메뉴 건너뛰기




Volumn 71, Issue 1, 2014, Pages 165-181

Cardiomyocyte growth and sarcomerogenesis at the intercalated disc

Author keywords

Adherens junction; Dilated cardiomyopathy; Electron microscopy; Heart structure; Transitional junction

Indexed keywords

ALPHAII SPECTRIN; BETA CATENIN; FODRIN; LIM PROTEIN; MUSCLE LIM PROTEIN; UNCLASSIFIED DRUG;

EID: 84891841634     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-013-1374-5     Document Type: Article
Times cited : (55)

References (56)
  • 1
    • 0030933063 scopus 로고    scopus 로고
    • MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure
    • DOI 10.1016/S0092-8674(00)81878-4
    • Arber S, Hunter JJ, Ross J Jr et al (1997) MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 88:393-403 (Pubitemid 27131381)
    • (1997) Cell , vol.88 , Issue.3 , pp. 393-403
    • Arber, S.1    Hunter, J.J.2    Ross Jr., J.3    Hongo, M.4    Sansig, G.5    Borg, J.6    Perriard, J.-C.7    Chien, K.R.8    Caroni, P.9
  • 2
    • 77955769377 scopus 로고    scopus 로고
    • The spectrin-ankyrin-4.1-adducin membrane skeleton: Adapting eukaryotic cells to the demands of animal life
    • 1:CAS:528:DC%2BC3cXhtVahtLnN 20668894 10.1007/s00709-010-0181-1
    • Baines AJ (2010) The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life. Protoplasma 244:99-131
    • (2010) Protoplasma , vol.244 , pp. 99-131
    • Baines, A.J.1
  • 3
    • 0028908119 scopus 로고
    • The cellular basis of dilated cardiomyopathy in humans
    • 1:CAS:528:DyaK2MXjvVyisrw%3D 7760353 10.1016/S0022-2828(08)80028-4
    • Beltrami CA, Finato N, Rocco M et al (1995) The cellular basis of dilated cardiomyopathy in humans. J Mol Cell Cardiol 27:291-305
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 291-305
    • Beltrami, C.A.1    Finato, N.2    Rocco, M.3
  • 4
    • 84859249623 scopus 로고    scopus 로고
    • From myofibril to membrane; The transitional junction at the intercalated disc
    • 1:CAS:528:DC%2BC3MXhsFyhtLvO 10.2741/3972
    • Bennett PM (2012) From myofibril to membrane; the transitional junction at the intercalated disc. Front Biosci 17:1035-1050
    • (2012) Front Biosci , vol.17 , pp. 1035-1050
    • Bennett, P.M.1
  • 5
    • 4043122640 scopus 로고    scopus 로고
    • Not just a plasma membrane protein: In cardiac muscle cells alpha-II spectrin also shows a close association with myofibrils
    • DOI 10.1023/B:JURE.0000035892.77399.51
    • Bennett PM, Baines AJ, Lecomte MC et al (2004) Not just a plasma membrane protein: in cardiac muscle cells alpha-II spectrin also shows a close association with myofibrils. J Muscle Res Cell Motil 25:119-126 (Pubitemid 39060886)
    • (2004) Journal of Muscle Research and Cell Motility , vol.25 , Issue.2 , pp. 119-126
    • Bennett, P.M.1    Baines, A.J.2    Lecomte, M.-C.3    Maggs, A.M.4    Pinder, J.C.5
  • 6
    • 33745425651 scopus 로고    scopus 로고
    • The transitional junction: A new functional subcellular domain at the intercalated disc
    • DOI 10.1091/mbc.E05-12-1109
    • Bennett PM, Maggs AM, Baines AJ et al (2006) The transitional junction: a new functional subcellular domain at the intercalated disc. Mol Biol Cell 17:2091-2100 (Pubitemid 44011621)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 2091-2100
    • Bennett, P.M.1    Maggs, A.M.2    Baines, A.J.3    Pinder, J.C.4
  • 7
    • 33646555794 scopus 로고    scopus 로고
    • The area composita of adhering junctions connecting heart muscle cells of vertebrates, II. Colocalizations of desmosomal and fascia adherens molecules in the intercalated disk
    • 1:CAS:528:DC%2BD28XmsVOju7g%3D 16600422 10.1016/j.ejcb.2006.02.009
    • Borrmann CM, Grund C, Kuhn C et al (2006) The area composita of adhering junctions connecting heart muscle cells of vertebrates, II. Colocalizations of desmosomal and fascia adherens molecules in the intercalated disk. Eur J Cell Biol 85:469-485
    • (2006) Eur J Cell Biol , vol.85 , pp. 469-485
    • Borrmann, C.M.1    Grund, C.2    Kuhn, C.3
  • 11
    • 0034025435 scopus 로고    scopus 로고
    • The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of βI-spectrin
    • Flick MJ, Konieczny SF (2000) The muscle regulatory and structural protein MLP is a cytoskeletal binding partner of beta I-spectrin. J Cell Sci 113(Pt 9):1553-1564 (Pubitemid 30312504)
    • (2000) Journal of Cell Science , vol.113 , Issue.9 , pp. 1553-1564
    • Flick, M.J.1    Konieczny, S.F.2
  • 12
    • 0022142987 scopus 로고
    • The sarcoplasmic reticulum of mouse heart: Its divisions, configurations, and distribution
    • 1:STN:280:DyaL283islKktQ%3D%3D 3835280 10.1016/0889-1605(85)90080-1
    • Forbes MS, Hawkey LA, Jirge SK et al (1985) The sarcoplasmic reticulum of mouse heart: its divisions, configurations, and distribution. J Ultrastruct Res 93:1-16
    • (1985) J Ultrastruct Res , vol.93 , pp. 1-16
    • Forbes, M.S.1    Hawkey, L.A.2    Jirge, S.K.3
  • 13
    • 0022410203 scopus 로고
    • Intercalated discs of mammalian heart: A review of structure and function
    • DOI 10.1016/0040-8166(85)90001-1
    • Forbes MS, Sperelakis N (1985) Intercalated discs of mammalian heart: a review of structure and function. Tissue Cell 17:605-648 (Pubitemid 16243839)
    • (1985) Tissue and Cell , vol.17 , Issue.5 , pp. 605-648
    • Forbes, M.S.1    Sperelakis, N.2
  • 14
    • 77952938686 scopus 로고    scopus 로고
    • Discovering the molecular components of intercellular junctions - A historical view
    • 20066111 10.1101/cshperspect.a003061
    • Franke WW (2009) Discovering the molecular components of intercellular junctions - a historical view. Cold Spring Harb Perspect Biol 1:a003061
    • (2009) Cold Spring Harb Perspect Biol , vol.1 , pp. 003061
    • Franke, W.W.1
  • 15
    • 0035841636 scopus 로고    scopus 로고
    • Cardiomyopathies: From genetics to the prospect of treatment
    • DOI 10.1016/S0140-6736(01)06657-0
    • Franz WM, Muller OJ, Katus HA (2001) Cardiomyopathies: from genetics to the prospect of treatment. Lancet 358:1627-1637 (Pubitemid 33101920)
    • (2001) Lancet , vol.358 , Issue.9293 , pp. 1627-1637
    • Franz, W.-M.1    Muller, O.J.2    Katus, H.A.3
  • 16
    • 62449236060 scopus 로고    scopus 로고
    • Back to square one: What do we know about the functions of muscle LIM protein in the heart?
    • Gehmlich K, Geier C, Milting H et al (2008) Back to square one: what do we know about the functions of muscle LIM protein in the heart? J Muscle Res Cell Motil 29(6-8):155-158
    • (2008) J Muscle Res Cell Motil , vol.29 , Issue.6-8 , pp. 155-158
    • Gehmlich, K.1    Geier, C.2    Milting, H.3
  • 17
    • 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 KJ et al (2004) Decreased interactions of mutant muscle LIM protein (MLP) with N-RAP and alpha-actinin and their implication for hypertrophic cardiomyopathy. Cell Tissue Res 317:129-136 (Pubitemid 39070612)
    • (2004) Cell and Tissue Research , vol.317 , Issue.2 , pp. 129-136
    • Gehmlich, K.1    Geier, C.2    Osterziel, K.J.3    Van Der Ven, P.F.M.4    Furst, D.O.5
  • 18
    • 0028960907 scopus 로고
    • Structural remodelling and mechanical dysfunction of cardiac myocytes in heart failure
    • 1:CAS:528:DyaK2MXltVertbk%3D 7602601 10.1016/0022-2828(95)90000-4
    • Gerdes AM, Capasso JM (1995) Structural remodelling and mechanical dysfunction of cardiac myocytes in heart failure. J Mol Cell Cardiol 27:849-856
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 849-856
    • Gerdes, A.M.1    Capasso, J.M.2
  • 19
    • 0034130363 scopus 로고    scopus 로고
    • Identification of a novel C-terminal variant of βII spectrin: Two isoforms of βII spectrin have distinct intracellular locations and activities
    • Hayes NV, Scott C, Heerkens E et al (2000) Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities. J Cell Sci 113(Pt 11):2023-2034 (Pubitemid 30386506)
    • (2000) Journal of Cell Science , vol.113 , Issue.11 , pp. 2023-2034
    • Hayes, N.V.L.1    Scott, C.2    Heerkens, E.3    Ohanian, V.4    Maggs, A.M.5    Pinder, J.C.6    Kordeli, E.7    Baines, A.J.8
  • 21
    • 77956186257 scopus 로고    scopus 로고
    • Stabilised beta-catenin in postnatal ventricular myocardium leads to dilated cardiomyopathy and premature death
    • 1:CAS:528:DC%2BC3cXpslClsrg%3D 20376467 10.1007/s00395-010-0101-8
    • Hirschy A, Croquelois A, Perriard E et al (2010) Stabilised beta-catenin in postnatal ventricular myocardium leads to dilated cardiomyopathy and premature death. Basic Res Cardiol 105:597-608
    • (2010) Basic Res Cardiol , vol.105 , pp. 597-608
    • Hirschy, A.1    Croquelois, A.2    Perriard, E.3
  • 22
    • 30044442758 scopus 로고    scopus 로고
    • Establishment of cardiac cytoarchitecture in the developing mouse heart
    • DOI 10.1016/j.ydbio.2005.10.046, PII S0012160605007839
    • Hirschy A, Schatzmann F, Ehler E et al (2006) Establishment of cardiac cytoarchitecture in the developing mouse heart. Dev Biol 289:430-441 (Pubitemid 43049945)
    • (2006) Developmental Biology , vol.289 , Issue.2 , pp. 430-441
    • Hirschy, A.1    Schatzmann, F.2    Ehler, E.3    Perriard, J.-C.4
  • 23
    • 77649170228 scopus 로고    scopus 로고
    • Molecular basis of hereditary cardiomyopathy: Abnormalities in calcium sensitivity, stretch response, stress response and beyond
    • 1:CAS:528:DC%2BC3cXisVaht70%3D 20075948 10.1038/jhg.2009.138
    • Kimura A (2010) Molecular basis of hereditary cardiomyopathy: abnormalities in calcium sensitivity, stretch response, stress response and beyond. J Hum Genet 55:81-90
    • (2010) J Hum Genet , vol.55 , pp. 81-90
    • Kimura, A.1
  • 25
    • 0033678504 scopus 로고    scopus 로고
    • The cytoskeleton and related proteins in the human failing heart
    • 1:CAS:528:DC%2BD3MXhsVKk 16228910 10.1023/A:1009813621103
    • Kostin S, Hein S, Arnon E et al (2000) The cytoskeleton and related proteins in the human failing heart. Heart Fail Rev 5:271-280
    • (2000) Heart Fail Rev , vol.5 , pp. 271-280
    • Kostin, S.1    Hein, S.2    Arnon, E.3
  • 26
    • 0034798853 scopus 로고    scopus 로고
    • Characterisation of postnatal growth of the murine heart
    • DOI 10.1007/s004290100206
    • Leu M, Ehler E, Perriard JC (2001) Characterisation of postnatal growth of the murine heart. Anat Embryol (Berl) 204:217-224 (Pubitemid 32938437)
    • (2001) Anatomy and Embryology , vol.204 , Issue.3 , pp. 217-224
    • Leu, M.1    Ehler, E.2    Perriard, J.-C.3
  • 27
    • 84861211989 scopus 로고    scopus 로고
    • Loss of alphaT-catenin alters the hybrid adhering junctions in the heart and leads to dilated cardiomyopathy and ventricular arrhythmia following acute ischemia
    • 1:CAS:528:DC%2BC38Xmsl2nu7Y%3D 22421363 10.1242/jcs.098640
    • Li J, Goossens S, Van Hengel J et al (2012) Loss of alphaT-catenin alters the hybrid adhering junctions in the heart and leads to dilated cardiomyopathy and ventricular arrhythmia following acute ischemia. J Cell Sci 125:1058-1067
    • (2012) J Cell Sci , vol.125 , pp. 1058-1067
    • Li, J.1    Goossens, S.2    Van Hengel, J.3
  • 28
    • 84862755022 scopus 로고    scopus 로고
    • A new perspective on intercalated disc organization: Implications for heart disease
    • 2879923 20585598
    • Li J, Radice GL (2010) A new perspective on intercalated disc organization: implications for heart disease. Dermatol Res Pract 2010:207835
    • (2010) Dermatol Res Pract , vol.2010 , pp. 207835
    • Li, J.1    Radice, G.L.2
  • 29
    • 17444401402 scopus 로고    scopus 로고
    • N-RAP expression during mouse heart development
    • DOI 10.1002/dvdy.20314
    • Lu S, Borst DE, Horowits R (2005) N-RAP expression during mouse heart development. Dev Dyn 233:201-212 (Pubitemid 40548039)
    • (2005) Developmental Dynamics , vol.233 , Issue.1 , pp. 201-212
    • Lu, S.1    Borst, D.E.2    Horowits, R.3
  • 30
    • 66149091985 scopus 로고    scopus 로고
    • Loss of t-tubules and other changes to surface topography in ventricular myocytes from failing human and rat heart
    • 1:CAS:528:DC%2BD1MXlsFait74%3D 19342485 10.1073/pnas.0809777106
    • Lyon AR, Macleod KT, Zhang Y et al (2009) Loss of t-tubules and other changes to surface topography in ventricular myocytes from failing human and rat heart. Proc Natl Acad Sci USA 106:6854-6859
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6854-6859
    • Lyon, A.R.1    Macleod, K.T.2    Zhang, Y.3
  • 31
    • 79952196493 scopus 로고    scopus 로고
    • Novel interactions of ankyrins-G at the costameres: The muscle-specific obscurin/titin-binding-related domain (OTBD) binds plectin and filamin C
    • 1:CAS:528:DC%2BC3MXjsFWnur8%3D 21223964 10.1016/j.yexcr.2011.01.002
    • Maiweilidan Y, Klauza I, Kordeli E (2011) Novel interactions of ankyrins-G at the costameres: the muscle-specific obscurin/titin-binding-related domain (OTBD) binds plectin and filamin C. Exp Cell Res 317:724-736
    • (2011) Exp Cell Res , vol.317 , pp. 724-736
    • Maiweilidan, Y.1    Klauza, I.2    Kordeli, E.3
  • 33
    • 0025978369 scopus 로고
    • Cellular basis of chronic ventricular remodelling after myocardial infarction in rats
    • 1:STN:280:DyaK38%2Fns1Gkuw%3D%3D 1742871 10.1161/01.RES.68.3.856
    • Olivetti G, Capasso JM, Meggs LG et al (1991) Cellular basis of chronic ventricular remodelling after myocardial infarction in rats. Circ Res 68:856-869
    • (1991) Circ Res , vol.68 , pp. 856-869
    • Olivetti, G.1    Capasso, J.M.2    Meggs, L.G.3
  • 34
    • 76649113736 scopus 로고    scopus 로고
    • Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin
    • 1:CAS:528:DC%2BC3cXjs1Kku70%3D 20086044 10.1242/jcs.056432
    • Peng X, Cuff LE, Lawton CD et al (2010) Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin. J Cell Sci 123:567-577
    • (2010) J Cell Sci , vol.123 , pp. 567-577
    • Peng, X.1    Cuff, L.E.2    Lawton, C.D.3
  • 35
    • 0037237653 scopus 로고    scopus 로고
    • Dilated cardiomyopathy: A disease of the intercalated disc?
    • DOI 10.1016/S1050-1738(02)00209-8, PII S1050173802002098
    • Perriard JC, Hirschy A, Ehler E (2003) Dilated cardiomyopathy: a disease of the intercalated disc? Trends Cardiovasc Med 13:30-38 (Pubitemid 36120547)
    • (2003) Trends in Cardiovascular Medicine , vol.13 , Issue.1 , pp. 30-38
    • Perriard, J.-C.1    Hirschy, A.2    Ehler, E.3
  • 36
    • 84862023004 scopus 로고    scopus 로고
    • Isoforms of protein 4.1 are differentially distributed in heart muscle cells: Relation of 4.1R and 4.1G to components of the Ca(2+) homeostasis system
    • 1:CAS:528:DC%2BC38XmvFKmu74%3D 22429617 10.1016/j.yexcr.2012.03.003
    • Pinder JC, Taylor-Harris PM, Bennett PM et al (2012) Isoforms of protein 4.1 are differentially distributed in heart muscle cells: relation of 4.1R and 4.1G to components of the Ca(2+) homeostasis system. Exp Cell Res 318:1467-1479
    • (2012) Exp Cell Res , vol.318 , pp. 1467-1479
    • Pinder, J.C.1    Taylor-Harris, P.M.2    Bennett, P.M.3
  • 38
    • 76649084202 scopus 로고    scopus 로고
    • Molecular and functional characterization of a novel cardiac-specific human tropomyosin isoform
    • 1:CAS:528:DC%2BC3cXlvFajug%3D%3D 2822663 20065163 10.1161/CIRCULATIONAHA. 109.889725
    • Rajan S, Jagatheesan G, Karam CN et al (2010) Molecular and functional characterization of a novel cardiac-specific human tropomyosin isoform. Circulation 121:410-418
    • (2010) Circulation , vol.121 , pp. 410-418
    • Rajan, S.1    Jagatheesan, G.2    Karam, C.N.3
  • 39
    • 84865214658 scopus 로고    scopus 로고
    • Intercalated disc abnormalities, reduced Na(+) current density, and conduction slowing in desmoglein-2 mutant mice prior to cardiomyopathic changes
    • 1:CAS:528:DC%2BC38Xht1egu7vF 22764152 10.1093/cvr/cvs219
    • Rizzo S, Lodder EM, Verkerk AO et al (2012) Intercalated disc abnormalities, reduced Na(+) current density, and conduction slowing in desmoglein-2 mutant mice prior to cardiomyopathic changes. Cardiovasc Res 95:409-418
    • (2012) Cardiovasc Res , vol.95 , pp. 409-418
    • Rizzo, S.1    Lodder, E.M.2    Verkerk, A.O.3
  • 40
    • 77954558964 scopus 로고    scopus 로고
    • Assembly and dynamics of myofibrils
    • 2896905 20625425 10.1155/2010/858606
    • Sanger JW, Wang J, Fan Y et al (2010) Assembly and dynamics of myofibrils. J Biomed Biotechnol 2010:858606
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 858606
    • Sanger, J.W.1    Wang, J.2    Fan, Y.3
  • 42
    • 0029268878 scopus 로고
    • Multifaceted morphological alterations are present in the failing human heart
    • 1:CAS:528:DyaK2MXltVertbY%3D 7602602 10.1016/0022-2828(95)90034-9
    • Schaper J, Hein S, Scholz D et al (1995) Multifaceted morphological alterations are present in the failing human heart. J Mol Cell Cardiol 27:857-861
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 857-861
    • Schaper, J.1    Hein, S.2    Scholz, D.3
  • 43
    • 79957866415 scopus 로고    scopus 로고
    • EH-myomesin splice isoform is a novel marker for dilated cardiomyopathy
    • 1:CAS:528:DC%2BC3MXhsFGnu7w%3D 3032906 21069531 10.1007/s00395-010-0131-2
    • Schoenauer R, Emmert MY, Felley A et al (2011) EH-myomesin splice isoform is a novel marker for dilated cardiomyopathy. Basic Res Cardiol 106:233-247
    • (2011) Basic Res Cardiol , vol.106 , pp. 233-247
    • Schoenauer, R.1    Emmert, M.Y.2    Felley, A.3
  • 44
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • DOI 10.1016/S0092-8674(01)00242-2
    • Seidman JG, Seidman C (2001) The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 104:557-567 (Pubitemid 32201950)
    • (2001) Cell , vol.104 , Issue.4 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 46
    • 54449098592 scopus 로고    scopus 로고
    • Cytoskeletal protein 4.1R affects repolarization and regulates calcium handling in the heart
    • 1:CAS:528:DC%2BD1cXhtFOis73O 18787192 10.1161/CIRCRESAHA.108.176461
    • Stagg MA, Carter E, Sohrabi N et al (2008) Cytoskeletal protein 4.1R affects repolarization and regulates calcium handling in the heart. Circ Res 103:855-863
    • (2008) Circ Res , vol.103 , pp. 855-863
    • Stagg, M.A.1    Carter, E.2    Sohrabi, N.3
  • 47
    • 17644413588 scopus 로고    scopus 로고
    • Cardiac muscle cell cytoskeletal protein 4.1: Analysis of transcripts and subcellular location - Relevance to membrane integrity, microstructure, and possible role in heart failure
    • DOI 10.1007/s00335-004-2436-7
    • Taylor-Harris PM, Keating LA, Maggs AM et al (2005) Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location - relevance to membrane integrity, microstructure, and possible role in heart failure. Mamm Genome 16:137-151 (Pubitemid 40569190)
    • (2005) Mammalian Genome , vol.16 , Issue.3 , pp. 137-151
    • Taylor-Harris, P.M.1    Keating, L.A.2    Maggs, A.M.3    Phillips, G.W.4    Birks, E.J.5    Franklin, R.C.G.6    Yacoub, M.H.7    Baines, A.J.8    Pinder, J.C.9
  • 48
    • 0018372655 scopus 로고
    • Domains of receptor mobility and endocytosis in the membranes of neonatal human erythrocytes and reticulocytes are deficient in spectrin
    • Tokuyasu KT, Schekman R, Singer SJ (1979) Domains of receptor mobility and endocytosis in the membranes of neonatal human erythrocytes and reticulocytes are deficient in spectrin. J Cell Biol 80:481-486 (Pubitemid 9091520)
    • (1979) Journal of Cell Biology , vol.80 , Issue.2 , pp. 481-486
    • Tokuyasu, K.T.1    Schekman, R.2    Singer, S.J.3
  • 51
    • 33645068887 scopus 로고    scopus 로고
    • A role for muscle LIM protein (MLP) in vascular remodelling
    • 1:CAS:528:DC%2BD28XivVGqsLk%3D 16519896 10.1016/j.yjmcc.2006.01.005
    • Wang X, Li Q, Adhikari N et al (2006) A role for muscle LIM protein (MLP) in vascular remodelling. J Mol Cell Cardiol 40:503-509
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 503-509
    • Wang, X.1    Li, Q.2    Adhikari, N.3
  • 54
    • 76149101293 scopus 로고    scopus 로고
    • Weaving hypothesis of cardiomyocyte sarcomeres: Discovery of periodic broadening and narrowing of intercalated disk during volume-load change
    • 20056839 10.2353/ajpath.2010.090348
    • Yoshida M, Sho E, Nanjo H et al (2010) Weaving hypothesis of cardiomyocyte sarcomeres: discovery of periodic broadening and narrowing of intercalated disk during volume-load change. Am J Pathol 176:660-678
    • (2010) Am J Pathol , vol.176 , pp. 660-678
    • Yoshida, M.1    Sho, E.2    Nanjo, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.