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Volumn 586, Issue 14, 2012, Pages 2003-2015

Matrix-dependent perturbation of TGFβ signaling and disease

Author keywords

Extracellular matrix; Fibrillin; Integrin; Marfan syndrome; Stiff skin syndrome; Transforming growth factor beta

Indexed keywords

ADAMST LIKE PROTEIN 2; ADAMTS1 PROTEIN; ANGIOTENSIN 1 RECEPTOR; ANGIOTENSIN 2 RECEPTOR; CELL MEMBRANE PROTEIN; CHEMOKINE RECEPTOR CCR2; ENALAPRIL; FIBRILLIN; FIBRILLIN 1; FIBULIN; FIBULIN 4; FIBULIN 5; GELATINASE A; GELATINASE B; INTEGRIN; LOSARTAN; METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MONOCYTE CHEMOTACTIC PROTEIN 1; PERINDOPRIL; PLACEBO; RECEPTOR REGULATED SMAD PROTEIN; SIMVASTATIN; SMAD2 PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; UNCLASSIFIED DRUG;

EID: 84862763855     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.05.027     Document Type: Review
Times cited : (113)

References (139)
  • 1
    • 21444434608 scopus 로고    scopus 로고
    • Fibronectin regulates latent transforming growth factor-β (TGFβ) by controlling matrix assembly of latent TGFβ binding protein-1
    • S.L. Dallas, P. Sivakumar, C.J.P. Jones, Q. Chen, D.M. Peters, D.F. Mosher, M.J. Humphries, and C.M. Kielty Fibronectin regulates latent transforming growth factor-β (TGFβ) by controlling matrix assembly of latent TGFβ binding protein-1 J. Biol. Chem. 280 2005 18871 18880
    • (2005) J. Biol. Chem. , vol.280 , pp. 18871-18880
    • Dallas, S.L.1    Sivakumar, P.2    Jones, C.J.P.3    Chen, Q.4    Peters, D.M.5    Mosher, D.F.6    Humphries, M.J.7    Kielty, C.M.8
  • 2
    • 34548844181 scopus 로고    scopus 로고
    • Potential role for heparan sulfate proteoglycans in regulation of transforming growth factor-β (TGF-β) by modulating assembly of latent TGF-β-binding protein-1
    • Q. Chen, P. Sivakumar, C. Barley, D.M. Peters, R.R. Gomes, M.C. Farach-Carson, and S.L. Dallas Potential role for heparan sulfate proteoglycans in regulation of transforming growth factor-β (TGF-β) by modulating assembly of latent TGF-β-binding protein-1 J. Biol. Chem. 282 2007 26418 26430
    • (2007) J. Biol. Chem. , vol.282 , pp. 26418-26430
    • Chen, Q.1    Sivakumar, P.2    Barley, C.3    Peters, D.M.4    Gomes, R.R.5    Farach-Carson, M.C.6    Dallas, S.L.7
  • 4
    • 49049110677 scopus 로고    scopus 로고
    • Integrins and the activation of latent transforming growth factor β1 - An intimate relationship
    • P.-J. Wipff, and B. Hinz Integrins and the activation of latent transforming growth factor β1 - An intimate relationship Eur. J. Cell Biol. 87 2008 601 615
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 601-615
    • Wipff, P.-J.1    Hinz, B.2
  • 9
    • 0028175961 scopus 로고
    • Angiotensin receptor regulates cardiac hypertrophy and transforming growth factor-beta 1 expression
    • A.D. Everett, A. Tufro-McReddie, A. Fisher, and R.A. Gomez Angiotensin receptor regulates cardiac hypertrophy and transforming growth factor-beta 1 expression Hypertension. 23 1994 587 592
    • (1994) Hypertension. , vol.23 , pp. 587-592
    • Everett, A.D.1    Tufro-Mcreddie, A.2    Fisher, A.3    Gomez, R.A.4
  • 10
    • 0034051005 scopus 로고    scopus 로고
    • Angiotensin II upregulates transforming growth factor-beta type i receptor on rat vascular smooth muscle cells
    • N. Fukuda, W.Y. Hu, A. Kubo, H. Kishioka, C. Satoh, M. Soma, Y. Izumi, and K. Kanmatsuse Angiotensin II upregulates transforming growth factor-beta type I receptor on rat vascular smooth muscle cells Am. J. Hypertens. 13 2000 191 198
    • (2000) Am. J. Hypertens. , vol.13 , pp. 191-198
    • Fukuda, N.1    Hu, W.Y.2    Kubo, A.3    Kishioka, H.4    Satoh, C.5    Soma, M.6    Izumi, Y.7    Kanmatsuse, K.8
  • 11
    • 0032836965 scopus 로고    scopus 로고
    • Angiotensin II stimulates expression of transforming growth factor beta receptor type II in cultured mouse proximal tubular cells
    • G. Wolf, F.N. Ziyadeh, and R.A. Stahl Angiotensin II stimulates expression of transforming growth factor beta receptor type II in cultured mouse proximal tubular cells J. Mol. Med. 77 1999 556 564
    • (1999) J. Mol. Med. , vol.77 , pp. 556-564
    • Wolf, G.1    Ziyadeh, F.N.2    Stahl, R.A.3
  • 12
    • 0942301311 scopus 로고    scopus 로고
    • Angiotensin II induces thrombospondin-1 production in human mesangial cells via p38 MAPK and JNK: A mechanism for activation of latent TGF-beta1
    • T. Naito, T. Masaki, D.J. Nikolic-Paterson, C. Tanji, N. Yorioka, and N. Kohno Angiotensin II induces thrombospondin-1 production in human mesangial cells via p38 MAPK and JNK: a mechanism for activation of latent TGF-beta1 Am. J. Physiol. Renal. Physiol. 286 2 2004 F278 F287
    • (2004) Am. J. Physiol. Renal. Physiol. , vol.286 , Issue.2
    • Naito, T.1    Masaki, T.2    Nikolic-Paterson, D.J.3    Tanji, C.4    Yorioka, N.5    Kohno, N.6
  • 16
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signalling
    • R. Derynck, and Y.E. Zhang Smad-dependent and Smad-independent pathways in TGF-beta family signalling Nature. 425 2003 577 584
    • (2003) Nature. , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 19
    • 7444272132 scopus 로고    scopus 로고
    • Angiotensin AT2 receptor contributes to cardiovascular remodelling of aged rats during chronic AT1 receptor blockade
    • E.S. Jones, M.J. Black, and R.E. Widdop Angiotensin AT2 receptor contributes to cardiovascular remodelling of aged rats during chronic AT1 receptor blockade J. Mol. Cell Cardiol. 37 2004 1023 1030
    • (2004) J. Mol. Cell Cardiol. , vol.37 , pp. 1023-1030
    • Jones, E.S.1    Black, M.J.2    Widdop, R.E.3
  • 22
    • 17444380829 scopus 로고    scopus 로고
    • Usefulness of enalapril versus propranolol or atenolol for prevention of aortic dilation in patients with the Marfan syndrome
    • A.T. Yetman, R.A. Bornemeier, and B.W. McCrindle Usefulness of enalapril versus propranolol or atenolol for prevention of aortic dilation in patients with the Marfan syndrome Am. J. Cardiol. 95 2005 1125 1127
    • (2005) Am. J. Cardiol. , vol.95 , pp. 1125-1127
    • Yetman, A.T.1    Bornemeier, R.A.2    McCrindle, B.W.3
  • 23
    • 34948849376 scopus 로고    scopus 로고
    • Effect of perindopril on large artery stiffness and aortic root diameter in patients with Marfan syndrome: A randomized controlled trial
    • A.A. Ahimastos, A. Aggarwal, K.M. D'Orsa, M.F. Formosa, A.J. White, R. Savarirayan, A.M. Dart, and B.A. Kingwell Effect of perindopril on large artery stiffness and aortic root diameter in patients with Marfan syndrome: a randomized controlled trial JAMA. 298 13 2007 1539 1547
    • (2007) JAMA. , vol.298 , Issue.13 , pp. 1539-1547
    • Ahimastos, A.A.1    Aggarwal, A.2    D'Orsa, K.M.3    Formosa, M.F.4    White, A.J.5    Savarirayan, R.6    Dart, A.M.7    Kingwell, B.A.8
  • 25
    • 65549088034 scopus 로고    scopus 로고
    • P38 MAPK is an early determinant of promiscuous Smad2/3 signaling in the aortas of fibrillin-1 (Fbn1)-null mice
    • L. Carta, S. Smaldone, L. Zilberberg, D. Loch, H.C. Dietz, D.B. Rifkin, and F. Ramirez P38 MAPK is an early determinant of promiscuous Smad2/3 signaling in the aortas of fibrillin-1 (Fbn1)-null mice J. Biol. Chem. 284 9 2009 5630 5636
    • (2009) J. Biol. Chem. , vol.284 , Issue.9 , pp. 5630-5636
    • Carta, L.1    Smaldone, S.2    Zilberberg, L.3    Loch, D.4    Dietz, H.C.5    Rifkin, D.B.6    Ramirez, F.7
  • 26
    • 49049102691 scopus 로고    scopus 로고
    • Genetic approaches for changing the heart and dissecting complex syndromes
    • M.A. Moga, T. Nakamura, and J. Robbins Genetic approaches for changing the heart and dissecting complex syndromes J. Mol. Cell Cardiol. 45 2 2008 148 155
    • (2008) J. Mol. Cell Cardiol. , vol.45 , Issue.2 , pp. 148-155
    • Moga, M.A.1    Nakamura, T.2    Robbins, J.3
  • 27
    • 42549132541 scopus 로고    scopus 로고
    • Long-term doxycycline is more effective than atenolol to prevent thoracic aortic aneurysm in marfan syndrome through the inhibition of matrix metalloproteinase-2 and -9
    • A.W. Chung, H.H. Yang, M.W. Radomski, and C. van Breemen Long-term doxycycline is more effective than atenolol to prevent thoracic aortic aneurysm in marfan syndrome through the inhibition of matrix metalloproteinase-2 and -9 Circ. Res. 102 8 2008 e73 e85
    • (2008) Circ. Res. , vol.102 , Issue.8
    • Chung, A.W.1    Yang, H.H.2    Radomski, M.W.3    Van Breemen, C.4
  • 28
    • 37549052556 scopus 로고    scopus 로고
    • Doxycycline delays aneurysm rupture in a mouse model of Marfan syndrome
    • W. Xiong, R.A. Knispel, H.C. Dietz, F. Ramirez, and B.T. Baxter Doxycycline delays aneurysm rupture in a mouse model of Marfan syndrome J. Vasc. Surg. 47 1 2008 166 172
    • (2008) J. Vasc. Surg. , vol.47 , Issue.1 , pp. 166-172
    • Xiong, W.1    Knispel, R.A.2    Dietz, H.C.3    Ramirez, F.4    Baxter, B.T.5
  • 29
    • 70350538712 scopus 로고    scopus 로고
    • Long-term effects of losartan on structure and function of the thoracic aorta in a mouse model of Marfan syndrome
    • H.H. Yang, J.M. Kim, E. Chum, C. van Breemen, and A.W. Chung Long-term effects of losartan on structure and function of the thoracic aorta in a mouse model of Marfan syndrome Br. J. Pharmacol. 158 6 2009 1503 1512
    • (2009) Br. J. Pharmacol. , vol.158 , Issue.6 , pp. 1503-1512
    • Yang, H.H.1    Kim, J.M.2    Chum, E.3    Van Breemen, C.4    Chung, A.W.5
  • 30
    • 77955473542 scopus 로고    scopus 로고
    • Effectiveness of combination of losartan potassium and doxycycline versus single-drug treatments in the secondary prevention of thoracic aortic aneurysm in Marfan syndrome
    • H.H. Yang, J.M. Kim, E. Chum, C. van Breemen, and A.W. Chung Effectiveness of combination of losartan potassium and doxycycline versus single-drug treatments in the secondary prevention of thoracic aortic aneurysm in Marfan syndrome J. Thorac. Cardiovasc. Surg. 140 2 2010 305 312
    • (2010) J. Thorac. Cardiovasc. Surg. , vol.140 , Issue.2 , pp. 305-312
    • Yang, H.H.1    Kim, J.M.2    Chum, E.3    Van Breemen, C.4    Chung, A.W.5
  • 31
    • 0037389156 scopus 로고    scopus 로고
    • Oncostatin M, an interleukin-6 family cytokine, upregulates matrix metalloproteinase-9 through the mitogen-activated protein kinase kinase-extracellular signal-regulated kinase pathway in cultured smooth muscle cells
    • T. Nagata, H. Kai, R. Shibata, M. Koga, A. Yoshimura, and T. Imaizumi Oncostatin M, an interleukin-6 family cytokine, upregulates matrix metalloproteinase-9 through the mitogen-activated protein kinase kinase-extracellular signal-regulated kinase pathway in cultured smooth muscle cells Arterioscler. Thromb. Vasc. Biol. 23 4 2003 588 593
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , Issue.4 , pp. 588-593
    • Nagata, T.1    Kai, H.2    Shibata, R.3    Koga, M.4    Yoshimura, A.5    Imaizumi, T.6
  • 32
    • 10044256495 scopus 로고    scopus 로고
    • Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries
    • P.A. Lucchesi, A. Sabri, S. Belmadani, and K. Matrougui Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries Circulation. 110 23 2004 3587 3593
    • (2004) Circulation. , vol.110 , Issue.23 , pp. 3587-3593
    • Lucchesi, P.A.1    Sabri, A.2    Belmadani, S.3    Matrougui, K.4
  • 33
    • 73949130785 scopus 로고    scopus 로고
    • Simvastatin inhibits angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-knockout mice. possible role of ERK
    • Y. Zhang, J.C. Naggar, C.M. Welzig, D. Beasley, K.S. Moulton, H.J. Park, and J.B. Galper Simvastatin inhibits angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-knockout mice. possible role of ERK Arterioscler. Thromb. Vasc. Biol. 29 11 2009 1764 1771
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , Issue.11 , pp. 1764-1771
    • Zhang, Y.1    Naggar, J.C.2    Welzig, C.M.3    Beasley, D.4    Moulton, K.S.5    Park, H.J.6    Galper, J.B.7
  • 36
    • 0028828221 scopus 로고
    • Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly
    • E.A. Putnam, H. Zhang, F. Ramirez, and D.M. Milewicz Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly Nat. Genet. 11 4 1995 456 458
    • (1995) Nat. Genet. , vol.11 , Issue.4 , pp. 456-458
    • Putnam, E.A.1    Zhang, H.2    Ramirez, F.3    Milewicz, D.M.4
  • 37
    • 84862765305 scopus 로고    scopus 로고
    • Chapter 22: Fibrosis Insights from Stiff Skin Syndrome in Scleroderma
    • F.M. Wigley, J. Varga, C.P. Denton, Springer Press
    • E.E. Gerber, and H.C. Dietz Chapter 22: Fibrosis Insights from Stiff Skin Syndrome in Scleroderma F.M. Wigley, J. Varga, C.P. Denton, From Pathogenesis to Comprehensive Management 2012 Springer Press
    • (2012) From Pathogenesis to Comprehensive Management
    • Gerber, E.E.1    Dietz, H.C.2
  • 39
    • 0033041098 scopus 로고    scopus 로고
    • Remodeling of elastic fiber components in scleroderma skin
    • E.C. Davis, S.A. Blattel, and R.P. Mecham Remodeling of elastic fiber components in scleroderma skin Connect. Tissue Res. 40 2 1999 113 121
    • (1999) Connect. Tissue Res. , vol.40 , Issue.2 , pp. 113-121
    • Davis, E.C.1    Blattel, S.A.2    Mecham, R.P.3
  • 40
    • 67650480995 scopus 로고    scopus 로고
    • Transforming growth factor beta as a therapeutic target in systemic sclerosis
    • J. Varga, and B. Pasche Transforming growth factor beta as a therapeutic target in systemic sclerosis Nat. Rev. Rheumatol. 5 4 2009 200 206
    • (2009) Nat. Rev. Rheumatol. , vol.5 , Issue.4 , pp. 200-206
    • Varga, J.1    Pasche, B.2
  • 41
    • 25444501226 scopus 로고    scopus 로고
    • Involvement of alphavbeta5 integrin-mediated activation of latent transforming growth factor beta1 in autocrine transforming growth factor beta signaling in systemic sclerosis fibroblasts
    • Y. Asano, H. Ihn, K. Yamane, M. Jinnin, Y. Mimura, and K. Tamaki Involvement of alphavbeta5 integrin-mediated activation of latent transforming growth factor beta1 in autocrine transforming growth factor beta signaling in systemic sclerosis fibroblasts Arthritis Rheum. 52 9 2005 2897 2905
    • (2005) Arthritis Rheum. , vol.52 , Issue.9 , pp. 2897-2905
    • Asano, Y.1    Ihn, H.2    Yamane, K.3    Jinnin, M.4    Mimura, Y.5    Tamaki, K.6
  • 43
    • 28244449083 scopus 로고    scopus 로고
    • Increased expression of integrin alpha(v)beta3 contributes to the establishment of autocrine TGF-beta signaling in scleroderma fibroblasts
    • Y. Asano, H. Ihn, K. Yamane, M. Jinnin, Y. Mimura, and K. Tamaki Increased expression of integrin alpha(v)beta3 contributes to the establishment of autocrine TGF-beta signaling in scleroderma fibroblasts J. Immunol. 175 11 2005 7708 7718
    • (2005) J. Immunol. , vol.175 , Issue.11 , pp. 7708-7718
    • Asano, Y.1    Ihn, H.2    Yamane, K.3    Jinnin, M.4    Mimura, Y.5    Tamaki, K.6
  • 44
    • 73549107232 scopus 로고    scopus 로고
    • Activation, integrin-mediated transforming growth factor-β, a potential therapeutic target in fibrogenic disorders
    • S. Nishimura Activation, integrin-mediated transforming growth factor-β, a potential therapeutic target in fibrogenic disorders Am. J. Pathol. 175 4 2009 1362 1370
    • (2009) Am. J. Pathol. , vol.175 , Issue.4 , pp. 1362-1370
    • Nishimura, S.1
  • 45
    • 75949103899 scopus 로고    scopus 로고
    • Integrin-TGF-beta crosstalk in fibrosis, cancer and wound healing
    • C. Margadant, and A. Sonnenberg Integrin-TGF-beta crosstalk in fibrosis, cancer and wound healing EMBO Rep. 11 2 2010 97 105
    • (2010) EMBO Rep. , vol.11 , Issue.2 , pp. 97-105
    • Margadant, C.1    Sonnenberg, A.2
  • 46
    • 72149111953 scopus 로고    scopus 로고
    • The myofibroblast: Paradigm for a mechanically active cell
    • B. Hinz The myofibroblast: paradigm for a mechanically active cell J. Biomech. 43 1 2010 146 155
    • (2010) J. Biomech. , vol.43 , Issue.1 , pp. 146-155
    • Hinz, B.1
  • 47
    • 28444434653 scopus 로고    scopus 로고
    • Shared expression of phenotypic markers in systemic sclerosis indicates a convergence of pericytes and fibroblasts to a myofibroblast lineage in fibrosis
    • V.S. Rajkumar, K. Howell, K. Csiszar, C.P. Denton, C.M. Black, and D.J. Abraham Shared expression of phenotypic markers in systemic sclerosis indicates a convergence of pericytes and fibroblasts to a myofibroblast lineage in fibrosis Arthritis Res. Ther. 7 5 2005 R1113 R1123
    • (2005) Arthritis Res. Ther. , vol.7 , Issue.5
    • Rajkumar, V.S.1    Howell, K.2    Csiszar, K.3    Denton, C.P.4    Black, C.M.5    Abraham, D.J.6
  • 49
    • 79960101053 scopus 로고    scopus 로고
    • CCN2 is required for the TGF-β induced activation of Smad1-Erk1/2 signaling network
    • S.S. Nakerakanti, A.M. Bujor, and M. Trojanowska CCN2 is required for the TGF-β induced activation of Smad1-Erk1/2 signaling network PLoS ONE. 6 2011 e21911
    • (2011) PLoS ONE. , vol.6 , pp. 21911
    • Nakerakanti, S.S.1    Bujor, A.M.2    Trojanowska, M.3
  • 50
    • 0037358192 scopus 로고    scopus 로고
    • Integrin αvβ3, requirement for VEGFR2-mediated activation of SAPK2/p38 and for Hsp90-dependent phosphorylation of focal adhesion kinase in endothelial cells activated by VEGF
    • B. Masson-Gadais, F. Houle, J. Laferriere, and J. Huot Integrin αvβ3, requirement for VEGFR2-mediated activation of SAPK2/p38 and for Hsp90-dependent phosphorylation of focal adhesion kinase in endothelial cells activated by VEGF Cell Stress Chaperones. 8 2003 37 52
    • (2003) Cell Stress Chaperones. , vol.8 , pp. 37-52
    • Masson-Gadais, B.1    Houle, F.2    Laferriere, J.3    Huot, J.4
  • 52
    • 31444448603 scopus 로고    scopus 로고
    • Insulin-like growth factor-I signaling in smooth muscle cells is regulated by ligand binding to the sequence of the β3-subunit of αvβ3
    • L.A. Maile, W.H. Busby, K. Sitko, B.E. Capps, T. Sergent, J. Badley-Clarke, and D.R. Clemmons Insulin-like growth factor-I signaling in smooth muscle cells is regulated by ligand binding to the sequence of the β3-subunit of αvβ3 Mol. Endocrinol. 20 2006 405 413
    • (2006) Mol. Endocrinol. , vol.20 , pp. 405-413
    • Maile, L.A.1    Busby, W.H.2    Sitko, K.3    Capps, B.E.4    Sergent, T.5    Badley-Clarke, J.6    Clemmons, D.R.7
  • 53
    • 79960675151 scopus 로고    scopus 로고
    • Tenascin-C enhances crosstalk signaling of integrin αvβ3/ PDGFR-β complex by SRC recruitment promoting PDGF-induced proliferation and migration in smooth muscle cells
    • T. Ishigaki, K. Imanaka-Yoshida, N. Shimojo, S. Matsushima, W. Taki, and T. Yoshida Tenascin-C enhances crosstalk signaling of integrin αvβ3/PDGFR-β complex by SRC recruitment promoting PDGF-induced proliferation and migration in smooth muscle cells J. Cell Physiol. 226 10 2011 2617 2624
    • (2011) J. Cell Physiol. , vol.226 , Issue.10 , pp. 2617-2624
    • Ishigaki, T.1    Imanaka-Yoshida, K.2    Shimojo, N.3    Matsushima, S.4    Taki, W.5    Yoshida, T.6
  • 54
    • 3142706142 scopus 로고    scopus 로고
    • Competition for talin results in trans-dominant inhibition of integrin activation
    • D.A. Calderwood, V. Tai, G. Di Paolo, P. De Camilli, and M.H. Ginsberg Competition for talin results in trans-dominant inhibition of integrin activation J. Biol. Chem. 279 28 2004 28889 28895
    • (2004) J. Biol. Chem. , vol.279 , Issue.28 , pp. 28889-28895
    • Calderwood, D.A.1    Tai, V.2    Di Paolo, G.3    De Camilli, P.4    Ginsberg, M.H.5
  • 55
    • 57649136750 scopus 로고    scopus 로고
    • Integrin cross-talk in endothelial cells is regulated by protein kinase A and protein phosphatase 1
    • A.M. Gonzalez, J. Claiborne, and J.C. Jones Integrin cross-talk in endothelial cells is regulated by protein kinase A and protein phosphatase 1 J. Biol. Chem. 283 46 2008 31849 31860
    • (2008) J. Biol. Chem. , vol.283 , Issue.46 , pp. 31849-31860
    • Gonzalez, A.M.1    Claiborne, J.2    Jones, J.C.3
  • 56
    • 77957252478 scopus 로고    scopus 로고
    • Loss of beta1-integrin enhances TGF-beta1-induced collagen expression in epithelial cells via increased alphavbeta3-integrin and Rac1 activity
    • T. Hayashida, J.C. Jones, C.K. Lee, and H.W. Schnaper Loss of beta1-integrin enhances TGF-beta1-induced collagen expression in epithelial cells via increased alphavbeta3-integrin and Rac1 activity J. Biol. Chem. 285 40 2010 30741 30751
    • (2010) J. Biol. Chem. , vol.285 , Issue.40 , pp. 30741-30751
    • Hayashida, T.1    Jones, J.C.2    Lee, C.K.3    Schnaper, H.W.4
  • 57
    • 4444249880 scopus 로고    scopus 로고
    • Alpha(v)beta(3) integrin interacts with the transforming growth factor beta (TGFbeta) type II receptor to potentiate the proliferative effects of TGFbeta1 in living human lung fibroblasts
    • A.K. Scaffidi, N. Petrovic, Y.P. Moodley, M. Fogel-Petrovic, K.M. Kroeger, R.M. Seeber, K.A. Eidne, P.J. Thompson, and D.A. Knight Alpha(v)beta(3) integrin interacts with the transforming growth factor beta (TGFbeta) type II receptor to potentiate the proliferative effects of TGFbeta1 in living human lung fibroblasts J. Biol. Chem. 279 2004 37726 37733
    • (2004) J. Biol. Chem. , vol.279 , pp. 37726-37733
    • Scaffidi, A.K.1    Petrovic, N.2    Moodley, Y.P.3    Fogel-Petrovic, M.4    Kroeger, K.M.5    Seeber, R.M.6    Eidne, K.A.7    Thompson, P.J.8    Knight, D.A.9
  • 58
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • C.H. Streuli, and N. Akhtar Signal co-operation between integrins and other receptor systems Biochem. J. 418 3 2009 491 506
    • (2009) Biochem. J. , vol.418 , Issue.3 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 59
    • 82155188913 scopus 로고    scopus 로고
    • Fibronectin protects from excessive liver fibrosis by modulating the availability of and responsiveness of stellate cells to active TGF-β
    • N. Kawelke, M. Vasel, C. Sens, A. Au, S. Dooley, and I.A. Nakchbandi Fibronectin protects from excessive liver fibrosis by modulating the availability of and responsiveness of stellate cells to active TGF-β PLoS One. 6 11 2011 e28181
    • (2011) PLoS One. , vol.6 , Issue.11 , pp. 28181
    • Kawelke, N.1    Vasel, M.2    Sens, C.3    Au, A.4    Dooley, S.5    Nakchbandi, I.A.6
  • 62
    • 80052538877 scopus 로고    scopus 로고
    • Regulation of fibronectin-EDA through CTGF domain-specific interactions with TGFβ2 and its receptor TGFβRII
    • R. Khankan, N. Oliver, S. He, S.J. Ryan, and D.R. Hinton Regulation of fibronectin-EDA through CTGF domain-specific interactions with TGFβ2 and its receptor TGFβRII Invest. Ophthalmol. Vis. Sci. 52 8 2011 5068 5078
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , Issue.8 , pp. 5068-5078
    • Khankan, R.1    Oliver, N.2    He, S.3    Ryan, S.J.4    Hinton, D.R.5
  • 66
    • 79956330132 scopus 로고    scopus 로고
    • Lessons on the pathogenesis of aneurysm from heritable conditions
    • M.E. Lindsay, and H.C. Dietz Lessons on the pathogenesis of aneurysm from heritable conditions Nature. 473 7347 2011 308 316
    • (2011) Nature. , vol.473 , Issue.7347 , pp. 308-316
    • Lindsay, M.E.1    Dietz, H.C.2
  • 67
  • 68
    • 52049111663 scopus 로고    scopus 로고
    • TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta
    • M. Yamashita, K. Fatyol, C. Jin, X. Wang, Z. Liu, and Y.E. Zhang TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta Mol. Cell. 31 6 2008 918 924
    • (2008) Mol. Cell. , vol.31 , Issue.6 , pp. 918-924
    • Yamashita, M.1    Fatyol, K.2    Jin, C.3    Wang, X.4    Liu, Z.5    Zhang, Y.E.6
  • 72
    • 79955009402 scopus 로고    scopus 로고
    • SMAD4 mutation segregating in a family with juvenile polyposis, aortopathy, and mitral valve dysfunction
    • S. Andrabi, M.R. Bekheirnia, P. Robbins-Furman, R.A. Lewis, T.W. Prior, and L. Potocki SMAD4 mutation segregating in a family with juvenile polyposis, aortopathy, and mitral valve dysfunction Am. J. Med. Genet. A. 155A 5 2011 1165 1169
    • (2011) Am. J. Med. Genet. A. , vol.155 A , Issue.5 , pp. 1165-1169
    • Andrabi, S.1    Bekheirnia, M.R.2    Robbins-Furman, P.3    Lewis, R.A.4    Prior, T.W.5    Potocki, L.6
  • 74
    • 35948999623 scopus 로고    scopus 로고
    • Compound heterozygous mutations in fibulin-4 causing neonatal lethal pulmonary artery occlusion, aortic aneurysm, arachnodactyly, and mild cutis laxa
    • M. Dasouki, D. Markova, R. Garola, T. Sasaki, N.L. Charbonneau, L.Y. Sakai, and M.L. Chu Compound heterozygous mutations in fibulin-4 causing neonatal lethal pulmonary artery occlusion, aortic aneurysm, arachnodactyly, and mild cutis laxa Am. J. Med. Genet. A. 143A 22 2007 2635 2641
    • (2007) Am. J. Med. Genet. A. , vol.143 A , Issue.22 , pp. 2635-2641
    • Dasouki, M.1    Markova, D.2    Garola, R.3    Sasaki, T.4    Charbonneau, N.L.5    Sakai, L.Y.6    Chu, M.L.7
  • 75
    • 77649165897 scopus 로고    scopus 로고
    • Fibulin-4 deficiency results in ascending aortic aneurysms: A potential link between abnormal smooth muscle cell phenotype and aneurysm progression
    • J. Huang, E.C. Davis, S.L. Chapman, M. Budatha, L.Y. Marmorstein, R.A. Word, and H. Yanagisawa Fibulin-4 deficiency results in ascending aortic aneurysms: a potential link between abnormal smooth muscle cell phenotype and aneurysm progression Circ. Res. 106 3 2009 583 592
    • (2009) Circ. Res. , vol.106 , Issue.3 , pp. 583-592
    • Huang, J.1    Davis, E.C.2    Chapman, S.L.3    Budatha, M.4    Marmorstein, L.Y.5    Word, R.A.6    Yanagisawa, H.7
  • 79
    • 57749098804 scopus 로고    scopus 로고
    • Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity
    • P. Atsawasuwan, Y. Mochida, M. Katafuchi, M. Kaku, K.S. Fong, K. Csiszar, and M. Yamauchi Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity J. Biol. Chem. 283 49 2008 34229 34240
    • (2008) J. Biol. Chem. , vol.283 , Issue.49 , pp. 34229-34240
    • Atsawasuwan, P.1    Mochida, Y.2    Katafuchi, M.3    Kaku, M.4    Fong, K.S.5    Csiszar, K.6    Yamauchi, M.7
  • 81
    • 0036713792 scopus 로고    scopus 로고
    • Disruption of the gene encoding the latent transforming growth factor-beta binding protein 4 (LTBP-4) causes abnormal lung development, cardiomyopathy, and colorectal cancer
    • A. Sterner-Kock, I.S. Thorey, K. Koli, F. Wempe, J. Otte, T. Bangsow, K. Kuhlmeier, T. Kirchner, S. Jin, J. Keski-Oja, and H. von Melchner Disruption of the gene encoding the latent transforming growth factor-beta binding protein 4 (LTBP-4) causes abnormal lung development, cardiomyopathy, and colorectal cancer Genes Dev. 16 2002 2264 2273
    • (2002) Genes Dev. , vol.16 , pp. 2264-2273
    • Sterner-Kock, A.1    Thorey, I.S.2    Koli, K.3    Wempe, F.4    Otte, J.5    Bangsow, T.6    Kuhlmeier, K.7    Kirchner, T.8    Jin, S.9    Keski-Oja, J.10    Von Melchner, H.11
  • 84
    • 78650365007 scopus 로고    scopus 로고
    • Long form of latent TGF-β binding protein 1 (Ltbp1L) regulates cardiac valve development
    • V. Todorovic, E. Finnegan, L. Freyer, L. Zilberberg, M. Ota, and D.B. Rifkin Long form of latent TGF-β binding protein 1 (Ltbp1L) regulates cardiac valve development Dev. Dyn. 240 2011 176 187
    • (2011) Dev. Dyn. , vol.240 , pp. 176-187
    • Todorovic, V.1    Finnegan, E.2    Freyer, L.3    Zilberberg, L.4    Ota, M.5    Rifkin, D.B.6
  • 85
    • 70450253102 scopus 로고    scopus 로고
    • A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms
    • S. Apte A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms JBC. 284 2009 31493 31497
    • (2009) JBC. , vol.284 , pp. 31493-31497
    • Apte, S.1
  • 86
    • 80052927249 scopus 로고    scopus 로고
    • Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: A novel mechanism influencing microfibril assembly and function
    • D. Hubmacher, and S. Apte Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: a novel mechanism influencing microfibril assembly and function Cell. Mol. Life Sci. 68 2011 3137 3148
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 3137-3148
    • Hubmacher, D.1    Apte, S.2
  • 96
    • 0037712529 scopus 로고    scopus 로고
    • Large aneurysms of the ascending aorta and major coronary arteries in a patient with hereditary hemorrhagic telangiectasia
    • D.H. Hsi, G.F. Ryan, S.O. Hellems, D.C. Cheeran, and L.A. Sheils Large aneurysms of the ascending aorta and major coronary arteries in a patient with hereditary hemorrhagic telangiectasia Mayo Clin. Proc. 78 6 2003 774 776
    • (2003) Mayo Clin. Proc. , vol.78 , Issue.6 , pp. 774-776
    • Hsi, D.H.1    Ryan, G.F.2    Hellems, S.O.3    Cheeran, D.C.4    Sheils, L.A.5
  • 97
    • 75149123475 scopus 로고    scopus 로고
    • Thoracic endografting in a patient with hereditary hemorrhagic telangiectasia presenting with a descending thoracic aneurysm
    • N.D. Andersen, J. Dubose, A. Shah, T. Lee, S.B. Wechsler, and G.C. Hughes Thoracic endografting in a patient with hereditary hemorrhagic telangiectasia presenting with a descending thoracic aneurysm J. Vasc. Surg. 51 2 2010 468 470
    • (2010) J. Vasc. Surg. , vol.51 , Issue.2 , pp. 468-470
    • Andersen, N.D.1    Dubose, J.2    Shah, A.3    Lee, T.4    Wechsler, S.B.5    Hughes, G.C.6
  • 110
    • 21444434608 scopus 로고    scopus 로고
    • Fibronectin regulates latent transforming growth factor-beta (TGF beta) by controlling matrix assembly of latent TGF beta-binding protein-1
    • S.L. Dallas, P. Sivakumar, C.J. Jones, Q. Chen, D.M. Peters, D.F. Mosher, M.J. Humphries, and C.M. Kielty Fibronectin regulates latent transforming growth factor-beta (TGF beta) by controlling matrix assembly of latent TGF beta-binding protein-1 J. Biol. Chem. 280 19 2005 18871 18880
    • (2005) J. Biol. Chem. , vol.280 , Issue.19 , pp. 18871-18880
    • Dallas, S.L.1    Sivakumar, P.2    Jones, C.J.3    Chen, Q.4    Peters, D.M.5    Mosher, D.F.6    Humphries, M.J.7    Kielty, C.M.8
  • 111
    • 34548844181 scopus 로고    scopus 로고
    • Potential role for heparan sulfate proteoglycans in regulation of transforming growth factor-beta (TGF-beta) by modulating assembly of latent TGF-beta-binding protein-1
    • Q. Chen, P. Sivakumar, C. Barley, D.M. Peters, R.R. Gomes, M.C. Farach-Carson, and S.L. Dallas Potential role for heparan sulfate proteoglycans in regulation of transforming growth factor-beta (TGF-beta) by modulating assembly of latent TGF-beta-binding protein-1 J. Biol. Chem. 282 36 2007 26418 26430
    • (2007) J. Biol. Chem. , vol.282 , Issue.36 , pp. 26418-26430
    • Chen, Q.1    Sivakumar, P.2    Barley, C.3    Peters, D.M.4    Gomes, R.R.5    Farach-Carson, M.C.6    Dallas, S.L.7
  • 112
    • 70450187617 scopus 로고    scopus 로고
    • The regulation of TGFbeta signal transduction
    • A. Moustakas, and C.H. Heldin The regulation of TGFbeta signal transduction Development. 136 22 2009 3699 3714
    • (2009) Development. , vol.136 , Issue.22 , pp. 3699-3714
    • Moustakas, A.1    Heldin, C.H.2
  • 114
    • 34447549291 scopus 로고    scopus 로고
    • Filamin A-mediated down-regulation of the exchange factor Ras-GRF1 correlates with decreased matrix metalloproteinase-9 expression in human melanoma cells
    • T.N. Zhu, H.J. He, S. Kole, T. D'Souza, R. Agarwal, P.J. Morin, and M. Bernier Filamin A-mediated down-regulation of the exchange factor Ras-GRF1 correlates with decreased matrix metalloproteinase-9 expression in human melanoma cells J. Biol. Chem. 282 20 2007 14816 14826
    • (2007) J. Biol. Chem. , vol.282 , Issue.20 , pp. 14816-14826
    • Zhu, T.N.1    He, H.J.2    Kole, S.3    D'Souza, T.4    Agarwal, R.5    Morin, P.J.6    Bernier, M.7
  • 115
    • 0035947593 scopus 로고    scopus 로고
    • Filamin associates with Smads and regulates transforming growth factor-beta signaling
    • A. Sasaki, Y. Masuda, Y. Ohta, K. Ikeda, and K. Watanabe Filamin associates with Smads and regulates transforming growth factor-beta signaling J. Biol. Chem. 276 21 2001 17871 17877
    • (2001) J. Biol. Chem. , vol.276 , Issue.21 , pp. 17871-17877
    • Sasaki, A.1    Masuda, Y.2    Ohta, Y.3    Ikeda, K.4    Watanabe, K.5
  • 117
    • 65449146692 scopus 로고    scopus 로고
    • Absence of TGFbeta signaling in embryonic vascular smooth muscle leads to reduced lysyl oxidase expression, impaired elastogenesis, and aneurysm
    • B. Choudhary, J. Zhou, P. Li, S. Thomas, V. Kaartinen, and H.M. Sucov Absence of TGFbeta signaling in embryonic vascular smooth muscle leads to reduced lysyl oxidase expression, impaired elastogenesis, and aneurysm Genesis. 47 2 2009 115 121
    • (2009) Genesis. , vol.47 , Issue.2 , pp. 115-121
    • Choudhary, B.1    Zhou, J.2    Li, P.3    Thomas, S.4    Kaartinen, V.5    Sucov, H.M.6
  • 118
    • 78149464338 scopus 로고    scopus 로고
    • Conditional inactivation of TGF-β type II receptor in smooth muscle cells and epicardium causes lethal aortic and cardiac defects
    • D. Langlois, M. Hneino, L. Bouazza, A. Parlakian, T. Sasaki, G. Bricca, and J.Y. Li Conditional inactivation of TGF-β type II receptor in smooth muscle cells and epicardium causes lethal aortic and cardiac defects Transgenic Res. 19 6 2010 1069 1082
    • (2010) Transgenic Res. , vol.19 , Issue.6 , pp. 1069-1082
    • Langlois, D.1    Hneino, M.2    Bouazza, L.3    Parlakian, A.4    Sasaki, T.5    Bricca, G.6    Li, J.Y.7
  • 119
    • 18844387660 scopus 로고    scopus 로고
    • Angiotensin II activates the Smad pathway in vascular smooth muscle cells by a transforming growth factor-beta-independent mechanism
    • J. Rodríguez-Vita, E. Sánchez-López, V. Esteban, M. Rupérez, J. Egido, and M. Ruiz-Ortega Angiotensin II activates the Smad pathway in vascular smooth muscle cells by a transforming growth factor-beta-independent mechanism Circulation. 111 19 2005 2509 2517
    • (2005) Circulation. , vol.111 , Issue.19 , pp. 2509-2517
    • Rodríguez-Vita, J.1    Sánchez-López, E.2    Esteban, V.3    Rupérez, M.4    Egido, J.5    Ruiz-Ortega, M.6
  • 122
    • 76649100088 scopus 로고    scopus 로고
    • TGF-beta in the pathogenesis and prevention of disease: A matter of aneurysmic proportions
    • H.C. Dietz TGF-beta in the pathogenesis and prevention of disease: a matter of aneurysmic proportions J. Clin. Invest. 120 2 2010 403 407
    • (2010) J. Clin. Invest. , vol.120 , Issue.2 , pp. 403-407
    • Dietz, H.C.1
  • 123
    • 74749083638 scopus 로고    scopus 로고
    • Lysyl oxidase resolves inflammation by reducing monocyte chemoattractant protein-1 in abdominal aortic aneurysm
    • M. Onoda, K. Yoshimura, H. Aoki, Y. Ikeda, N. Morikage, A. Furutani, M. Matsuzaki, and K. Hamano Lysyl oxidase resolves inflammation by reducing monocyte chemoattractant protein-1 in abdominal aortic aneurysm Atherosclerosis. 208 2 2010 366 369
    • (2010) Atherosclerosis. , vol.208 , Issue.2 , pp. 366-369
    • Onoda, M.1    Yoshimura, K.2    Aoki, H.3    Ikeda, Y.4    Morikage, N.5    Furutani, A.6    Matsuzaki, M.7    Hamano, K.8
  • 125
    • 80052819014 scopus 로고    scopus 로고
    • Transforming growth factor (TGF)-β signaling in cardiac remodeling
    • M. Dobaczewski, W. Chen, and N.G. Frangogiannis Transforming growth factor (TGF)-β signaling in cardiac remodeling J. Mol. Cell Cardiol. 51 4 2011 600 606
    • (2011) J. Mol. Cell Cardiol. , vol.51 , Issue.4 , pp. 600-606
    • Dobaczewski, M.1    Chen, W.2    Frangogiannis, N.G.3
  • 127
    • 0033848657 scopus 로고    scopus 로고
    • Myocardial fibrosis in transforming growth factor beta 1 heterozygous mice
    • W.W. Brooks, and C.H. Conrad Myocardial fibrosis in transforming growth factor beta 1 heterozygous mice J. Mol. Cell Cardiol. 32 2 2000 187 195
    • (2000) J. Mol. Cell Cardiol. , vol.32 , Issue.2 , pp. 187-195
    • Brooks, W.W.1    Conrad, C.H.2
  • 129
    • 37549050584 scopus 로고    scopus 로고
    • Transforming growth factor-beta receptor antagonism attenuates myocardial fibrosis in mice with cardiac-restricted overexpression of tumor necrosis factor
    • Y. Sakata, A.L. Chancey, V.G. Divakaran, K. Sekiguchi, N. Sivasubramanian, and D.L. Mann Transforming growth factor-beta receptor antagonism attenuates myocardial fibrosis in mice with cardiac-restricted overexpression of tumor necrosis factor Basic Res. Cardiol. 103 1 2008 60 68
    • (2008) Basic Res. Cardiol. , vol.103 , Issue.1 , pp. 60-68
    • Sakata, Y.1    Chancey, A.L.2    Divakaran, V.G.3    Sekiguchi, K.4    Sivasubramanian, N.5    Mann, D.L.6
  • 130
    • 0036645337 scopus 로고    scopus 로고
    • Transforming growth factor-beta function blocking prevents myocardial fibrosis and diastolic dysfunction in pressure-overloaded rats
    • F. Kuwahara, H. Kai, K. Tokuda, M. Kai, A. Takeshita, K. Egashira, and T. Imaizumi Transforming growth factor-beta function blocking prevents myocardial fibrosis and diastolic dysfunction in pressure-overloaded rats Circulation 106 1 2002 130 135
    • (2002) Circulation , vol.106 , Issue.1 , pp. 130-135
    • Kuwahara, F.1    Kai, H.2    Tokuda, K.3    Kai, M.4    Takeshita, A.5    Egashira, K.6    Imaizumi, T.7
  • 133
    • 0037178816 scopus 로고    scopus 로고
    • Context-specific effects of fibulin-5 (DANCE/EVEC) on cell proliferation, motility, and invasion. Fibulin-5 is induced by transforming growth factor-beta and affects protein kinase cascades
    • W.P. Schiemann, G.C. Blobe, D.E. Kalume, A. Pandey, and H.F. Lodish Context-specific effects of fibulin-5 (DANCE/EVEC) on cell proliferation, motility, and invasion. Fibulin-5 is induced by transforming growth factor-beta and affects protein kinase cascades J. Biol. Chem. 277 2002 27367 27377
    • (2002) J. Biol. Chem. , vol.277 , pp. 27367-27377
    • Schiemann, W.P.1    Blobe, G.C.2    Kalume, D.E.3    Pandey, A.4    Lodish, H.F.5
  • 134
    • 3042742348 scopus 로고    scopus 로고
    • Fibulin-5 antagonizes vascular endothelial growth factor (VEGF) signaling and angiogenic sprouting by endothelial cells
    • A.R. Albig, and W.P. Schiemann Fibulin-5 antagonizes vascular endothelial growth factor (VEGF) signaling and angiogenic sprouting by endothelial cells DNA Cell Biol. 23 6 2004 367 379
    • (2004) DNA Cell Biol. , vol.23 , Issue.6 , pp. 367-379
    • Albig, A.R.1    Schiemann, W.P.2
  • 135
    • 57349137178 scopus 로고    scopus 로고
    • Fibulin-5 initiates epithelial-mesenchymal transition (EMT) and enhances EMT induced by TGF-beta in mammary epithelial cells via a MMP-dependent mechanism
    • Y.H. Lee, A.R. Albig, M. Regner, B.J. Schiemann, and W.P. Schiemann Fibulin-5 initiates epithelial-mesenchymal transition (EMT) and enhances EMT induced by TGF-beta in mammary epithelial cells via a MMP-dependent mechanism Carcinogenesis. 29 12 2008 2243 2251
    • (2008) Carcinogenesis. , vol.29 , Issue.12 , pp. 2243-2251
    • Lee, Y.H.1    Albig, A.R.2    Regner, M.3    Schiemann, B.J.4    Schiemann, W.P.5
  • 136
    • 84861032487 scopus 로고    scopus 로고
    • Overexpression of Fibulin-5 in Retinal Pigment Epithelial Cells Inhibits Cell Proliferation and Migration and Downregulates VEGF, CXCR4, and TGFB1 Expression in Cocultured Choroidal Endothelial Cells
    • [Epub ahead of print]
    • Li F., Xu H., Zeng Y., Yin Z.Q. (2012). Overexpression of Fibulin-5 in Retinal Pigment Epithelial Cells Inhibits Cell Proliferation and Migration and Downregulates VEGF, CXCR4, and TGFB1 Expression in Cocultured Choroidal Endothelial Cells. Curr. Eye Res. [Epub ahead of print].
    • (2012) Curr. Eye Res.
    • Li, F.1    Xu, H.2    Zeng, Y.3    Yin, Z.Q.4
  • 139
    • 80053137997 scopus 로고    scopus 로고
    • Mice lacking Nf1 in osteochondroprogenitor cells display skeletal dysplasia similar to patients with neurofibromatosis type i
    • W. Wang, J.S. Nyman, K. Ono, D.A. Stevenson, X. Yang, and F. Elefteriou Mice lacking Nf1 in osteochondroprogenitor cells display skeletal dysplasia similar to patients with neurofibromatosis type I Hum. Mol. Genet. 20 2011 3910 3924
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 3910-3924
    • Wang, W.1    Nyman, J.S.2    Ono, K.3    Stevenson, D.A.4    Yang, X.5    Elefteriou, F.6


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