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Volumn 184, Issue 5, 2014, Pages 1518-1528

Bortezomib partially improves laminin α2 chain-deficient muscular dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; LAMININ ALPHA2; MICRORNA; MICRORNA 1; MICRORNA 133A; PROTEASOME; UNCLASSIFIED DRUG; BORONIC ACID DERIVATIVE; LAMININ; PYRAZINE DERIVATIVE;

EID: 84899502670     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.1016/j.ajpath.2014.01.019     Document Type: Article
Times cited : (28)

References (66)
  • 1
    • 0036227621 scopus 로고    scopus 로고
    • Merosin-deficient muscular dystrophy, autosomal recessive (MDC1A, MIM#156225, LAMA2 gene coding for α2 chain of laminin)
    • V. Allamand, and P. Guicheney Merosin-deficient muscular dystrophy, autosomal recessive (MDC1A, MIM#156225, LAMA2 gene coding for α2 chain of laminin) Eur J Hum Genet 10 2002 91 94
    • (2002) Eur J Hum Genet , vol.10 , pp. 91-94
    • Allamand, V.1    Guicheney, P.2
  • 2
    • 23744477107 scopus 로고    scopus 로고
    • The congenital muscular dystrophies
    • ed 3 A.G. Angel, C. Franzini-Armstrong, McGraw-Hill New York
    • T. Voit, and F.M.S. Tomé The congenital muscular dystrophies ed 3 A.G. Angel, C. Franzini-Armstrong, Myology: Basic and Clinical vol 2 2004 McGraw-Hill New York 1203 1238
    • (2004) Myology: Basic and Clinical , vol.2 , pp. 1203-1238
    • Voit, T.1    Tomé, F.M.S.2
  • 3
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development
    • I. Leivo, and E. Engvall Merosin, a protein specific for basement membranes of Schwann cells, striated muscle, and trophoblast, is expressed late in nerve and muscle development Proc Natl Acad Sci USA 85 1988 1544 1588
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1544-1588
    • Leivo, I.1    Engvall, E.2
  • 4
    • 0028334735 scopus 로고
    • Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse
    • H. Xu, P. Christmas, X.R. Wu, U.M. Wewer, and E. Engvall Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse Proc Natl Acad Sci USA 91 1994 5572 5576
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5572-5576
    • Xu, H.1    Christmas, P.2    Wu, X.R.3    Wewer, U.M.4    Engvall, E.5
  • 7
    • 0033557707 scopus 로고    scopus 로고
    • Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins
    • J.F. Talts, Z. Andac, W. Gohring, A. Brancaccio, and R. Timpl Binding of the G domains of laminin α1 and α2 chains and perlecan to heparin, sulfatides, α-dystroglycan and several extracellular matrix proteins EMBO J 18 1999 863 870
    • (1999) EMBO J , vol.18 , pp. 863-870
    • Talts, J.F.1    Andac, Z.2    Gohring, W.3    Brancaccio, A.4    Timpl, R.5
  • 8
    • 0037155254 scopus 로고    scopus 로고
    • Alternative splice variants of α7β1 integrin selectively recognize different laminin isoforms
    • H. von der Mark, I. Williams, O. Wendler, L. Sorokin, K. von der Mark, and E. Pöschl Alternative splice variants of α7β1 integrin selectively recognize different laminin isoforms J Biol Chem 277 2002 6012 6016
    • (2002) J Biol Chem , vol.277 , pp. 6012-6016
    • Von Der Mark, H.1    Williams, I.2    Wendler, O.3    Sorokin, L.4    Von Der Mark, K.5    Pöschl, E.6
  • 9
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • J.M. Ervasti, and K.P. Campbell A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin J Cell Biol 122 1993 809 823
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 11
    • 0030610576 scopus 로고    scopus 로고
    • Integrins (α7β1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy
    • P.H. Vachon, H. Xu, L. Liu, F. Loechel, Y. Hayashi, K. Arahata, J.C. Reed, U.M. Wewer, and E. Engvall Integrins (α7β1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy J Clin Invest 10 1997 1870 1881
    • (1997) J Clin Invest , vol.10 , pp. 1870-1881
    • Vachon, P.H.1    Xu, H.2    Liu, L.3    Loechel, F.4    Hayashi, Y.5    Arahata, K.6    Reed, J.C.7    Wewer, U.M.8    Engvall, E.9
  • 13
    • 33644892480 scopus 로고    scopus 로고
    • Laminin α1 chain mediated reduction of laminin α2 chain deficient muscular dystrophy involves integrin α7β1 and dystroglycan
    • K.I. Gawlik, U. Mayer, K. Blomberg, A. Sonnenberg, P. Ekblom, and M. Durbeej Laminin α1 chain mediated reduction of laminin α2 chain deficient muscular dystrophy involves integrin α7β1 and dystroglycan FEBS Lett 580 2006 1759 1765
    • (2006) FEBS Lett , vol.580 , pp. 1759-1765
    • Gawlik, K.I.1    Mayer, U.2    Blomberg, K.3    Sonnenberg, A.4    Ekblom, P.5    Durbeej, M.6
  • 14
    • 0033391990 scopus 로고    scopus 로고
    • Activation of the Lama2 gene in muscle regeneration: Abortive regeneration in laminin α2-deficiency
    • W. Kuang, H. Xu, J.T. Vilquin, and E. Engvall Activation of the Lama2 gene in muscle regeneration: abortive regeneration in laminin α2-deficiency Lab Invest 79 1999 1601 1613
    • (1999) Lab Invest , vol.79 , pp. 1601-1613
    • Kuang, W.1    Xu, H.2    Vilquin, J.T.3    Engvall, E.4
  • 16
    • 84863251717 scopus 로고    scopus 로고
    • Skeletal muscle laminin and MDC1A: Pathogenesis and treatment strategies
    • K.I. Gawlik, and M. Durbeej Skeletal muscle laminin and MDC1A: pathogenesis and treatment strategies Skelet Muscle 1 2011 9
    • (2011) Skelet Muscle , vol.1 , pp. 9
    • Gawlik, K.I.1    Durbeej, M.2
  • 17
    • 0030610896 scopus 로고    scopus 로고
    • Laminin α2 chain-null mutant mice by targeted disruption of the Lama2 gene: A new model of merosin (laminin 2)-deficient congenital muscular dystrophy
    • Y. Miyagoe, K. Hanaoka, I. Nonaka, M. Hayasaka, Y. Nabeshima, K. Arahata, Y. Nabeshima, and S. Takeda Laminin α2 chain-null mutant mice by targeted disruption of the Lama2 gene: a new model of merosin (laminin 2)-deficient congenital muscular dystrophy FEBS Lett 415 1997 33 39
    • (1997) FEBS Lett , vol.415 , pp. 33-39
    • Miyagoe, Y.1    Hanaoka, K.2    Nonaka, I.3    Hayasaka, M.4    Nabeshima, Y.5    Arahata, K.6    Nabeshima, Y.7    Takeda, S.8
  • 19
    • 4444354572 scopus 로고    scopus 로고
    • Laminin α1 chain reduces muscular dystrophy in laminin α2 chain deficient mice
    • K. Gawlik, Y. Miyagoe-Suzuki, P. Ekblom, S. Takeda, and M. Durbeej Laminin α1 chain reduces muscular dystrophy in laminin α2 chain deficient mice Hum Mol Genet 13 2004 1775 1784
    • (2004) Hum Mol Genet , vol.13 , pp. 1775-1784
    • Gawlik, K.1    Miyagoe-Suzuki, Y.2    Ekblom, P.3    Takeda, S.4    Durbeej, M.5
  • 20
    • 33748750613 scopus 로고    scopus 로고
    • Laminin α1 chain improves laminin α2 chain deficient neuropathy
    • K.I. Gawlik, J.Y. Li, Å. Petersén, and M. Durbeej Laminin α1 chain improves laminin α2 chain deficient neuropathy Hum Mol Genet 15 2006 2690 2700
    • (2006) Hum Mol Genet , vol.15 , pp. 2690-2700
    • Gawlik, K.I.1    Li, J.Y.2    Petersén, Å.3    Durbeej, M.4
  • 21
    • 77955394628 scopus 로고    scopus 로고
    • Distinct roles for laminin globular domains in laminin α1 chain mediated rescue of murine laminin α2 chain deficiency
    • K.I. Gawlik, M. Åkerlund, V. Carmignac, H. Elamaa, and M. Durbeej Distinct roles for laminin globular domains in laminin α1 chain mediated rescue of murine laminin α2 chain deficiency PLoS One 5 2010 e11549
    • (2010) PLoS One , vol.5 , pp. 11549
    • Gawlik, K.I.1    Åkerlund, M.2    Carmignac, V.3    Elamaa, H.4    Durbeej, M.5
  • 22
    • 77954104087 scopus 로고    scopus 로고
    • Transgenic overexpression of laminin α1 chain in laminin α2 chain-deficient mice rescues the disease throughout the lifespan
    • K.I. Gawlik, and M. Durbeej Transgenic overexpression of laminin α1 chain in laminin α2 chain-deficient mice rescues the disease throughout the lifespan Muscle Nerve 42 2010 30 37
    • (2010) Muscle Nerve , vol.42 , pp. 30-37
    • Gawlik, K.I.1    Durbeej, M.2
  • 23
    • 0032528845 scopus 로고    scopus 로고
    • Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models [Erratum appeared in J Clin Invest 1998, 102(6):following 1275]
    • W. Kuang, H. Xu, P.H. Vachon, and E. Engvall Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models [Erratum appeared in J Clin Invest 1998, 102(6):following 1275] J Clin Invest 102 1998 844 852
    • (1998) J Clin Invest , vol.102 , pp. 844-852
    • Kuang, W.1    Xu, H.2    Vachon, P.H.3    Engvall, E.4
  • 24
    • 20444434366 scopus 로고    scopus 로고
    • Overexpression of mini-agrin in skeletal muscle increases muscle integrity and regenerative capacity in laminin-α2-deficient mice
    • C.F. Bentzinger, P. Barzaghi, S. Lin, and M.A. Rüegg Overexpression of mini-agrin in skeletal muscle increases muscle integrity and regenerative capacity in laminin-α2-deficient mice FASEB J 19 2005 934 942
    • (2005) FASEB J , vol.19 , pp. 934-942
    • Bentzinger, C.F.1    Barzaghi, P.2    Lin, S.3    Rüegg, M.A.4
  • 25
    • 33947721728 scopus 로고    scopus 로고
    • Linker molecules between laminins and dystroglycan ameliorate laminin-α2-deficient muscular dystrophy at all disease stages
    • S. Meinen, P. Barzaghi, S. Lin, H. Lochmüller, and M.A. Rüegg Linker molecules between laminins and dystroglycan ameliorate laminin-α2-deficient muscular dystrophy at all disease stages J Cell Biol 176 2007 979 993
    • (2007) J Cell Biol , vol.176 , pp. 979-993
    • Meinen, S.1    Barzaghi, P.2    Lin, S.3    Lochmüller, H.4    Rüegg, M.A.5
  • 26
    • 79960289893 scopus 로고    scopus 로고
    • Transgenic overexpression of the α7 integrin reduces muscle pathology and improves viability in the dy(W) mouse model of merosin-deficient congenital muscular dystrophy type 1A
    • J.A. Doe, R.D. Wuebbles, E.T. Allred, J.E. Rooney, M. Elorza, and D.J. Burkin Transgenic overexpression of the α7 integrin reduces muscle pathology and improves viability in the dy(W) mouse model of merosin-deficient congenital muscular dystrophy type 1A J Cell Sci 124 2011 2287 2297
    • (2011) J Cell Sci , vol.124 , pp. 2287-2297
    • Doe, J.A.1    Wuebbles, R.D.2    Allred, E.T.3    Rooney, J.E.4    Elorza, M.5    Burkin, D.J.6
  • 27
    • 85047693919 scopus 로고    scopus 로고
    • Inhibition of apoptosis improves outcome in a model of congenital muscular dystrophy
    • M. Girgenrath, J.A. Dominov, C.A. Kostek, and J.B. Miller Inhibition of apoptosis improves outcome in a model of congenital muscular dystrophy J Clin Invest 114 2004 1635 1639
    • (2004) J Clin Invest , vol.114 , pp. 1635-1639
    • Girgenrath, M.1    Dominov, J.A.2    Kostek, C.A.3    Miller, J.B.4
  • 28
    • 79957521292 scopus 로고    scopus 로고
    • Muscle-specific expression of insulin-like growth factor 1 improves outcome in Lama2Dy-w mice, a model for congenital muscular dystrophy type 1A
    • A. Kumar, J. Yamauchi, T. Girgenrath, and M. Girgenrath Muscle-specific expression of insulin-like growth factor 1 improves outcome in Lama2Dy-w mice, a model for congenital muscular dystrophy type 1A Hum Mol Genet 20 2011 2333 2343
    • (2011) Hum Mol Genet , vol.20 , pp. 2333-2343
    • Kumar, A.1    Yamauchi, J.2    Girgenrath, T.3    Girgenrath, M.4
  • 30
    • 60849118087 scopus 로고    scopus 로고
    • Pathology is alleviated by doxycycline in a laminin-α2-null model of congenital muscular dystrophy
    • M. Girgenrath, M.L. Beermann, V.K. Vishnudas, S. Homma, and J.B. Miller Pathology is alleviated by doxycycline in a laminin-α2-null model of congenital muscular dystrophy Ann Neurol 65 2009 47 56
    • (2009) Ann Neurol , vol.65 , pp. 47-56
    • Girgenrath, M.1    Beermann, M.L.2    Vishnudas, V.K.3    Homma, S.4    Miller, J.B.5
  • 32
    • 84874716506 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor antagonists alleviate muscle pathology in the mouse model for laminin-α2-deficient congenital muscular dystrophy (MDC1A)
    • S. Meinen, S. Lin, and M.A. Rüegg Angiotensin II type 1 receptor antagonists alleviate muscle pathology in the mouse model for laminin-α2-deficient congenital muscular dystrophy (MDC1A) Skelet Muscle 2 2012 18
    • (2012) Skelet Muscle , vol.2 , pp. 18
    • Meinen, S.1    Lin, S.2    Rüegg, M.A.3
  • 33
    • 84859075862 scopus 로고    scopus 로고
    • Laminin-111 protein therapy reduces muscle pathology and improves viability of a mouse model of merosin-deficient congenital muscular dystrophy
    • J.E. Rooney, J.R. Knapp, B.L. Hodges, R.D. Wuebbles, and D.J. Burkin Laminin-111 protein therapy reduces muscle pathology and improves viability of a mouse model of merosin-deficient congenital muscular dystrophy Am J Pathol 180 2012 1593 1602
    • (2012) Am J Pathol , vol.180 , pp. 1593-1602
    • Rooney, J.E.1    Knapp, J.R.2    Hodges, B.L.3    Wuebbles, R.D.4    Burkin, D.J.5
  • 34
    • 78651076693 scopus 로고    scopus 로고
    • Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice
    • V. Carmignac, R. Quéré, and M. Durbeej Proteasome inhibition improves the muscle of laminin α2 chain-deficient mice Hum Mol Genet 20 2011 541 552
    • (2011) Hum Mol Genet , vol.20 , pp. 541-552
    • Carmignac, V.1    Quéré, R.2    Durbeej, M.3
  • 35
    • 81855205301 scopus 로고    scopus 로고
    • Autophagy is increased in laminin α2 chain-deficient muscle and inhibition improves muscle morphology in a mouse model of MDC1A
    • V. Carmignac, M. Svensson, Z. Körner, L. Elowsson, C. Matsumura, K. Gawlik, V. Allamand, and M. Durbeej Autophagy is increased in laminin α2 chain-deficient muscle and inhibition improves muscle morphology in a mouse model of MDC1A Hum Mol Genet 20 2011 4891 4902
    • (2011) Hum Mol Genet , vol.20 , pp. 4891-4902
    • Carmignac, V.1    Svensson, M.2    Körner, Z.3    Elowsson, L.4    Matsumura, C.5    Gawlik, K.6    Allamand, V.7    Durbeej, M.8
  • 36
    • 84871940845 scopus 로고    scopus 로고
    • Development of proteasome inhibitors as research tools and cancer drugs
    • A.L. Goldberg Development of proteasome inhibitors as research tools and cancer drugs J Cell Biol 199 2012 583 588
    • (2012) J Cell Biol , vol.199 , pp. 583-588
    • Goldberg, A.L.1
  • 41
    • 77957273064 scopus 로고    scopus 로고
    • A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor κb pathway in skeletal muscle
    • L. Laure, N. Danièle, L. Suel, S. Marchand, S. Aubert, N. Bourg, C. Roudauc, S. Dugez, M. Bartoli, and I. Richard A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor κB pathway in skeletal muscle FEBS J 277 2010 4322 4337
    • (2010) FEBS J , vol.277 , pp. 4322-4337
    • Laure, L.1    Danièle, N.2    Suel, L.3    Marchand, S.4    Aubert, S.5    Bourg, N.6    Roudauc, C.7    Dugez, S.8    Bartoli, M.9    Richard, I.10
  • 43
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • J. Vandesompele, K. De Preter, F. Pattyn, B. Poppe, N. Van Roy, A. De Paepe, and F. Speleman Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes Genome Biol 3 2002 RESEARCH0034
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 44
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • M.W. Pfaffl, G.W. Horgan, and L. Dempfle Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR Nucleic Acids Res 30 2002 e36
    • (2002) Nucleic Acids Res , vol.30 , pp. 36
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 45
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene
    • H. Xu, X.R. Wu, U.M. Wewer, and E. Engvall Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene Nat Genet 8 1994 297 302
    • (1994) Nat Genet , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.R.2    Wewer, U.M.3    Engvall, E.4
  • 46
    • 0029024847 scopus 로고
    • Identification of a novel mutant transcript of laminin α2 chain gene responsible for muscular dystrophy and dysmyelination in dy2J mice
    • Y. Sunada, S.M. Bernier, A. Utani, Y. Yamada, and K.P. Campbell Identification of a novel mutant transcript of laminin α2 chain gene responsible for muscular dystrophy and dysmyelination in dy2J mice Hum Mol Genet 4 1995 1055 1061
    • (1995) Hum Mol Genet , vol.4 , pp. 1055-1061
    • Sunada, Y.1    Bernier, S.M.2    Utani, A.3    Yamada, Y.4    Campbell, K.P.5
  • 49
    • 33344460712 scopus 로고    scopus 로고
    • Expression profiling of muscles from Fukuyama-type congenital muscular dystrophy and laminin α2 deficient congenital muscular dystrophy; Is congenital muscular dystrophy a primary fibrotic disease?
    • M. Taniguchi, H. Kurahashi, S. Noguchi, J. Sese, T. Okinaga, T. Tsukahara, P. Guicheney, K. Ozono, I. Nishino, S. Morishita, and T. Toda Expression profiling of muscles from Fukuyama-type congenital muscular dystrophy and laminin α2 deficient congenital muscular dystrophy; is congenital muscular dystrophy a primary fibrotic disease? Biochem Biophys Res Commun 342 2006 489 502
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 489-502
    • Taniguchi, M.1    Kurahashi, H.2    Noguchi, S.3    Sese, J.4    Okinaga, T.5    Tsukahara, T.6    Guicheney, P.7    Ozono, K.8    Nishino, I.9    Morishita, S.10    Toda, T.11
  • 53
    • 79960955062 scopus 로고    scopus 로고
    • Apoptosis inhibitors and mini-agrin have additive benefits in congenital muscular dystrophy mice
    • S. Meinen, S. Lin, R. Thurnherr, M. Erb, T. Meier, and M.A. Rüegg Apoptosis inhibitors and mini-agrin have additive benefits in congenital muscular dystrophy mice EMBO Mol Med 3 2011 465 479
    • (2011) EMBO Mol Med , vol.3 , pp. 465-479
    • Meinen, S.1    Lin, S.2    Thurnherr, R.3    Erb, M.4    Meier, T.5    Rüegg, M.A.6
  • 54
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • J.B. Almond, and G.M. Cohen The proteasome: a novel target for cancer chemotherapy Leukemia 16 2002 433 443
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 55
    • 35348988646 scopus 로고    scopus 로고
    • Managing and avoiding bortezomib toxicity
    • J. Menashe Managing and avoiding bortezomib toxicity Community Oncol 4 2007 480 484
    • (2007) Community Oncol , vol.4 , pp. 480-484
    • Menashe, J.1
  • 58
    • 84894126274 scopus 로고    scopus 로고
    • Loss of dystrophin and β-sarcoglycan significantly exacerbates the phenotype of laminin α2 chain-deficient animals
    • K.I. Gawlik, J. Holmberg, and M. Durbeej Loss of dystrophin and β-sarcoglycan significantly exacerbates the phenotype of laminin α2 chain-deficient animals Am J Pathol 184 2014 740 752
    • (2014) Am J Pathol , vol.184 , pp. 740-752
    • Gawlik, K.I.1    Holmberg, J.2    Durbeej, M.3
  • 60
    • 0141760313 scopus 로고    scopus 로고
    • Proteasome inhibitor (MG-132) treatment of mdx mice rescues the expression and membrane localization of dystrophin and dystrophin-associated proteins
    • G. Bonuccelli, F. Sotgia, W. Schubert, D.S. Park, P.G. Frank, S.E. Woodman, L. Insabato, M. Cammer, C. Minetti, and M.P. Lisanti Proteasome inhibitor (MG-132) treatment of mdx mice rescues the expression and membrane localization of dystrophin and dystrophin-associated proteins Am J Pathol 163 2003 1663 1675
    • (2003) Am J Pathol , vol.163 , pp. 1663-1675
    • Bonuccelli, G.1    Sotgia, F.2    Schubert, W.3    Park, D.S.4    Frank, P.G.5    Woodman, S.E.6    Insabato, L.7    Cammer, M.8    Minetti, C.9    Lisanti, M.P.10
  • 62
    • 34548266210 scopus 로고    scopus 로고
    • Localized treatment with a novel FDA-approved proteasome inhibitor blocks the degradation of dystrophin and dystrophin-associated proteins in mdx mice
    • G. Bonuccelli, F. Sotgia, F. Capozza, E. Gazzerro, C. Minetti, and M.P. Lisanti Localized treatment with a novel FDA-approved proteasome inhibitor blocks the degradation of dystrophin and dystrophin-associated proteins in mdx mice Cell Cycle 6 2007 1242 1248
    • (2007) Cell Cycle , vol.6 , pp. 1242-1248
    • Bonuccelli, G.1    Sotgia, F.2    Capozza, F.3    Gazzerro, E.4    Minetti, C.5    Lisanti, M.P.6
  • 63
    • 84867444389 scopus 로고    scopus 로고
    • A proteasome inhibitor fails to attenuate dystrophic pathology in mdx mice
    • e4f84a944d8930
    • J. Selzby, C. Morris, L. Morris, and L. Sweeney A proteasome inhibitor fails to attenuate dystrophic pathology in mdx mice PLoS Curr 4 2012 e4f84a944d8930
    • (2012) PLoS Curr , vol.4
    • Selzby, J.1    Morris, C.2    Morris, L.3    Sweeney, L.4
  • 64
    • 84858965806 scopus 로고    scopus 로고
    • Proteasomal inhibition restores biological function of mis-sense mutated dysferlin in patient-derived muscle cells
    • B.A. Azakir, S. Di Fulvio, J. Kinter, and M. Sinnreich Proteasomal inhibition restores biological function of mis-sense mutated dysferlin in patient-derived muscle cells J Biol Chem 287 2012 10344 10354
    • (2012) J Biol Chem , vol.287 , pp. 10344-10354
    • Azakir, B.A.1    Di Fulvio, S.2    Kinter, J.3    Sinnreich, M.4
  • 65
    • 43949109275 scopus 로고    scopus 로고
    • Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle
    • C. Mammucari, S. Schiaffino, and M. Sandri Downstream of Akt: FoxO3 and mTOR in the regulation of autophagy in skeletal muscle Autophagy 4 2008 524 526
    • (2008) Autophagy , vol.4 , pp. 524-526
    • Mammucari, C.1    Schiaffino, S.2    Sandri, M.3
  • 66
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle
    • K.J. Langenbach, and T.A. Rando Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle Muscle Nerve 26 2002 644 653
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.