a severe form of congenital myopathy. J. Cell Biol. 2001, 155, 605-612.
    • (2001) J. Cell Biol. , vol.155 , pp. 605-612
    • Zhou, Q.1    Chu, P.-H.2    Huang, C.3    Cheng, C.-F.4
  • 123
    • 0344873698 scopus 로고    scopus 로고
    • Mutations in Cypher/ZASP in patients with dilated cardiomyopathy and left ventricular non-compaction
    • Vatta, M., Mohapatra, B., Jimenez, S., Sanchez, X. et al., Mutations in Cypher/ZASP in patients with dilated cardiomyopathy and left ventricular non-compaction. J. Am. Coll. Cardiol. 2003, 42, 2014-2027.
    • (2003) J. Am. Coll. Cardiol. , vol.42 , pp. 2014-2027
    • Vatta, M.1    Mohapatra, B.2    Jimenez, S.3    Sanchez, X.4
  • 124
    • 10744231114 scopus 로고    scopus 로고
    • A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the binding affinity to protein kinase C
    • Arimura, T., Hayashi, T., Terada, H., Lee, S.-Y. et al., A Cypher/ZASP mutation associated with dilated cardiomyopathy alters the binding affinity to protein kinase C. J. Biol. Chem. 2004, 279, 6746-6752.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6746-6752
    • Arimura, T.1    Hayashi, T.2    Terada, H.3    Lee, S.-Y.4
  • 125
    • 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
  • 126
    • 67650427412 scopus 로고    scopus 로고
    • Zyxin mediates actin fiber reorganization in epithelial-mesenchymal transition and contributes to endocardial morphogenesis
    • Mori, M., Nakagami, H., Koibuchi, N., Miura, K. et al., Zyxin mediates actin fiber reorganization in epithelial-mesenchymal transition and contributes to endocardial morphogenesis. Mol. Biol. Cell 2009, 20, 3115-3124.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3115-3124
    • Mori, M.1    Nakagami, H.2    Koibuchi, N.3    Miura, K.4
  • 127
    • 26444507242 scopus 로고    scopus 로고
    • Atrial natriuretic peptide promotes cardiomyocyte survival by cGMP-dependent nuclear accumulation of zyxin and Akt
    • Kato, T., Muraski, J., Chen, Y., Tsujita, Y. et al., Atrial natriuretic peptide promotes cardiomyocyte survival by cGMP-dependent nuclear accumulation of zyxin and Akt. J. Clin. Invest. 2005, 115, 2716-2730.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2716-2730
    • Kato, T.1    Muraski, J.2    Chen, Y.3    Tsujita, Y.4
  • 128
    • 1642542475 scopus 로고    scopus 로고
    • Focal adhesion protein Zyxin is a mechanosensitive modulator of gene expression in vascular smooth muscle cells
    • Cattaruzza, M., Lattrich, C., Hecker, M., Focal adhesion protein Zyxin is a mechanosensitive modulator of gene expression in vascular smooth muscle cells. Hypertension 2004, 43, 726-730.
    • (2004) Hypertension , vol.43 , pp. 726-730
    • Cattaruzza, M.1    Lattrich, C.2    Hecker, M.3
  • 129
    • 0030967789 scopus 로고    scopus 로고
    • Nuclear-cytoplasmic shuttling of the focal contact protein, Zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus
    • Nix, D. A., Beckerle, M. C., Nuclear-cytoplasmic shuttling of the focal contact protein, Zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. J. Cell Biol. 1997, 138, 1139-1147.
    • (1997) J. Cell Biol. , vol.138 , pp. 1139-1147
    • Nix, D.A.1    Beckerle, M.C.2
  • 130
    • 0037306002 scopus 로고    scopus 로고
    • Antihypertrophic actions of the natriuretic peptides in adult rat cardiomyocytes: Importance of cyclic GMP
    • Rosenkranz, A. C., Woods, R. L., Dusting, G. J., Ritchie, R. H., Antihypertrophic actions of the natriuretic peptides in adult rat cardiomyocytes: Importance of cyclic GMP. Cardiovasc. Res. 2003, 57, 515-522.
    • (2003) Cardiovasc. Res. , vol.57 , pp. 515-522
    • Rosenkranz, A.C.1    Woods, R.L.2    Dusting, G.J.3    Ritchie, R.H.4
  • 131
    • 0035938201 scopus 로고    scopus 로고
    • LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains
    • Wang, Y., Gilmore, T. D., LIM domain protein Trip6 has a conserved nuclear export signal, nuclear targeting sequences, and multiple transactivation domains. Biochim. Biophys. Acta 2001, 1538, 260-272.
    • (2001) Biochim. Biophys. Acta , vol.1538 , pp. 260-272
    • Wang, Y.1    Gilmore, T.D.2
  • 132
    • 0030872241 scopus 로고    scopus 로고
    • Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein
    • Roof, D. J., Hayes, A., Adamian, M., Chishti, A. H., Li, T., Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. J. Cell Biol. 1997, 138, 575-588.
    • (1997) J. Cell Biol. , vol.138 , pp. 575-588
    • Roof, D.J.1    Hayes, A.2    Adamian, M.3    Chishti, A.H.4    Li, T.5
  • 134
    • 34247210703 scopus 로고    scopus 로고
    • Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin
    • Barrientos, T., Frank, D., Kuwahara, K., Bezprozvannaya, S. et al., Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate with STARS and directly bind F-actin. J. Biol. Chem. 2007, 282, 8393-8403.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8393-8403
    • Barrientos, T.1    Frank, D.2    Kuwahara, K.3    Bezprozvannaya, S.4
  • 135
    • 65349161753 scopus 로고    scopus 로고
    • Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression
    • Zheng, B., Han, M., Bernier, M., Wen, J.-K., Nuclear actin and actin-binding proteins in the regulation of transcription and gene expression. FEBS J. 2009, 276, 2669-2685.
    • (2009) FEBS J. , vol.276 , pp. 2669-2685
    • Zheng, B.1    Han, M.2    Bernier, M.3    Wen, J.-K.4
  • 136
    • 0037178784 scopus 로고    scopus 로고
    • Exploring the neighborhood: adhesion-coupled cell mechanosensors
    • Geiger, B., Bershadsky, A., Exploring the neighborhood: adhesion-coupled cell mechanosensors. Cell 2002, 110, 139-142.
    • (2002) Cell , vol.110 , pp. 139-142
    • Geiger, B.1    Bershadsky, A.2
  • 137
    • 0037134779 scopus 로고    scopus 로고
    • MS1, a novel stress-responsive, muscle-specific gene that is up-regulated in the early stages of pressure overload-induced left ventricular hypertrophy
    • Mahadeva, H., Brooks, G., Lodwick, D., Chong, N. W., Samani, N. J., MS1, a novel stress-responsive, muscle-specific gene that is up-regulated in the early stages of pressure overload-induced left ventricular hypertrophy. FEBS Lett. 2002, 521, 100-104.
    • (2002) FEBS Lett. , vol.521 , pp. 100-104
    • Mahadeva, H.1    Brooks, G.2    Lodwick, D.3    Chong, N.W.4    Samani, N.J.5
  • 138
    • 34248164443 scopus 로고    scopus 로고
    • Paxillin and ponsin interact in nascent costameres of muscle cells
    • Gehmlich, K., Pinotsis, N., Hayeß, K., van der Ven, P. F. M. et al., Paxillin and ponsin interact in nascent costameres of muscle cells. J. Mol. Biol. 2007, 369, 665-682.
    • (2007) J. Mol. Biol. , vol.369 , pp. 665-682
    • Gehmlich, K.1    Pinotsis, N.2    Hayeß, K.3    van der Ven, P.F.M.4
  • 139
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel, M., George, E. L., Kim, A., Tamimi, R. et al., The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 2002, 22, 901-915.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4
  • 140
    • 11144234830 scopus 로고    scopus 로고
    • Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin
    • Melendez, J., Turner, C., Avraham, H., Steinberg, S. F. et al., Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin. J. Biol. Chem. 2004, 279, 53516-53523.
    • (2004) J. Biol. Chem. , vol.279 , pp. 53516-53523
    • Melendez, J.1    Turner, C.2    Avraham, H.3    Steinberg, S.F.4
  • 141
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown, M. C., Perrotta, J. A., Turner, C. E., Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 1996, 135, 1109-1123.
    • (1996) J. Cell Biol. , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 142
    • 0345701265 scopus 로고    scopus 로고
    • Expression of the LIM proteins paxillin and Hic-5 in human tissues
    • Yuminamochi, T., Yatomi, Y., Osada, M., Ohmori, T. et al., Expression of the LIM proteins paxillin and Hic-5 in human tissues. J. Histochem. Cytochem. 2003, 51, 513-521.
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 513-521
    • Yuminamochi, T.1    Yatomi, Y.2    Osada, M.3    Ohmori, T.4
  • 143
    • 69249216575 scopus 로고    scopus 로고
    • Hic-5 is required for fetal gene expression and cytoskeletal organization of neonatal cardiac myocytes
    • Yund, E. E., Hill, J. A., Keller, R. S., Hic-5 is required for fetal gene expression and cytoskeletal organization of neonatal cardiac myocytes. J. Mol. Cell. Cardiol. 2009, 47, 520-527.
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 520-527
    • Yund, E.E.1    Hill, J.A.2    Keller, R.S.3
  • 144
    • 79952736320 scopus 로고    scopus 로고
    • Four and a half LIM protein 1 gene mutations cause four distinct human myopathies: a comprehensive review of the clinical, histological and pathological features
    • Cowling, B. S., Cottle, D. L., Wilding, B. R., D'Arcy, C. E. et al., Four and a half LIM protein 1 gene mutations cause four distinct human myopathies: a comprehensive review of the clinical, histological and pathological features. Neuromusc. Disord. 2011, 21, 237-251.
    • (2011) Neuromusc. Disord. , vol.21 , pp. 237-251
    • Cowling, B.S.1    Cottle, D.L.2    Wilding, B.R.3    D'Arcy, C.E.4
  • 145
    • 44449118873 scopus 로고    scopus 로고
    • Four and a half LIM protein 1: a partner for KCNA5 in human atrium
    • Yang, Z., Browning, C. F., Hallaq, H., Yermalitskaya, L. et al., Four and a half LIM protein 1: a partner for KCNA5 in human atrium. Cardiovasc. Res. 2008, 78, 449-457.
    • (2008) Cardiovasc. Res. , vol.78 , pp. 449-457
    • Yang, Z.1    Browning, C.F.2    Hallaq, H.3    Yermalitskaya, L.4
  • 146
    • 44449178678 scopus 로고    scopus 로고
    • Four and a half LIM protein 1: A novel chaperone for atrium-specific Kv1. 5 channels with a potential role in atrial arrhythmogenesis
    • Dobrev, D., Wettwer, E., Four and a half LIM protein 1: A novel chaperone for atrium-specific Kv1. 5 channels with a potential role in atrial arrhythmogenesis. Cardiovasc. Res. 2008, 78, 411-412.
    • (2008) Cardiovasc. Res. , vol.78 , pp. 411-412
    • Dobrev, D.1    Wettwer, E.2
  • 147
    • 0033578613 scopus 로고    scopus 로고
    • Characterization of Two Isoforms of the Skeletal Muscle LIM Protein 1, SLIM1
    • Brown, S., McGrath, M. J., Ooms, L. M., Gurung, R. et al., Characterization of Two Isoforms of the Skeletal Muscle LIM Protein 1, SLIM1. J. Biol. Chem. 1999, 274, 27083-27091.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27083-27091
    • Brown, S.1    McGrath, M.J.2    Ooms, L.M.3    Gurung, R.4
  • 148
    • 0034004352 scopus 로고    scopus 로고
    • The LIM domain: Regulation by association
    • Bach, I., The LIM domain: Regulation by association. Mech. Dev. 2000, 91, 5-17.
    • (2000) Mech. Dev. , vol.91 , pp. 5-17
    • Bach, I.1
  • 149
    • 0034994307 scopus 로고    scopus 로고
    • Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1)
    • Ng, E. K. O., Lee, S. M. Y., Li, H.-Y., Ngai, S.-M. et al., Characterization of tissue-specific LIM domain protein (FHL1C) which is an alternatively spliced isoform of a human LIM-only protein (FHL1). J. Cell. Biochem. 2001, 82, 1-10.
    • (2001) J. Cell. Biochem. , vol.82 , pp. 1-10
    • Ng, E.K.O.1    Lee, S.M.Y.2    Li, H.-Y.3    Ngai, S.-M.4
  • 150
    • 0034234785 scopus 로고    scopus 로고
    • Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system
    • Chu, P.-H., Ruiz-Lozano, P., Zhou, Q., Cai, C., Chen, J., Expression patterns of FHL/SLIM family members suggest important functional roles in skeletal muscle and cardiovascular system. Mech. Dev. 2000, 95, 259-265.
    • (2000) Mech. Dev. , vol.95 , pp. 259-265
    • Chu, P.-H.1    Ruiz-Lozano, P.2    Zhou, Q.3    Cai, C.4    Chen, J.5
  • 151
    • 41549150673 scopus 로고    scopus 로고
    • Comparative proteomics profiling of a phospholamban mutant mouse model of dilated cardiomyopathy reveals progressive intracellular stress responses
    • Gramolini, A. O., Kislinger, T., Alikhani-Koopaei, R., Fong, V. et al., Comparative proteomics profiling of a phospholamban mutant mouse model of dilated cardiomyopathy reveals progressive intracellular stress responses. Mol. Cell Proteomics 2008, 7, 519-533.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 519-533
    • Gramolini, A.O.1    Kislinger, T.2    Alikhani-Koopaei, R.3    Fong, V.4
  • 152
    • 0034687593 scopus 로고    scopus 로고
    • Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays
    • Yang, J., Moravec, C. S., Sussman, M. A., DiPaola, N. R. et al., Decreased SLIM1 expression and increased gelsolin expression in failing human hearts measured by high-density oligonucleotide arrays. Circulation 2000, 102, 3046-3052.
    • (2000) Circulation , vol.102 , pp. 3046-3052
    • Yang, J.1    Moravec, C.S.2    Sussman, M.A.3    DiPaola, N.R.4
  • 153
    • 78650073322 scopus 로고    scopus 로고
    • Genes, proteins and complexes: the multifaceted nature of FHL family proteins in diverse tissues
    • Shathasivam, T., Kislinger, T., Gramolini, A. O., Genes, proteins and complexes: the multifaceted nature of FHL family proteins in diverse tissues. J. Cell Mol. Med. 2010, 14, 2702-2720.
    • (2010) J. Cell Mol. Med. , vol.14 , pp. 2702-2720
    • Shathasivam, T.1    Kislinger, T.2    Gramolini, A.O.3
  • 154
    • 77649302442 scopus 로고    scopus 로고
    • Contractures and hypertrophic cardiomyopathy in a novel FHL1 mutation
    • Knoblauch, H., Geier, C., Adams, S., Budde, B. et al., Contractures and hypertrophic cardiomyopathy in a novel FHL1 mutation. Ann. Neurol. 2010, 67, 136-140.
    • (2010) Ann. Neurol. , vol.67 , pp. 136-140
    • Knoblauch, H.1    Geier, C.2    Adams, S.3    Budde, B.4
  • 155
    • 0034801287 scopus 로고    scopus 로고
    • Expression profiling of cardiac genes in human hypertrophic cardiomyopathy: insight into the pathogenesis of phenotypes
    • Lim, D. S., Roberts, R., Marian, A. J., Expression profiling of cardiac genes in human hypertrophic cardiomyopathy: insight into the pathogenesis of phenotypes. J. Am. Coll. Cardiol. 2001, 38, 1175-1180.
    • (2001) J. Am. Coll. Cardiol. , vol.38 , pp. 1175-1180
    • Lim, D.S.1    Roberts, R.2    Marian, A.J.3
  • 156
    • 0345167075 scopus 로고    scopus 로고
    • Common genomic response in different mouse models of β-adrenergic-induced cardiomyopathy
    • Gaussin, V., Tomlinson, J. E., Depre, C., Engelhardt, S. et al., Common genomic response in different mouse models of β-adrenergic-induced cardiomyopathy. Circulation 2003, 108, 2926-2933.
    • (2003) Circulation , vol.108 , pp. 2926-2933
    • Gaussin, V.1    Tomlinson, J.E.2    Depre, C.3    Engelhardt, S.4
  • 157
    • 57449117141 scopus 로고    scopus 로고
    • An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice
    • Sheikh, F., Raskin, A., Chu, P.-H., Lange, S. et al., An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice. J. Clin. Invest. 2008, 118, 3870-3880.
    • (2008) J. Clin. Invest. , vol.118 , pp. 3870-3880
    • Sheikh, F.1    Raskin, A.2    Chu, P.-H.3    Lange, S.4
  • 158
    • 79651470741 scopus 로고    scopus 로고
    • Transgenic overexpression of USP15 in the heart induces cardiac remodeling in mice
    • Isumi, Y., Hirata, T., Saitoh, H., Miyakawa, T. et al., Transgenic overexpression of USP15 in the heart induces cardiac remodeling in mice. Biochem. Biophys. Res. Commun. 2011, 405, 216-221.
    • (2011) Biochem. Biophys. Res. Commun. , vol.405 , pp. 216-221
    • Isumi, Y.1    Hirata, T.2    Saitoh, H.3    Miyakawa, T.4
  • 159
    • 0032515886 scopus 로고    scopus 로고
    • Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart
    • Chan, K. K., Wing Tsui, S. K., Lee, S. M. Y., Luk, S. C. W. et al., Molecular cloning and characterization of FHL2, a novel LIM domain protein preferentially expressed in human heart. Gene 1998, 210, 345-350.
    • (1998) Gene , vol.210 , pp. 345-350
    • Chan, K.K.1    Wing Tsui, S.K.2    Lee, S.M.Y.3    Luk, S.C.W.4
  • 160
    • 33748361572 scopus 로고    scopus 로고
    • FHL2/SLIM3 decreases cardiomyocyte survival by inhibitory interaction with sphingosine kinase-1
    • Sun, J. X., Yan, G. J., Ren, A. X., You, B., Liao, J. K., FHL2/SLIM3 decreases cardiomyocyte survival by inhibitory interaction with sphingosine kinase-1. Circ. Res. 2006, 99, 468-476.
    • (2006) Circ. Res. , vol.99 , pp. 468-476
    • Sun, J.X.1    Yan, G.J.2    Ren, A.X.3    You, B.4    Liao, J.K.5
  • 161
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • Lange, S., Auerbach, D., McLoughlin, P., Perriard, E. et al., Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2. J. Cell Sci. 2002, 115, 4925-4936.
    • (2002) J. Cell Sci. , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    McLoughlin, P.3    Perriard, E.4
  • 162
    • 33745698393 scopus 로고    scopus 로고
    • Functional analysis of titin/connectin N2-B mutations found in cardiomyopathy
    • Kimura, A., Matsumoto, Y., Hayashi, T., Inagaki, N. et al., Functional analysis of titin/connectin N2-B mutations found in cardiomyopathy. J. Muscle Res. Cell Motil. 2005, 26, 367-374.
    • (2005) J. Muscle Res. Cell Motil. , vol.26 , pp. 367-374
    • Kimura, A.1    Matsumoto, Y.2    Hayashi, T.3    Inagaki, N.4
  • 163
    • 62849109969 scopus 로고    scopus 로고
    • Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes
    • Bovill, E., Westaby, S., Crisp, A., Jacobs, S., Shaw, T., Reduction of four-and-a-half LIM-protein 2 expression occurs in human left ventricular failure and leads to altered localization and reduced activity of metabolic enzymes. J. Thorac. Cardiovasc. Surg. 2009, 137, 853-861.
    • (2009) J. Thorac. Cardiovasc. Surg. , vol.137 , pp. 853-861
    • Bovill, E.1    Westaby, S.2    Crisp, A.3    Jacobs, S.4    Shaw, T.5
  • 164
    • 0033805096 scopus 로고    scopus 로고
    • FHL2 (SLIM3) is not essential for cardiac development and function
    • Chu, P.-H., Bardwell, W. M., Gu, Y., Ross J., Jr., Chen, J., FHL2 (SLIM3) is not essential for cardiac development and function. Mol. Cell. Biol. 2000, 20, 7460-7462.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7460-7462
    • Chu, P.-H.1    Bardwell, W.M.2    Gu, Y.3    Ross Jr, J.4    Chen, J.5
  • 165
    • 0035811023 scopus 로고    scopus 로고
    • Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation
    • Kong, Y., Shelton, J. M., Rothermel, B., Li, X. et al., Cardiac-specific LIM protein FHL2 modifies the hypertrophic response to beta-adrenergic stimulation. Circulation 2001, 103, 2731-2738.
    • (2001) Circulation , vol.103 , pp. 2731-2738
    • Kong, Y.1    Shelton, J.M.2    Rothermel, B.3    Li, X.4
  • 166
    • 0037083981 scopus 로고    scopus 로고
    • The transcriptional coactivator FHL2 transmits Rho signals from the cell membrane into the nucleus
    • Muller, J. M., Metzger, E., Greschik, H., Bosserhoff, A.-K. et al., The transcriptional coactivator FHL2 transmits Rho signals from the cell membrane into the nucleus. EMBO J. 2002, 21, 736-748.
    • (2002) EMBO J. , vol.21 , pp. 736-748
    • Muller, J.M.1    Metzger, E.2    Greschik, H.3    Bosserhoff, A.-K.4
  • 167
    • 1642458404 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes
    • Purcell, N. H., Darwis, D., Bueno, O. F., Muller, J. M. et al., Extracellular signal-regulated kinase 2 interacts with and is negatively regulated by the LIM-only protein FHL2 in cardiomyocytes. Mol. Cell. Biol. 2004, 24, 1081-1095.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1081-1095
    • Purcell, N.H.1    Darwis, D.2    Bueno, O.F.3    Muller, J.M.4
  • 169
    • 33645317063 scopus 로고    scopus 로고
    • hERG potassium channels and cardiac arrhythmia
    • Sanguinetti, M. C., Tristani-Firouzi, M., hERG potassium channels and cardiac arrhythmia. Nature 2006, 440, 463-469.
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 170
    • 50849133238 scopus 로고    scopus 로고
    • The four and a half LIM domain protein 2 interacts with and regulates the HERG channel
    • Lin, J., Lin, S., Yu, X., Choy, P. C. et al., The four and a half LIM domain protein 2 interacts with and regulates the HERG channel. FEBS J. 2008, 275, 4531-4539.
    • (2008) FEBS J. , vol.275 , pp. 4531-4539
    • Lin, J.1    Lin, S.2    Yu, X.3    Choy, P.C.4
  • 171
    • 79251486645 scopus 로고    scopus 로고
    • PINCH: more than just an adaptor protein in cellular response
    • Kovalevich, J., Tracy, B., Langford, D., PINCH: more than just an adaptor protein in cellular response. J. Cell. Physiol. 2011, 226, 940-947.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 940-947
    • Kovalevich, J.1    Tracy, B.2    Langford, D.3
  • 172
    • 74249119019 scopus 로고    scopus 로고
    • Particularly interesting cysteine- and histidine-rich protein in cardiac development and remodeling
    • 810.
    • Liang, X., Sun, Y., Chen, J., Particularly interesting cysteine- and histidine-rich protein in cardiac development and remodeling. J. Invest. Med. 2009, 57, 842-848. 810.
    • (2009) J. Invest. Med. , vol.57 , pp. 842-848
    • Liang, X.1    Sun, Y.2    Chen, J.3
  • 174
    • 65549125472 scopus 로고    scopus 로고
    • Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase
    • Yang, Y. W. X., Hawkins, C. A., Chen, K., Vaynberg, J. et al., Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase. J. Biol. Chem. 2008, 284, 5836-5844.
    • (2008) J. Biol. Chem. , vol.284 , pp. 5836-5844
    • Yang, Y.W.X.1    Hawkins, C.A.2    Chen, K.3    Vaynberg, J.4
  • 175
    • 84873063322 scopus 로고    scopus 로고
    • PINCH proteins regulate cardiac contractility by modulating ILK-PKB signaling
    • MCB, 05269-05211.
    • Meder, B., Huttner, I. G., Sedaghat-Hamedani, F., Just, S. et al., PINCH proteins regulate cardiac contractility by modulating ILK-PKB signaling. Mol. Cell. Biol. 2011, MCB. 05269-05211.
    • (2011) Mol. Cell. Biol.
    • Meder, B.1    Huttner, I.G.2    Sedaghat-Hamedani, F.3    Just, S.4
  • 176
    • 77950518387 scopus 로고    scopus 로고
    • Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase
    • Chiswell, B. P., Stiegler, A. L., Razinia, Z., Nalibotski, E. et al., Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. J. Struct. Biol. 2010, 170, 157-163.
    • (2010) J. Struct. Biol. , vol.170 , pp. 157-163
    • Chiswell, B.P.1    Stiegler, A.L.2    Razinia, Z.3    Nalibotski, E.4
  • 177
    • 79956286435 scopus 로고    scopus 로고
    • Significance of thymosin β4 and implication of PINCH-1-ILK-α-parvin (PIP) complex in human dilated cardiomyopathy
    • Sopko, N., Qin, Y., Finan, A., Dadabayev, A. et al., Significance of thymosin β4 and implication of PINCH-1-ILK-α-parvin (PIP) complex in human dilated cardiomyopathy. PLoS One 2011, 6, e20184.
    • (2011) PLoS One , vol.6
    • Sopko, N.1    Qin, Y.2    Finan, A.3    Dadabayev, A.4
  • 178
    • 69549097709 scopus 로고    scopus 로고
    • Targeted ablation of PINCH1 and PINCH2 from murine myocardium results in dilated cardiomyopathy and early postnatal lethality
    • Liang, X., Sun, Y., Ye, M., Scimia, M. C. et al., Targeted ablation of PINCH1 and PINCH2 from murine myocardium results in dilated cardiomyopathy and early postnatal lethality. Circulation 2009, 120, 568-576.
    • (2009) Circulation , vol.120 , pp. 568-576
    • Liang, X.1    Sun, Y.2    Ye, M.3    Scimia, M.C.4
  • 179
    • 0037327126 scopus 로고    scopus 로고
    • Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation
    • Mukhopadhyay, M., Teufel, A., Yamashita, T., Agulnick, A. D. et al., Functional ablation of the mouse Ldb1 gene results in severe patterning defects during gastrulation. Development 2003, 130, 495-505.
    • (2003) Development , vol.130 , pp. 495-505
    • Mukhopadhyay, M.1    Teufel, A.2    Yamashita, T.3    Agulnick, A.D.4
  • 180
    • 0347093483 scopus 로고    scopus 로고
    • LIM-domain-binding protein 1: a multifunctional cofactor that interacts with diverse proteins
    • Matthews, J. M., Visvader, J. E., LIM-domain-binding protein 1: a multifunctional cofactor that interacts with diverse proteins. EMBO Rep. 2003, 4, 1132-1137.
    • (2003) EMBO Rep. , vol.4 , pp. 1132-1137
    • Matthews, J.M.1    Visvader, J.E.2
  • 181
    • 0037034807 scopus 로고    scopus 로고
    • Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors
    • Ostendorff, H. P., Peirano, R. I., Peters, M. A., Schluter, A. et al., Ubiquitination-dependent cofactor exchange on LIM homeodomain transcription factors. Nature 2002, 416, 99-103.
    • (2002) Nature , vol.416 , pp. 99-103
    • Ostendorff, H.P.1    Peirano, R.I.2    Peters, M.A.3    Schluter, A.4
  • 182
    • 74249091032 scopus 로고    scopus 로고
    • Multi-organ expression profiling uncovers a gene module in coronary artery disease involving transendothelial migration of leukocytes and LIM domain binding 2: The Stockholm Atherosclerosis Gene Expression (STAGE) study
    • Hagg, S., Skogsberg, J., Lundstrom, J., Noori, P. et al., Multi-organ expression profiling uncovers a gene module in coronary artery disease involving transendothelial migration of leukocytes and LIM domain binding 2: The Stockholm Atherosclerosis Gene Expression (STAGE) study. PLoS Genet. 2009, 5, e1000754.
    • (2009) PLoS Genet. , vol.5
    • Hagg, S.1    Skogsberg, J.2    Lundstrom, J.3    Noori, P.4
  • 184
    • 22344450109 scopus 로고    scopus 로고
    • Deficiency of actinin-associated LIM protein alters regional right ventricular function and hypertrophic remodeling
    • Lorenzen-Schmidt, I., McCulloch, A. D., Omens, J. H., Deficiency of actinin-associated LIM protein alters regional right ventricular function and hypertrophic remodeling. Ann. Biomed. Eng. 2005, 33, 888-896.
    • (2005) Ann. Biomed. Eng. , vol.33 , pp. 888-896
    • Lorenzen-Schmidt, I.1    McCulloch, A.D.2    Omens, J.H.3
  • 185
    • 33947165217 scopus 로고    scopus 로고
    • Islet 1 is expressed in distinct cardiovascular lineages, including pacemaker and coronary vascular cells
    • Sun, Y., Liang, X., Najafi, N., Cass, M. et al., Islet 1 is expressed in distinct cardiovascular lineages, including pacemaker and coronary vascular cells. Dev. Biol. 2007, 304, 286-296.
    • (2007) Dev. Biol. , vol.304 , pp. 286-296
    • Sun, Y.1    Liang, X.2    Najafi, N.3    Cass, M.4
  • 186
    • 0033575252 scopus 로고    scopus 로고
    • ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E
    • Murthy, K. K. C. K., Fortin, Y., Shen, S. H., Banville, D., ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. J. Biol. Chem. 1999, 274, 20679-20687.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20679-20687
    • Murthy, K.K.C.K.1    Fortin, Y.2    Shen, S.H.3    Banville, D.4
  • 187
    • 79952650379 scopus 로고    scopus 로고
    • Identification of an FHL1 protein complex containing ACTN1, ACTN4, and PDLIM1 using affinity purifications and MS-based protein-protein interaction analysis
    • Sharma, P., Shathasivam, T., Ignatchenko, V., Kislinger, T., Gramolini, A. O., Identification of an FHL1 protein complex containing ACTN1, ACTN4, and PDLIM1 using affinity purifications and MS-based protein-protein interaction analysis. Mol. Biosyst. 2011, 7, 1185-1196.
    • (2011) Mol. Biosyst. , vol.7 , pp. 1185-1196
    • Sharma, P.1    Shathasivam, T.2    Ignatchenko, V.3    Kislinger, T.4    Gramolini, A.O.5
  • 188
    • 34147100523 scopus 로고    scopus 로고
    • Structural analysis of four and half LIM protein-2 in dilated cardiomyopathy
    • Arimura, T., Hayashi, T., Matsumoto, Y., Shibata, H. et al., Structural analysis of four and half LIM protein-2 in dilated cardiomyopathy. Biochem. Biophys. Res. Commun. 2007, 357, 162-167.
    • (2007) Biochem. Biophys. Res. Commun. , vol.357 , pp. 162-167
    • Arimura, T.1    Hayashi, T.2    Matsumoto, Y.3    Shibata, H.4
  • 189
    • 3042708179 scopus 로고    scopus 로고
    • The PINCH-ILK-parvin complexes: assembly, functions and regulation
    • Wu, C., The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim. Biophys. Acta 2004, 1692, 55-62.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 55-62
    • Wu, C.1
  • 190
    • 0037377167 scopus 로고    scopus 로고
    • PINCH2 is a new five LIM domain protein, homologous to PINCHand localized to focal adhesions[star, open]
    • Braun, A., Bordoy, R., Stanchi, F., Moser, M. et al., PINCH2 is a new five LIM domain protein, homologous to PINCHand localized to focal adhesions[star, open]. Exp. Cell Res. 2003, 284, 237-248.
    • (2003) Exp. Cell Res. , vol.284 , pp. 237-248
    • Braun, A.1    Bordoy, R.2    Stanchi, F.3    Moser, M.4
  • 191
    • 16244413957 scopus 로고    scopus 로고
    • PINCH2 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes
    • Liang, X., Zhou, Q., Li, X., Sun, Y. et al., PINCH2 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes. Mol. Cell. Biol. 2005, 25, 3056-3062.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3056-3062
    • Liang, X.1    Zhou, Q.2    Li, X.3    Sun, Y.4
  • 192
    • 80054026316 scopus 로고    scopus 로고
    • The Human Protein Atlas as a proteomic resource for biomarker discovery
    • Ponten, F., Schwenk, J. M., Asplund, A., Edqvist, P. H. D., The Human Protein Atlas as a proteomic resource for biomarker discovery. J. Intern. Med. 2011, 270, 428-446.
    • (2011) J. Intern. Med. , vol.270 , pp. 428-446
    • Ponten, F.1    Schwenk, J.M.2    Asplund, A.3    Edqvist, P.H.D.4
  • 193
    • 57149110826 scopus 로고    scopus 로고
    • The Human Protein Atlas - a tool for pathology
    • Ponten, F., Jirstrom, K., Uhlen, M., The Human Protein Atlas - a tool for pathology. J. Pathol. 2008, 216, 387-393.
    • (2008) J. Pathol. , vol.216 , pp. 387-393
    • Ponten, F.1    Jirstrom, K.2    Uhlen, M.3


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