메뉴 건너뛰기




Volumn 23, Issue 24, 2013, Pages

Nuclear mechanics and mechanotransduction in health and disease

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR MATRIX PROTEIN;

EID: 84890643605     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2013.11.009     Document Type: Review
Times cited : (287)

References (93)
  • 2
    • 79960277917 scopus 로고    scopus 로고
    • A hitchhiker's guide to mechanobiology
    • J. Eyckmans, T. Boudou, X. Yu, and C.S. Chen A hitchhiker's guide to mechanobiology Dev. Cell 21 2011 35 47
    • (2011) Dev. Cell , vol.21 , pp. 35-47
    • Eyckmans, J.1    Boudou, T.2    Yu, X.3    Chen, C.S.4
  • 3
    • 58049211966 scopus 로고    scopus 로고
    • Mechanotransduction at a distance: Mechanically coupling the extracellular matrix with the nucleus
    • N. Wang, J.D. Tytell, and D.E. Ingber Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus Nat. Rev. Mol. Cell Biol. 10 2009 75 82
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 75-82
    • Wang, N.1    Tytell, J.D.2    Ingber, D.E.3
  • 4
    • 84862882928 scopus 로고    scopus 로고
    • Lamins at a glance
    • C.Y. Ho, and J. Lammerding Lamins at a glance J. Cell Sci. 125 2012 2087 2093
    • (2012) J. Cell Sci. , vol.125 , pp. 2087-2093
    • Ho, C.Y.1    Lammerding, J.2
  • 5
    • 77953577950 scopus 로고    scopus 로고
    • The nuclear envelope at a glance
    • K.L. Wilson, and J.M. Berk The nuclear envelope at a glance J. Cell Sci. 123 2010 1973 1978
    • (2010) J. Cell Sci. , vol.123 , pp. 1973-1978
    • Wilson, K.L.1    Berk, J.M.2
  • 6
    • 41649097238 scopus 로고    scopus 로고
    • Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin
    • T. Dechat, K. Pfleghaar, K. Sengupta, T. Shimi, D.K. Shumaker, L. Solimando, and R.D. Goldman Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin Genes Dev. 22 2008 832 853
    • (2008) Genes Dev. , vol.22 , pp. 832-853
    • Dechat, T.1    Pfleghaar, K.2    Sengupta, K.3    Shimi, T.4    Shumaker, D.K.5    Solimando, L.6    Goldman, R.D.7
  • 7
    • 84875190221 scopus 로고    scopus 로고
    • Genome architecture: Domain organization of interphase chromosomes
    • W.A. Bickmore, and B. van Steensel Genome architecture: domain organization of interphase chromosomes Cell 152 2013 1270 1284
    • (2013) Cell , vol.152 , pp. 1270-1284
    • Bickmore, W.A.1    Van Steensel, B.2
  • 12
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • E.S. Folker, C. Ostlund, G.W. Luxton, H.J. Worman, and G.G. Gundersen Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement Proc. Natl. Acad. Sci. USA 108 2011 131 136
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 131-136
    • Folker, E.S.1    Ostlund, C.2    Luxton, G.W.3    Worman, H.J.4    Gundersen, G.G.5
  • 13
    • 79960234802 scopus 로고    scopus 로고
    • TAN lines: A novel nuclear envelope structure involved in nuclear positioning
    • G.G. Luxton, E.R. Gomes, E.S. Folker, H.J. Worman, and G.G. Gundersen TAN lines: a novel nuclear envelope structure involved in nuclear positioning Nucleus 2 2011 173 181
    • (2011) Nucleus , vol.2 , pp. 173-181
    • Luxton, G.G.1    Gomes, E.R.2    Folker, E.S.3    Worman, H.J.4    Gundersen, G.G.5
  • 14
    • 70849084351 scopus 로고    scopus 로고
    • Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins
    • C. Ostlund, E.S. Folker, J.C. Choi, E.R. Gomes, G.G. Gundersen, and H.J. Worman Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins J. Cell Sci. 122 2009 4099 4108
    • (2009) J. Cell Sci. , vol.122 , pp. 4099-4108
    • Ostlund, C.1    Folker, E.S.2    Choi, J.C.3    Gomes, E.R.4    Gundersen, G.G.5    Worman, H.J.6
  • 16
    • 84875190548 scopus 로고    scopus 로고
    • Nuclear positioning
    • G.G. Gundersen, and H.J. Worman Nuclear positioning Cell 152 2013 1376 1389
    • (2013) Cell , vol.152 , pp. 1376-1389
    • Gundersen, G.G.1    Worman, H.J.2
  • 17
    • 84885846858 scopus 로고    scopus 로고
    • The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin
    • A. Rothballer, and U. Kutay The diverse functional LINCs of the nuclear envelope to the cytoskeleton and chromatin Chromosoma 122 2013 415 429
    • (2013) Chromosoma , vol.122 , pp. 415-429
    • Rothballer, A.1    Kutay, U.2
  • 18
    • 84875175486 scopus 로고    scopus 로고
    • When lamins go bad: Nuclear structure and disease
    • K.H. Schreiber, and B.K. Kennedy When lamins go bad: nuclear structure and disease Cell 152 2013 1365 1375
    • (2013) Cell , vol.152 , pp. 1365-1375
    • Schreiber, K.H.1    Kennedy, B.K.2
  • 19
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • A. Mejat, and T. Misteli LINC complexes in health and disease Nucleus 1 2010 40 52
    • (2010) Nucleus , vol.1 , pp. 40-52
    • Mejat, A.1    Misteli, T.2
  • 20
    • 78651103909 scopus 로고    scopus 로고
    • Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement
    • E.S. Folker, C. Ostlund, G.W. Luxton, H.J. Worman, and G.G. Gundersen Lamin A variants that cause striated muscle disease are defective in anchoring transmembrane actin-associated nuclear lines for nuclear movement Proc. Natl. Acad. Sci. USA 108 2010 131 136
    • (2010) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 131-136
    • Folker, E.S.1    Ostlund, C.2    Luxton, G.W.3    Worman, H.J.4    Gundersen, G.G.5
  • 21
    • 77955901384 scopus 로고    scopus 로고
    • Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement
    • G.W. Luxton, E.R. Gomes, E.S. Folker, E. Vintinner, and G.G. Gundersen Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement Science 329 2010 956 959
    • (2010) Science , vol.329 , pp. 956-959
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Vintinner, E.4    Gundersen, G.G.5
  • 23
    • 84865018091 scopus 로고    scopus 로고
    • A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis
    • A. Morimoto, H. Shibuya, X. Zhu, J. Kim, K. Ishiguro, M. Han, and Y. Watanabe A conserved KASH domain protein associates with telomeres, SUN1, and dynactin during mammalian meiosis J. Cell Biol. 198 2012 165 172
    • (2012) J. Cell Biol. , vol.198 , pp. 165-172
    • Morimoto, A.1    Shibuya, H.2    Zhu, X.3    Kim, J.4    Ishiguro, K.5    Han, M.6    Watanabe, Y.7
  • 24
    • 79960685238 scopus 로고    scopus 로고
    • The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton
    • M.L. Lombardi, D.E. Jaalouk, C.M. Shanahan, B. Burke, K.J. Roux, and J. Lammerding The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton J. Biol. Chem. 286 2011 26743 26753
    • (2011) J. Biol. Chem. , vol.286 , pp. 26743-26753
    • Lombardi, M.L.1    Jaalouk, D.E.2    Shanahan, C.M.3    Burke, B.4    Roux, K.J.5    Lammerding, J.6
  • 25
    • 0032066928 scopus 로고    scopus 로고
    • Assessment of strain field in endothelial cells subjected to uniaxial deformation of their substrate
    • N. Caille, Y. Tardy, and J.J. Meister Assessment of strain field in endothelial cells subjected to uniaxial deformation of their substrate Ann. Biomed. Eng. 26 1998 409 416
    • (1998) Ann. Biomed. Eng. , vol.26 , pp. 409-416
    • Caille, N.1    Tardy, Y.2    Meister, J.J.3
  • 26
    • 84871276691 scopus 로고    scopus 로고
    • Force-induced changes in subnuclear movement and rheology
    • E.A. Booth-Gauthier, T.A. Alcoser, G. Yang, and K.N. Dahl Force-induced changes in subnuclear movement and rheology Biophys. J. 103 2012 2423 2431
    • (2012) Biophys. J. , vol.103 , pp. 2423-2431
    • Booth-Gauthier, E.A.1    Alcoser, T.A.2    Yang, G.3    Dahl, K.N.4
  • 27
    • 84866424053 scopus 로고    scopus 로고
    • Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells
    • Y.C. Poh, S.P. Shevtsov, F. Chowdhury, D.C. Wu, S. Na, M. Dundr, and N. Wang Dynamic force-induced direct dissociation of protein complexes in a nuclear body in living cells Nat. Commun. 3 2012 866
    • (2012) Nat. Commun. , vol.3 , pp. 866
    • Poh, Y.C.1    Shevtsov, S.P.2    Chowdhury, F.3    Wu, D.C.4    Na, S.5    Dundr, M.6    Wang, N.7
  • 29
    • 77956187161 scopus 로고    scopus 로고
    • Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis
    • M. Brosig, J. Ferralli, L. Gelman, M. Chiquet, and R. Chiquet-Ehrismann Interfering with the connection between the nucleus and the cytoskeleton affects nuclear rotation, mechanotransduction and myogenesis Int. J. Biochem. Cell Biol. 42 2010 1717 1728
    • (2010) Int. J. Biochem. Cell Biol. , vol.42 , pp. 1717-1728
    • Brosig, M.1    Ferralli, J.2    Gelman, L.3    Chiquet, M.4    Chiquet-Ehrismann, R.5
  • 32
    • 84878116428 scopus 로고    scopus 로고
    • Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics
    • C.Y. Ho, D.E. Jaalouk, M.K. Vartiainen, and J. Lammerding Lamin A/C and emerin regulate MKL1-SRF activity by modulating actin dynamics Nature 497 2013 507 511
    • (2013) Nature , vol.497 , pp. 507-511
    • Ho, C.Y.1    Jaalouk, D.E.2    Vartiainen, M.K.3    Lammerding, J.4
  • 34
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • E.N. Olson, and A. Nordheim Linking actin dynamics and gene transcription to drive cellular motile functions Nat. Rev. Mol. Cell Biol. 11 2010 353 365
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 35
    • 84877742076 scopus 로고    scopus 로고
    • Nuclear actin network assembly by formins regulates the SRF coactivator MAL
    • C. Baarlink, H. Wang, and R. Grosse Nuclear actin network assembly by formins regulates the SRF coactivator MAL Science 340 2013 864 867
    • (2013) Science , vol.340 , pp. 864-867
    • Baarlink, C.1    Wang, H.2    Grosse, R.3
  • 36
    • 19344378383 scopus 로고    scopus 로고
    • Emerin caps the pointed end of actin filaments: Evidence for an actin cortical network at the nuclear inner membrane
    • J.M. Holaska, A.K. Kowalski, and K.L. Wilson Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane PLoS Biol. 2 2004 E231
    • (2004) PLoS Biol. , vol.2 , pp. 231
    • Holaska, J.M.1    Kowalski, A.K.2    Wilson, K.L.3
  • 38
    • 17844379382 scopus 로고    scopus 로고
    • Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells
    • E.R. Gomes, S. Jani, and G.G. Gundersen Nuclear movement regulated by Cdc42, MRCK, myosin, and actin flow establishes MTOC polarization in migrating cells Cell 121 2005 451 463
    • (2005) Cell , vol.121 , pp. 451-463
    • Gomes, E.R.1    Jani, S.2    Gundersen, G.G.3
  • 44
    • 40349101951 scopus 로고    scopus 로고
    • Towards an integrated understanding of the structure and mechanics of the cell nucleus
    • A.C. Rowat, J. Lammerding, H. Herrmann, and U. Aebi Towards an integrated understanding of the structure and mechanics of the cell nucleus BioEssays 30 2008 226 236
    • (2008) BioEssays , vol.30 , pp. 226-236
    • Rowat, A.C.1    Lammerding, J.2    Herrmann, H.3    Aebi, U.4
  • 45
    • 33745904741 scopus 로고    scopus 로고
    • Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome
    • K.N. Dahl, P. Scaffidi, M.F. Islam, A.G. Yodh, K.L. Wilson, and T. Misteli Distinct structural and mechanical properties of the nuclear lamina in Hutchinson-Gilford progeria syndrome Proc. Natl. Acad. Sci. USA 103 2006 10271 10276
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10271-10276
    • Dahl, K.N.1    Scaffidi, P.2    Islam, M.F.3    Yodh, A.G.4    Wilson, K.L.5    Misteli, T.6
  • 46
    • 43449096922 scopus 로고    scopus 로고
    • Increased mechanosensitivity and nuclear stiffness in Hutchinson-Gilford progeria cells: Effects of farnesyltransferase inhibitors
    • V.L. Verstraeten, J.Y. Ji, K.S. Cummings, R.T. Lee, and J. Lammerding Increased mechanosensitivity and nuclear stiffness in Hutchinson-Gilford progeria cells: effects of farnesyltransferase inhibitors Aging Cell 7 2008 383 393
    • (2008) Aging Cell , vol.7 , pp. 383-393
    • Verstraeten, V.L.1    Ji, J.Y.2    Cummings, K.S.3    Lee, R.T.4    Lammerding, J.5
  • 47
    • 84874812062 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria syndrome alters nuclear shape and reduces cell motility in three dimensional model substrates
    • E.A. Booth-Gauthier, V. Du, M. Ghibaudo, A.D. Rape, K.N. Dahl, and B. Ladoux Hutchinson-Gilford progeria syndrome alters nuclear shape and reduces cell motility in three dimensional model substrates Integr. Biol. 5 2013 569 577
    • (2013) Integr. Biol. , vol.5 , pp. 569-577
    • Booth-Gauthier, E.A.1    Du, V.2    Ghibaudo, M.3    Rape, A.D.4    Dahl, K.N.5    Ladoux, B.6
  • 50
    • 70149124068 scopus 로고    scopus 로고
    • Actomyosin is the main driver of interkinetic nuclear migration in the retina
    • C. Norden, S. Young, B.A. Link, and W.A. Harris Actomyosin is the main driver of interkinetic nuclear migration in the retina Cell 138 2009 1195 1208
    • (2009) Cell , vol.138 , pp. 1195-1208
    • Norden, C.1    Young, S.2    Link, B.A.3    Harris, W.A.4
  • 51
    • 84884183110 scopus 로고    scopus 로고
    • Cell biology in neuroscience: Mechanisms of cell migration in the nervous system
    • J.A. Cooper Cell biology in neuroscience: mechanisms of cell migration in the nervous system J. Cell Biol. 202 2013 725 734
    • (2013) J. Cell Biol. , vol.202 , pp. 725-734
    • Cooper, J.A.1
  • 52
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • M. Vicente-Manzanares, J. Zareno, L. Whitmore, C.K. Choi, and A.F. Horwitz Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells J. Cell Biol. 176 2007 573 580
    • (2007) J. Cell Biol. , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 58
    • 84861455680 scopus 로고    scopus 로고
    • Growing microtubules push the oocyte nucleus to polarize the Drosophila dorsal-ventral axis
    • T. Zhao, O.S. Graham, A. Raposo, and D. St Johnston Growing microtubules push the oocyte nucleus to polarize the Drosophila dorsal-ventral axis Science 336 2012 999 1003
    • (2012) Science , vol.336 , pp. 999-1003
    • Zhao, T.1    Graham, O.S.2    Raposo, A.3    St Johnston, D.4
  • 60
    • 84857566619 scopus 로고    scopus 로고
    • Cellular traction stresses increase with increasing metastatic potential
    • C.M. Kraning-Rush, J.P. Califano, and C.A. Reinhart-King Cellular traction stresses increase with increasing metastatic potential PLoS One 7 2012 e32572
    • (2012) PLoS One , vol.7 , pp. 32572
    • Kraning-Rush, C.M.1    Califano, J.P.2    Reinhart-King, C.A.3
  • 63
  • 68
    • 84861596451 scopus 로고    scopus 로고
    • A Chinese patient with acquired partial lipodystrophy caused by a novel mutation with LMNB2 gene
    • J. Gao, Y. Li, X. Fu, and X. Luo A Chinese patient with acquired partial lipodystrophy caused by a novel mutation with LMNB2 gene J. Ped. Endocrin. Metab 25 2012 375 377
    • (2012) J. Ped. Endocrin. Metab , vol.25 , pp. 375-377
    • Gao, J.1    Li, Y.2    Fu, X.3    Luo, X.4
  • 70
    • 84860327128 scopus 로고    scopus 로고
    • Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies
    • C.Y. Chen, Y.H. Chi, R.A. Mutalif, M.F. Starost, T.G. Myers, S.A. Anderson, C.L. Stewart, and K.T. Jeang Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies Cell 149 2012 565 577
    • (2012) Cell , vol.149 , pp. 565-577
    • Chen, C.Y.1    Chi, Y.H.2    Mutalif, R.A.3    Starost, M.F.4    Myers, T.G.5    Anderson, S.A.6    Stewart, C.L.7    Jeang, K.T.8
  • 72
    • 84875604713 scopus 로고    scopus 로고
    • Cancer biology and the nuclear envelope: A convoluted relationship
    • J.I. de Las Heras, D.G. Batrakou, and E.C. Schirmer Cancer biology and the nuclear envelope: a convoluted relationship Semin. Cancer Biol. 23 2013 125 137
    • (2013) Semin. Cancer Biol. , vol.23 , pp. 125-137
    • De Las Heras, J.I.1    Batrakou, D.G.2    Schirmer, E.C.3
  • 74
    • 84859589311 scopus 로고    scopus 로고
    • Lamin A/C protein is overexpressed in tissue-invading prostate cancer and promotes prostate cancer cell growth, migration and invasion through the PI3K/AKT/PTEN pathway
    • L. Kong, G. Schafer, H. Bu, Y. Zhang, Y. Zhang, and H. Klocker Lamin A/C protein is overexpressed in tissue-invading prostate cancer and promotes prostate cancer cell growth, migration and invasion through the PI3K/AKT/PTEN pathway Carcinogenesis 33 2012 751 759
    • (2012) Carcinogenesis , vol.33 , pp. 751-759
    • Kong, L.1    Schafer, G.2    Bu, H.3    Zhang, Y.4    Zhang, Y.5    Klocker, H.6
  • 75
    • 80054706102 scopus 로고    scopus 로고
    • The role of Lamin A in cytoskeleton organization in colorectal cancer cells: A proteomic investigation
    • C.R. Foster, J.L. Robson, W.J. Simon, J. Twigg, D. Cruikshank, R.G. Wilson, and C.J. Hutchison The role of Lamin A in cytoskeleton organization in colorectal cancer cells: a proteomic investigation Nucleus 2 2011 434 443
    • (2011) Nucleus , vol.2 , pp. 434-443
    • Foster, C.R.1    Robson, J.L.2    Simon, W.J.3    Twigg, J.4    Cruikshank, D.5    Wilson, R.G.6    Hutchison, C.J.7
  • 76
    • 84876287607 scopus 로고    scopus 로고
    • 'State-of-the-heart' of cardiac laminopathies
    • M.E. Cattin, A. Muchir, and G. Bonne 'State-of-the-heart' of cardiac laminopathies Curr. Opin. Cardiol. 28 2013 297 304
    • (2013) Curr. Opin. Cardiol. , vol.28 , pp. 297-304
    • Cattin, M.E.1    Muchir, A.2    Bonne, G.3
  • 77
    • 7944230540 scopus 로고    scopus 로고
    • The emergence of integrins: A personal and historical perspective
    • R.O. Hynes The emergence of integrins: a personal and historical perspective Matrix Biol. 23 2004 333 340
    • (2004) Matrix Biol. , vol.23 , pp. 333-340
    • Hynes, R.O.1
  • 79
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • A. Muchir, G. Bonne, A.J. van der Kooi, M. van Meegen, F. Baas, P.A. Bolhuis, M. de Visser, and K. Schwartz Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B) Hum. Mol. Genet. 9 2000 1453 1459
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    Van Der Kooi, A.J.3    Van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6    De Visser, M.7    Schwartz, K.8
  • 84
    • 0037342243 scopus 로고    scopus 로고
    • A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy
    • F. Caux, E. Dubosclard, O. Lascols, B. Buendia, O. Chazouilleres, A. Cohen, J.C. Courvalin, L. Laroche, J. Capeau, and C. Vigouroux A new clinical condition linked to a novel mutation in lamins A and C with generalized lipoatrophy, insulin-resistant diabetes, disseminated leukomelanodermic papules, liver steatosis, and cardiomyopathy J. Clin. Endocrinol. Metab 88 2003 1006 1013
    • (2003) J. Clin. Endocrinol. Metab , vol.88 , pp. 1006-1013
    • Caux, F.1    Dubosclard, E.2    Lascols, O.3    Buendia, B.4    Chazouilleres, O.5    Cohen, A.6    Courvalin, J.C.7    Laroche, L.8    Capeau, J.9    Vigouroux, C.10
  • 85
    • 0141681225 scopus 로고    scopus 로고
    • The strange case of the «lumper» lamin A/C gene and human premature ageing
    • G. Novelli, and M.R. D'Apice The strange case of the «lumper» lamin A/C gene and human premature ageing Trends Mol. Med. 9 2003 370 375
    • (2003) Trends Mol. Med. , vol.9 , pp. 370-375
    • Novelli, G.1    D'Apice, M.R.2
  • 90
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • S. Bione, E. Maestrini, S. Rivella, M. Mancini, S. Regis, G. Romeo, and D. Toniolo Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy Nat. Genet. 8 1994 323 327
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.