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Volumn 5 FEB, Issue , 2014, Pages

Genetic silencing of Nrf2 enhances X-ROS in dysferlin-deficient muscle

Author keywords

Dysferlin; Dystrophy; Nrf2; ROS; X ROS

Indexed keywords

DYSFERLIN; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 2; TRANSCRIPTION FACTOR NRF2;

EID: 84895505670     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00057     Document Type: Article
Times cited : (24)

References (48)
  • 1
    • 79954484329 scopus 로고    scopus 로고
    • Dysferlinopathies
    • doi: 10.1016/B978-0-08-045031-5.00007-4
    • Amato, A. A., and Brown, R. H. Jr. (2011). Dysferlinopathies. Handb. Clin. Neurol. 101, 111-118. doi: 10.1016/B978-0-08-045031-5.00007-4.
    • (2011) Handb. Clin. Neurol. , vol.101 , pp. 111-118
    • Amato, A.A.1    Brown Jr., R.H.2
  • 2
    • 77949457256 scopus 로고    scopus 로고
    • The clinical course of calpainopathy (LGMD2A) and dysferlinopathy (LGMD2B)
    • doi: 10.1179/174313209X380847
    • Angelini, C., Nardetto, L., Borsato, C., Padoan, R., Fanin, M., Nascimbeni, A. C., et al. (2010). The clinical course of calpainopathy (LGMD2A) and dysferlinopathy (LGMD2B). Neurol. Res. 32, 41-46. doi: 10.1179/174313209X380847.
    • (2010) Neurol. Res. , vol.32 , pp. 41-46
    • Angelini, C.1    Nardetto, L.2    Borsato, C.3    Padoan, R.4    Fanin, M.5    Nascimbeni, A.C.6
  • 3
    • 81455134409 scopus 로고    scopus 로고
    • Dysferlinopathy course and sportive activity: clues for possible treatment
    • Angelini, C., Peterle, E., Gaiani, A., Bortolussi, L., and Borsato, C. (2011). Dysferlinopathy course and sportive activity: clues for possible treatment. Acta Myol. 30, 127-132. Available online at: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3235880/.
    • (2011) Acta Myol. , vol.30 , pp. 127-132
    • Angelini, C.1    Peterle, E.2    Gaiani, A.3    Bortolussi, L.4    Borsato, C.5
  • 4
    • 1842556210 scopus 로고    scopus 로고
    • Dysferlin and the plasma membrane repair in muscular dystrophy
    • doi: 10.1016/j.tcb.2004.03.001
    • Bansal, D., and Campbell, K. P. (2004). Dysferlin and the plasma membrane repair in muscular dystrophy. Trends Cell Biol. 14, 206-213. doi: 10.1016/j.tcb.2004.03.001.
    • (2004) Trends Cell Biol. , vol.14 , pp. 206-213
    • Bansal, D.1    Campbell, K.P.2
  • 5
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • doi: 10.1038/nature01573
    • Bansal, D., Miyake, K., Vogel, S. S., Groh, S., Chen, C. C., Williamson, R., et al. (2003). Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 423, 168-172. doi: 10.1038/nature01573.
    • (2003) Nature , vol.423 , pp. 168-172
    • Bansal, D.1    Miyake, K.2    Vogel, S.S.3    Groh, S.4    Chen, C.C.5    Williamson, R.6
  • 6
    • 77951642473 scopus 로고    scopus 로고
    • Deletion of Keap1 in the lung attenuates acute cigarette smoke-induced oxidative stress and inflammation
    • doi: 10.1165/rcmb.2009-0054OC
    • Blake, D., Singh, A., Kombairaju, P., Malhotra, D., Mariani, T., Tuder, R., et al. (2010). Deletion of Keap1 in the lung attenuates acute cigarette smoke-induced oxidative stress and inflammation. Am. J. Respir. Cell Mol. Biol. 42, 524-536. doi: 10.1165/rcmb.2009-0054OC.
    • (2010) Am. J. Respir. Cell Mol. Biol. , vol.42 , pp. 524-536
    • Blake, D.1    Singh, A.2    Kombairaju, P.3    Malhotra, D.4    Mariani, T.5    Tuder, R.6
  • 7
    • 80052033151 scopus 로고    scopus 로고
    • Muscular dystrophy with marked Dysferlin deficiency is consistently caused by primary dysferlin gene mutations
    • doi: 10.1038/ejhg.2011.70
    • Cacciottolo, M., Numitone, G., Aurino, S., Caserta, I. R., Fanin, M., Politano, L., et al. (2011). Muscular dystrophy with marked Dysferlin deficiency is consistently caused by primary dysferlin gene mutations. Eur. J. Hum. Genet. 19, 974-980. doi: 10.1038/ejhg.2011.70.
    • (2011) Eur. J. Hum. Genet. , vol.19 , pp. 974-980
    • Cacciottolo, M.1    Numitone, G.2    Aurino, S.3    Caserta, I.R.4    Fanin, M.5    Politano, L.6
  • 8
    • 9444249870 scopus 로고    scopus 로고
    • The transcription factor Nrf2 protects against pulmonary fibrosis
    • doi: 10.1096/fj.03-1127fje
    • Cho, H. Y., Reddy, S. P., Yamamoto, M., and Kleeberger, S. R. (2004). The transcription factor Nrf2 protects against pulmonary fibrosis. FASEB J. 18, 1258-1260. doi: 10.1096/fj.03-1127fje.
    • (2004) FASEB J. , vol.18 , pp. 1258-1260
    • Cho, H.Y.1    Reddy, S.P.2    Yamamoto, M.3    Kleeberger, S.R.4
  • 9
    • 77953142289 scopus 로고    scopus 로고
    • Membrane wounding triggers ATP release and dysferlin-mediated intercellular calcium signaling
    • doi: 10.1242/jcs.066084
    • Covian-Nares, J. F., Koushik, S. V., Puhl, H. L. III., and Vogel, S. S. (2010). Membrane wounding triggers ATP release and dysferlin-mediated intercellular calcium signaling. J. Cell Sci. 123, 1884-1893. doi: 10.1242/jcs.066084.
    • (2010) J. Cell Sci. , vol.123 , pp. 1884-1893
    • Covian-Nares, J.F.1    Koushik, S.V.2    Puhl III, H.L.3    Vogel, S.S.4
  • 11
    • 82955207160 scopus 로고    scopus 로고
    • Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation
    • doi: 10.1371/journal.pone.0028563
    • Di Fulvio, S., Azakir, B. A., Therrien, C., and Sinnreich, M. (2011). Dysferlin interacts with histone deacetylase 6 and increases alpha-tubulin acetylation. PLoS One 6:e28563. doi: 10.1371/journal.pone.0028563.
    • (2011) PLoS One , vol.6
    • Di Fulvio, S.1    Azakir, B.A.2    Therrien, C.3    Sinnreich, M.4
  • 13
    • 79959203801 scopus 로고    scopus 로고
    • Dysferlinopathy: spectrum of pathological changes in skeletal muscle tissue
    • doi: 10.4103/0377-4929.81636
    • Gayathri, N., Alefia, R., Nalini, A., Yasha, T. C., Anita, M., Santosh, V., et al. (2011). Dysferlinopathy: spectrum of pathological changes in skeletal muscle tissue. Indian J. Pathol. Microbiol. 54, 350-354. doi: 10.4103/0377-4929.81636.
    • (2011) Indian J. Pathol. Microbiol. , vol.54 , pp. 350-354
    • Gayathri, N.1    Alefia, R.2    Nalini, A.3    Yasha, T.C.4    Anita, M.5    Santosh, V.6
  • 15
    • 79956095344 scopus 로고    scopus 로고
    • Growing muscle has different sarcolemmal properties from adult muscle: a proposal with scientific and clinical implications: reasons to reassess skeletal muscle molecular dynamics, cellular responses and suitability of experimental models of muscle disord
    • doi: 10.1002/bies.201000136
    • Grounds, M. D., and Shavlakadze, T. (2011). Growing muscle has different sarcolemmal properties from adult muscle: a proposal with scientific and clinical implications: reasons to reassess skeletal muscle molecular dynamics, cellular responses and suitability of experimental models of muscle disord. Bioessays 33, 458-468. doi: 10.1002/bies.201000136.
    • (2011) Bioessays , vol.33 , pp. 458-468
    • Grounds, M.D.1    Shavlakadze, T.2
  • 16
    • 0034719093 scopus 로고    scopus 로고
    • Identical dysferlin mutation in limb-girdle muscular dystrophy type 2B and distal myopathy
    • doi: 10.1212/WNL.55.12.1931
    • Illarioshkin, S. N., Ivanova-Smolenskaya, I. A., Greenberg, C. R., Nylen, E., Sukhorukov, V. S., Poleshchuk, V. V., et al. (2000). Identical dysferlin mutation in limb-girdle muscular dystrophy type 2B and distal myopathy. Neurology 55, 1931-1933. doi: 10.1212/WNL.55.12.1931.
    • (2000) Neurology , vol.55 , pp. 1931-1933
    • Illarioshkin, S.N.1    Ivanova-Smolenskaya, I.A.2    Greenberg, C.R.3    Nylen, E.4    Sukhorukov, V.S.5    Poleshchuk, V.V.6
  • 17
    • 84890831113 scopus 로고    scopus 로고
    • Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane
    • doi: 10.1073/pnas.1307960110
    • Kerr, J. P., Ziman, A. P., Mueller, A. L., Muriel, J. M., Kleinhans-Welte, E., Gumerson, J. D., et al. (2013). Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane. Proc. Natl. Acad. Sci. U.S.A. 110, 20831-20836. doi: 10.1073/pnas.1307960110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 20831-20836
    • Kerr, J.P.1    Ziman, A.P.2    Mueller, A.L.3    Muriel, J.M.4    Kleinhans-Welte, E.5    Gumerson, J.D.6
  • 18
    • 84864876833 scopus 로고    scopus 로고
    • Microtubules underlie dysfunction in Duchenne muscular dystrophy
    • doi: 10.1126/scisignal.2002829
    • Khairallah, R. J., Shi, G., Sbrana, F., Prosser, B. L., Borroto, C., Mazaitis, M. J., et al. (2012). Microtubules underlie dysfunction in Duchenne muscular dystrophy. Sci. Signal. 5, ra56. doi: 10.1126/scisignal.2002829.
    • (2012) Sci. Signal. , vol.5
    • Khairallah, R.J.1    Shi, G.2    Sbrana, F.3    Prosser, B.L.4    Borroto, C.5    Mazaitis, M.J.6
  • 19
    • 42649088396 scopus 로고    scopus 로고
    • Late onset in dysferlinopathy widens the clinical spectrum
    • doi: 10.1016/j.nmd.2008.01.004
    • Klinge, L., Dean, A. F., Kress, W., Dixon, P., Charlton, R., Muller, J. S., et al. (2008). Late onset in dysferlinopathy widens the clinical spectrum. Neuromuscul. Disord. 18, 288-290. doi: 10.1016/j.nmd.2008.01.004.
    • (2008) Neuromuscul. Disord. , vol.18 , pp. 288-290
    • Klinge, L.1    Dean, A.F.2    Kress, W.3    Dixon, P.4    Charlton, R.5    Muller, J.S.6
  • 20
    • 77955509776 scopus 로고    scopus 로고
    • The distribution and characterization of skeletal muscle lesions in dysferlin-deficient SJL and A/J mice
    • doi: 10.1016/j.etp.2009.06.009
    • Kobayashi, K., Izawa, T., Kuwamura, M., and Yamate, J. (2010). The distribution and characterization of skeletal muscle lesions in dysferlin-deficient SJL and A/J mice. Exp. Toxicol. Pathol. 62, 509-517. doi: 10.1016/j.etp.2009.06.009.
    • (2010) Exp. Toxicol. Pathol. , vol.62 , pp. 509-517
    • Kobayashi, K.1    Izawa, T.2    Kuwamura, M.3    Yamate, J.4
  • 21
    • 79955385633 scopus 로고    scopus 로고
    • Comparative gene expression analysis in the skeletal muscles of dysferlin-deficient SJL/J and A/J Mice
    • doi: 10.1293/tox.24.49
    • Kobayashi, K., Izawa, T., Kuwamura, M., and Yamate, J. (2011). Comparative gene expression analysis in the skeletal muscles of dysferlin-deficient SJL/J and A/J Mice. J. Toxicol. Pathol. 24, 49-62. doi: 10.1293/tox.24.49.
    • (2011) J. Toxicol. Pathol. , vol.24 , pp. 49-62
    • Kobayashi, K.1    Izawa, T.2    Kuwamura, M.3    Yamate, J.4
  • 22
    • 0347379869 scopus 로고    scopus 로고
    • Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing
    • doi: 10.1074/jbc.M307247200
    • Lennon, N. J., Kho, A., Bacskai, B. J., Perlmutter, S. L., Hyman, B. T., and Brown, R. H. Jr. (2003). Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing. J. Biol. Chem. 278, 50466-50473. doi: 10.1074/jbc.M307247200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50466-50473
    • Lennon, N.J.1    Kho, A.2    Bacskai, B.J.3    Perlmutter, S.L.4    Hyman, B.T.5    Brown Jr., R.H.6
  • 23
    • 51849129227 scopus 로고    scopus 로고
    • Decline in Nrf2-regulated antioxidants in chronic obstructive pulmonary disease lungs due to loss of its positive regulator, DJ-1
    • doi: 10.1164/rccm.200803-380OC
    • Malhotra, D., Thimmulappa, R., Navas-Acien, A., Sandford, A., Elliott, M., Singh, A., et al. (2008). Decline in Nrf2-regulated antioxidants in chronic obstructive pulmonary disease lungs due to loss of its positive regulator, DJ-1. Am. J. Respir. Crit. Care Med. 178, 592-604. doi: 10.1164/rccm.200803-380OC.
    • (2008) Am. J. Respir. Crit. Care Med. , vol.178 , pp. 592-604
    • Malhotra, D.1    Thimmulappa, R.2    Navas-Acien, A.3    Sandford, A.4    Elliott, M.5    Singh, A.6
  • 24
    • 0001161283 scopus 로고
    • Density and composition of mammalian muscle
    • Mendez, J., and Keys, A. (1960). Density and composition of mammalian muscle. Metabolism 9, 184-188.
    • (1960) Metabolism , vol.9 , pp. 184-188
    • Mendez, J.1    Keys, A.2
  • 25
    • 33846413196 scopus 로고    scopus 로고
    • Histological and immunohistological changes of the skeletal muscles in older SJL/J mice
    • doi: 10.1159/000097005
    • Nemoto, H., Konno, S., Nakazora, H., Miura, H., and Kurihara, T. (2007). Histological and immunohistological changes of the skeletal muscles in older SJL/J mice. Eur. Neurol. 57, 19-25. doi: 10.1159/000097005.
    • (2007) Eur. Neurol. , vol.57 , pp. 19-25
    • Nemoto, H.1    Konno, S.2    Nakazora, H.3    Miura, H.4    Kurihara, T.5
  • 27
    • 33746001621 scopus 로고    scopus 로고
    • Dysferlin mutations in LGMD2B, Miyoshi myopathy, and atypical dysferlinopathies
    • doi: 10.1002/humu.9355
    • Nguyen, K., Bassez, G., Bernard, R., Krahn, M., Labelle, V., Figarella-Branger, D., et al. (2005). Dysferlin mutations in LGMD2B, Miyoshi myopathy, and atypical dysferlinopathies. Hum. Mutat. 26, 165. doi: 10.1002/humu.9355.
    • (2005) Hum. Mutat. , vol.26 , pp. 165
    • Nguyen, K.1    Bassez, G.2    Bernard, R.3    Krahn, M.4    Labelle, V.5    Figarella-Branger, D.6
  • 28
    • 0346216799 scopus 로고    scopus 로고
    • Molecular bases of autosomal recessive limb-girdle muscular dystrophies
    • Nigro, V. (2003). Molecular bases of autosomal recessive limb-girdle muscular dystrophies. Acta Myol. 22, 35-42.
    • (2003) Acta Myol. , vol.22 , pp. 35-42
    • Nigro, V.1
  • 29
    • 78650755469 scopus 로고    scopus 로고
    • Histological assessment of SJL/J mice treated with the antioxidants coenzyme Q10 and resveratrol
    • doi: 10.1016/j.micron.2010.10.001
    • Potgieter, M., Pretorius, E., Van der Merwe, C. F., Beukes, M., Vieira, W. A., Auer, R. E., et al. (2011). Histological assessment of SJL/J mice treated with the antioxidants coenzyme Q10 and resveratrol. Micron 42, 275-282. doi: 10.1016/j.micron.2010.10.001.
    • (2011) Micron , vol.42 , pp. 275-282
    • Potgieter, M.1    Pretorius, E.2    Van der Merwe, C.F.3    Beukes, M.4    Vieira, W.A.5    Auer, R.E.6
  • 30
    • 84860740259 scopus 로고    scopus 로고
    • An in vivo rodent model of contraction-induced injury in the quadriceps muscle
    • doi: 10.1016/j.injury.2011.09.015
    • Pratt, S. J., Lawlor, M. W., Shah, S. B., and Lovering, R. M. (2012). An in vivo rodent model of contraction-induced injury in the quadriceps muscle. Injury 43, 788-793. doi: 10.1016/j.injury.2011.09.015.
    • (2012) Injury , vol.43 , pp. 788-793
    • Pratt, S.J.1    Lawlor, M.W.2    Shah, S.B.3    Lovering, R.M.4
  • 31
    • 84876337565 scopus 로고    scopus 로고
    • X-ROS signaling in the heart and skeletal muscle: stretch-dependent local ROS regulates [Ca2+]i
    • doi: 10.1016/j.yjmcc.2012.11.011
    • Prosser, B. L., Khairallah, R. J., Ziman, A. P., Ward, C. W., and Lederer, W. J. (2013). X-ROS signaling in the heart and skeletal muscle: stretch-dependent local ROS regulates [Ca2+]i. J. Mol. Cell. Cardiol. 58, 172-81. doi: 10.1016/j.yjmcc.2012.11.011.
    • (2013) J. Mol. Cell. Cardiol. , vol.58 , pp. 172-181
    • Prosser, B.L.1    Khairallah, R.J.2    Ziman, A.P.3    Ward, C.W.4    Lederer, W.J.5
  • 32
    • 80052623359 scopus 로고    scopus 로고
    • X-ROS signaling: rapid mechano-chemo transduction in heart
    • doi: 10.1126/science.1202768
    • Prosser, B. L., Ward, C. W., and Lederer, W. J. (2011). X-ROS signaling: rapid mechano-chemo transduction in heart. Science 333, 1440-1445. doi: 10.1126/science.1202768.
    • (2011) Science , vol.333 , pp. 1440-1445
    • Prosser, B.L.1    Ward, C.W.2    Lederer, W.J.3
  • 33
    • 22344438250 scopus 로고    scopus 로고
    • Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice
    • doi: 10.1084/jem.20050538
    • Rangasamy, T., Guo, J., Mitzner, W. A., Roman, J., Singh, A., Fryer, A. D., et al. (2005). Disruption of Nrf2 enhances susceptibility to severe airway inflammation and asthma in mice. J. Exp. Med. 202, 47-59. doi: 10.1084/jem.20050538.
    • (2005) J. Exp. Med. , vol.202 , pp. 47-59
    • Rangasamy, T.1    Guo, J.2    Mitzner, W.A.3    Roman, J.4    Singh, A.5    Fryer, A.D.6
  • 34
    • 84862834965 scopus 로고    scopus 로고
    • Oxidative damage in muscular dystrophy correlates with the severity of the pathology: role of glutathione metabolism
    • doi: 10.1007/s11064-011-0683-z
    • Renjini, R., Gayathri, N., Nalini, A., and Srinivas Bharath, M. (2012). Oxidative damage in muscular dystrophy correlates with the severity of the pathology: role of glutathione metabolism. Neurochem. Res. 37, 885-898. doi: 10.1007/s11064-011-0683-z.
    • (2012) Neurochem. Res. , vol.37 , pp. 885-898
    • Renjini, R.1    Gayathri, N.2    Nalini, A.3    Srinivas Bharath, M.4
  • 35
    • 77957756428 scopus 로고    scopus 로고
    • Dysfunctional Nrf2-Keap1 redox signaling in skeletal muscle of the sedentary old
    • doi: 10.1016/j.freeradbiomed.2010.08.010
    • Safdar, A., DeBeer, J., and Tarnopolsky, M. (2010). Dysfunctional Nrf2-Keap1 redox signaling in skeletal muscle of the sedentary old. Free Radic. Biol. Med. 49, 1487-1493. doi: 10.1016/j.freeradbiomed.2010.08.010.
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1487-1493
    • Safdar, A.1    DeBeer, J.2    Tarnopolsky, M.3
  • 36
    • 84895424950 scopus 로고    scopus 로고
    • Research approaches for a therapy of Duchenne muscular dystrophy
    • Scheuerbrandt, G. (2008). Research approaches for a therapy of Duchenne muscular dystrophy. Parent Proj. Muscular Dystrophy 1-21. Available online at: http://www.duchenne-information.eu.
    • (2008) Parent Proj. Muscular Dystrophy , pp. 1-21
    • Scheuerbrandt, G.1
  • 37
    • 78149284770 scopus 로고    scopus 로고
    • A new role for the muscle repair protein dysferlin in endothelial cell adhesion and angiogenesis
    • doi: 10.1161/ATVBAHA.110.208108
    • Sharma, A., Yu, C., Leung, C., Trane, A., Lau, M., Utokaparch, S., et al. (2010). A new role for the muscle repair protein dysferlin in endothelial cell adhesion and angiogenesis. Arterioscler. Thromb. Vasc. Biol. 30, 2196-2204. doi: 10.1161/ATVBAHA.110.208108.
    • (2010) Arterioscler. Thromb. Vasc. Biol. , vol.30 , pp. 2196-2204
    • Sharma, A.1    Yu, C.2    Leung, C.3    Trane, A.4    Lau, M.5    Utokaparch, S.6
  • 38
    • 58549105575 scopus 로고    scopus 로고
    • Targeting Nrf2 with the triterpenoid CDDO-imidazolide attenuates cigarette smoke induced emphysema and cardiac dysfunction in mice
    • doi: 10.1073/pnas.0804333106
    • Sussan, T., Rangasamy, T., Blake, D., Malhotra, D., El-Haddad, H., Bedja, D., et al. (2009). Targeting Nrf2 with the triterpenoid CDDO-imidazolide attenuates cigarette smoke induced emphysema and cardiac dysfunction in mice. Proc. Natl. Acad. Sci. U.S.A. 106, 250-255. doi: 10.1073/pnas.0804333106.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 250-255
    • Sussan, T.1    Rangasamy, T.2    Blake, D.3    Malhotra, D.4    El-Haddad, H.5    Bedja, D.6
  • 39
    • 77953012548 scopus 로고    scopus 로고
    • Stress-activated cap'n'collar transcription factors in aging and human disease
    • doi: 10.1126/scisignal.3112re3
    • Sykiotis, G., and Bohmann, D. (2010). Stress-activated cap'n'collar transcription factors in aging and human disease. Sci. Signal. 3, re3. doi: 10.1126/scisignal.3112re3.
    • (2010) Sci. Signal. , vol.3
    • Sykiotis, G.1    Bohmann, D.2
  • 40
    • 84882600223 scopus 로고    scopus 로고
    • Oxidative stress and pathology in muscular dystrophies: focus on protein thiol oxidation and dysferlinopathies
    • doi: 10.1111/febs.12142
    • Terrill, J. R., Radley-Crabb, H. G., Iwasaki, T., Lemckert, F. A., Arthur, P. G., and Grounds, M. D. (2013). Oxidative stress and pathology in muscular dystrophies: focus on protein thiol oxidation and dysferlinopathies. FEBS J. 17, 4149-4164. doi: 10.1111/febs.12142.
    • (2013) FEBS J. , vol.17 , pp. 4149-4164
    • Terrill, J.R.1    Radley-Crabb, H.G.2    Iwasaki, T.3    Lemckert, F.A.4    Arthur, P.G.5    Grounds, M.D.6
  • 41
    • 35449002458 scopus 로고    scopus 로고
    • Preclinical evaluation of targeting the Nrf2 pathway by triterpenoids (CDDO-Im and CDDO-Me) for protection from LPS-induced inflammatory response and reactive oxygen species in human peripheral blod mononuclear cells and neutrophils
    • doi: 10.1089/ars.2007.1745
    • Thimmulappa, R. K., Fuchs, R., Malhotra, D., Scollick, C., Traore, K., Bream, J., et al. (2007). Preclinical evaluation of targeting the Nrf2 pathway by triterpenoids (CDDO-Im and CDDO-Me) for protection from LPS-induced inflammatory response and reactive oxygen species in human peripheral blod mononuclear cells and neutrophils. Antioxid. Redox Signal. 9, 1963-1970. doi: 10.1089/ars.2007.1745.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 1963-1970
    • Thimmulappa, R.K.1    Fuchs, R.2    Malhotra, D.3    Scollick, C.4    Traore, K.5    Bream, J.6
  • 42
    • 33645530745 scopus 로고    scopus 로고
    • Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis
    • doi: 10.1172/JCI25790
    • Thimmulappa, R. K., Lee, H., Rangasamy, T., Reddy, S. P., Yamamoto, M., Kensler, T. W., et al. (2006). Nrf2 is a critical regulator of the innate immune response and survival during experimental sepsis. J. Clin. Invest. 116, 984-995. doi: 10.1172/JCI25790.
    • (2006) J. Clin. Invest. , vol.116 , pp. 984-995
    • Thimmulappa, R.K.1    Lee, H.2    Rangasamy, T.3    Reddy, S.P.4    Yamamoto, M.5    Kensler, T.W.6
  • 43
    • 30744443289 scopus 로고    scopus 로고
    • Common pathological mechanisms in mouse models for muscular dystrophies
    • doi: 10.1096/fj.05-4678fje
    • Turk, R., Sterrenburg, E., van der Wees, C. G., de Meijer, E. J., de Menezes, R. X., Groh, S., et al. (2006). Common pathological mechanisms in mouse models for muscular dystrophies. FASEB J. 20, 127-129. doi: 10.1096/fj.05-4678fje.
    • (2006) FASEB J. , vol.20 , pp. 127-129
    • Turk, R.1    Sterrenburg, E.2    van der Wees, C.G.3    de Meijer, E.J.4    de Menezes, R.X.5    Groh, S.6
  • 44
    • 17944377419 scopus 로고    scopus 로고
    • Dysferlin protein analysis in limb-girdle muscular dystrophies
    • doi: 10.1385/JMN:17:1:71
    • Vainzof, M., Anderson, L. V., McNally, E. M., Davis, D. B., Faulkner, G., Valle, G., et al. (2001). Dysferlin protein analysis in limb-girdle muscular dystrophies. J. Mol. Neurosci. 17, 71-80. doi: 10.1385/JMN:17:1:71.
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 71-80
    • Vainzof, M.1    Anderson, L.V.2    McNally, E.M.3    Davis, D.B.4    Faulkner, G.5    Valle, G.6
  • 45
    • 28244483213 scopus 로고    scopus 로고
    • The differential gene expression profiles of proximal and distal muscle groups are altered in pre-pathological dysferlin-deficient mice
    • doi: 10.1016/j.nmd.2005.09.002
    • Von der Hagen, M., Laval, S. H., Cree, L. M., Haldane, F., Pocock, M., Wappler, I., et al. (2005). The differential gene expression profiles of proximal and distal muscle groups are altered in pre-pathological dysferlin-deficient mice. Neuromuscul. Disord. 15, 863-877. doi: 10.1016/j.nmd.2005.09.002.
    • (2005) Neuromuscul. Disord. , vol.15 , pp. 863-877
    • Von der Hagen, M.1    Laval, S.H.2    Cree, L.M.3    Haldane, F.4    Pocock, M.5    Wappler, I.6
  • 46
    • 34250854714 scopus 로고    scopus 로고
    • Role of Nrf2 in protection against intracerebral hemorrhage injury in mice
    • doi: 10.1016/j.freeradbiomed.2007.04.020
    • Wang, J., Fields, J., Zhao, C., Langer, J., Thimmulappa, R. K., Kensler, T. W., et al. (2007). Role of Nrf2 in protection against intracerebral hemorrhage injury in mice. Free Radic. Biol. Med. 43, 408-414. doi: 10.1016/j.freeradbiomed.2007.04.020.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 408-414
    • Wang, J.1    Fields, J.2    Zhao, C.3    Langer, J.4    Thimmulappa, R.K.5    Kensler, T.W.6
  • 47
    • 0031880450 scopus 로고    scopus 로고
    • Functional aspects of skeletal muscle contractile apparatus and sarcoplasmic reticulum after fatigue
    • Williams, J. H., Ward, C. W., Spangenburg, E. E., and Nelson, R. M. (1998). Functional aspects of skeletal muscle contractile apparatus and sarcoplasmic reticulum after fatigue. J. Appl. Physiol. 85, 619-626.
    • (1998) J. Appl. Physiol. , vol.85 , pp. 619-626
    • Williams, J.H.1    Ward, C.W.2    Spangenburg, E.E.3    Nelson, R.M.4
  • 48
    • 78049309952 scopus 로고    scopus 로고
    • Quantitative measurement of Ca2+ in the sarcoplasmic reticulum lumen of mammalian skeletal muscle
    • doi: 10.1016/j.bpj.2010.08.032
    • Ziman, A. P., Ward, C. W., Rodney, G. G., Lederer, W. J., and Bloch, R. J. (2010). Quantitative measurement of Ca2+ in the sarcoplasmic reticulum lumen of mammalian skeletal muscle. Biophys. J. 99, 2705-2714. doi: 10.1016/j.bpj.2010.08.032.
    • (2010) Biophys. J. , vol.99 , pp. 2705-2714
    • Ziman, A.P.1    Ward, C.W.2    Rodney, G.G.3    Lederer, W.J.4    Bloch, R.J.5


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