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Volumn 289, Issue 1, 2014, Pages 365-378

Nuclear recruitment of neuronal nitric-oxide synthase by α-syntrophin is crucial for the induction of mitochondrial biogenesis

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Indexed keywords

CYTOLOGY;

EID: 84891691639     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.506733     Document Type: Article
Times cited : (47)

References (72)
  • 1
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases. Regulation and function
    • Förstermann, U., and Sessa, W. C. (2012) Nitric oxide synthases. Regulation and function. Eur. Heart J. 33, 829-837
    • (2012) Eur. Heart J. , vol.33 , pp. 829-837
    • Förstermann, U.1    Sessa, W.C.2
  • 2
    • 0345731023 scopus 로고    scopus 로고
    • Interplay of Cu,Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes
    • DOI 10.1080/15216540310001628717
    • Rotilio, G., Aquilano, K., and Ciriolo, M. R. (2003) Interplay of Cu, Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes. IUBMB Life 55, 629-634 (Pubitemid 38019842)
    • (2003) IUBMB Life , vol.55 , Issue.10-11 , pp. 629-634
    • Rotilio, G.1    Aquilano, K.2    Ciriolo, M.R.3
  • 3
    • 77954143681 scopus 로고    scopus 로고
    • Subcellular and cellular locations of nitric oxide synthase isoforms as determinants of health and disease
    • Villanueva, C., and Giulivi, C. (2010) Subcellular and cellular locations of nitric oxide synthase isoforms as determinants of health and disease. Free Radic Biol. Med. 49, 307-316
    • (2010) Free Radic Biol. Med. , vol.49 , pp. 307-316
    • Villanueva, C.1    Giulivi, C.2
  • 4
    • 67349230279 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase. Structure, subcellular localization, regulation, and clinical implications
    • Zhou, L., and Zhu, D. Y. (2009) Neuronal nitric oxide synthase. Structure, subcellular localization, regulation, and clinical implications. Nitric Oxide 20, 223-230
    • (2009) Nitric Oxide , vol.20 , pp. 223-230
    • Zhou, L.1    Zhu, D.Y.2
  • 5
    • 0141888365 scopus 로고    scopus 로고
    • NOS 3 subcellular localization in the regulation of nitric oxide production
    • DOI 10.1046/j.1365-201X.2003.01181.x
    • Sullivan, J. C., and Pollock, J. S. (2003) NOS3 subcellular localization in the regulation of nitric oxide production. Acta Physiol. Scand. 179, 115-122 (Pubitemid 37249245)
    • (2003) Acta Physiologica Scandinavica , vol.179 , Issue.2 , pp. 115-122
    • Sullivan, J.C.1    Pollock, J.S.2
  • 6
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains
    • DOI 10.1016/S0092-8674(00)81053-3
    • Brenman, J. E., Chao, D. S., Gee, S. H., McGee, A. W., Craven, S. E., Santillano, D. R., Wu, Z., Huang, F., Xia, H., Peters, M. F., Froehner, S. C., and Bredt, D. S. (1996) Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell 84, 757-767 (Pubitemid 26094205)
    • (1996) Cell , vol.84 , Issue.5 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5    Santillano, D.R.6    Wu, Z.7    Huang, F.8    Xia, H.9    Peters, M.F.10    Froehner, S.C.11    Bredt, D.S.12
  • 8
    • 84871691679 scopus 로고    scopus 로고
    • N-Methyl-D-aspartate receptor-dependent denitrosylation of neuronal nitric oxide synthase increase the enzyme activity
    • Qu, Z. W., Miao, W. Y., Hu, S. Q., Li, C., Zhuo, X. L., Zong, Y. Y., Wu, Y. P., and Zhang, G. Y. (2012) N-Methyl-D-aspartate receptor-dependent denitrosylation of neuronal nitric oxide synthase increase the enzyme activity. PLoS One 7, e52788
    • (2012) PLoS One , vol.7
    • Qu, Z.W.1    Miao, W.Y.2    Hu, S.Q.3    Li, C.4    Zhuo, X.L.5    Zong, Y.Y.6    Wu, Y.P.7    Zhang, G.Y.8
  • 9
    • 0034054230 scopus 로고    scopus 로고
    • Distinct expression of splice variants of neuronal nitric oxide synthase in the human gastrointestinal tract
    • Saur, D., Paehge, H., Schusdziarra, V., and Allescher, H. D. (2000) Distinct expression of splice variants of neuronal nitric oxide synthase in the human gastrointestinal tract. Gastroenterology 118, 849-858 (Pubitemid 30243748)
    • (2000) Gastroenterology , vol.118 , Issue.5 , pp. 849-858
    • Saur, D.1    Paehge, H.2    Schusdziarra, V.3    Allescher, H.4
  • 10
    • 0035379806 scopus 로고    scopus 로고
    • Increased expression of neuronal nitric oxide synthase spliced variants in reactive astrocytes of amyotrophic lateral sclerosis human spinal cord
    • Catania, M. V., Aronica, E., Yankaya, B., and Troost, D. (2001) Increased expression of neuronal nitric oxide synthase spliced variants in reactive astrocytes of amyotrophic lateral sclerosis human spinal cord. J. Neurosci. 21, RC148
    • (2001) J. Neurosci. , vol.21
    • Catania, M.V.1    Aronica, E.2    Yankaya, B.3    Troost, D.4
  • 11
    • 0000661219 scopus 로고    scopus 로고
    • Tissue- and development-specific expression of multiple alternatively spliced transcripts of rat neuronal nitric oxide synthase
    • Lee, M. A., Cai, L., Hübner, N., Lee, Y. A., and Lindpaintner, K. (1997) Tissue- and development-specific expression of multiple alternatively spliced transcripts of rat neuronal nitric oxide synthase. J. Clin. Invest. 100, 1507-1512 (Pubitemid 27425777)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.6 , pp. 1507-1512
    • Lee, M.A.1    Cai, L.2    Hubner, N.3    Lee, Y.A.4    Lindpaintner, K.5
  • 12
    • 0037565274 scopus 로고    scopus 로고
    • Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu,Zn superoxide dismutase mutant involved in familial ALS
    • DOI 10.1046/j.1471-4159.2003.01783.x
    • Aquilano, K., Rotilio, G., and Ciriolo, M. R. (2003) Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu, Zn superoxide dismutase mutant involved in familial ALS. J. Neurochem. 85, 1324-1335 (Pubitemid 36613279)
    • (2003) Journal of Neurochemistry , vol.85 , Issue.5 , pp. 1324-1335
    • Aquilano, K.1    Rotilio, G.2    Ciriolo, M.R.3
  • 13
    • 78650233501 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase interacts with Sp1 through the PDZ domain inhibiting Sp1-mediated copper-zinc superoxide dismutase expression
    • Baldelli, S., Aquilano, K., Rotilio, G., and Ciriolo, M. R. (2011) Neuronal nitric oxide synthase interacts with Sp1 through the PDZ domain inhibiting Sp1-mediated copper-zinc superoxide dismutase expression. Int. J. Biochem. Cell Biol. 43, 163-169
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 163-169
    • Baldelli, S.1    Aquilano, K.2    Rotilio, G.3    Ciriolo, M.R.4
  • 15
    • 0032578844 scopus 로고    scopus 로고
    • Isolation and characterization of a novel, human neuronal nitric oxide synthase cDNA
    • DOI 10.1006/bbrc.1998.9578
    • Larsson, B., and Phillips, S. C. (1998) Isolation and characterization of a novel, human neuronal nitric oxide synthase cDNA. Biochem. Biophys. Res. Commun. 251, 898-902 (Pubitemid 28512808)
    • (1998) Biochemical and Biophysical Research Communications , vol.251 , Issue.3 , pp. 898-902
    • Larsson, B.1    Phillips, S.C.2
  • 16
    • 0029933799 scopus 로고    scopus 로고
    • Neuronal nitric-oxide synthasemu, an alternatively spliced isoform expressed in differentiated skeletal muscle
    • Silvagno, F., Xia, H., and Bredt, D. S. (1996) Neuronal nitric-oxide synthasemu, an alternatively spliced isoform expressed in differentiated skeletal muscle. J. Biol. Chem. 271, 11204-11208
    • (1996) J. Biol. Chem. , vol.271 , pp. 11204-11208
    • Silvagno, F.1    Xia, H.2    Bredt, D.S.3
  • 17
    • 84868560653 scopus 로고    scopus 로고
    • Redox regulation of mitochondrial biogenesis
    • Piantadosi, C. A., and Suliman, H. B. (2012) Redox regulation of mitochondrial biogenesis. Free Radic. Biol. Med. 53, 2043-2053
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 2043-2053
    • Piantadosi, C.A.1    Suliman, H.B.2
  • 20
    • 84864960619 scopus 로고    scopus 로고
    • Caloric restriction and the nutrient-sensing PGC-1α in mitochondrial homeostasis. New perspectives in neurodegeneration
    • Lettieri Barbato, D., Baldelli, S., Pagliei, B., Aquilano, K., and Ciriolo, M. R. (2012) Caloric restriction and the nutrient-sensing PGC-1α in mitochondrial homeostasis. New perspectives in neurodegeneration. Int. J. Cell Biol. 2012, 759583
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 759583
    • Lettieri Barbato, D.1    Baldelli, S.2    Pagliei, B.3    Aquilano, K.4    Ciriolo, M.R.5
  • 21
    • 84877805400 scopus 로고    scopus 로고
    • Punctum on two different transcription factors regulated by PGC-1α. Nuclear factor erythroid-derived 2-like 2 and nuclear respiratory factor 2
    • Baldelli, S., Aquilano, K., and Ciriolo, M. R. (2013) Punctum on two different transcription factors regulated by PGC-1α. Nuclear factor erythroid-derived 2-like 2 and nuclear respiratory factor 2. Biochim. Biophys. Acta 1830, 4137-4146
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 4137-4146
    • Baldelli, S.1    Aquilano, K.2    Ciriolo, M.R.3
  • 22
    • 84871671895 scopus 로고    scopus 로고
    • Nitric oxide in skeletal muscle. Role on mitochondrial biogenesis and function
    • Tengan, C. H., Rodrigues, G. S., and Godinho, R. O. (2012) Nitric oxide in skeletal muscle. Role on mitochondrial biogenesis and function. Int. J. Mol. Sci. 13, 17160-17184
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 17160-17184
    • Tengan, C.H.1    Rodrigues, G.S.2    Godinho, R.O.3
  • 23
    • 33749630419 scopus 로고    scopus 로고
    • PGC-1-related coactivator: Immediate early expression and characterization of a CREB/NRF-1 binding domain associated with cytochrome c promoter occupancy and respiratory growth
    • DOI 10.1128/MCB.00585-06
    • Vercauteren, K., Pasko, R. A., Gleyzer, N., Marino, V. M., and Scarpulla, R. C. (2006) PGC-1-related coactivator. Immediate early expression and characterization of a CREB/NRF-1 binding domain associated with cytochrome c promoter occupancy and respiratory growth. Mol. Cell Biol. 26, 7409-7419 (Pubitemid 44547693)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.20 , pp. 7409-7419
    • Vercauteren, K.1    Pasko, R.A.2    Gleyzer, N.3    Marino, V.M.4    Scarpulla, R.C.5
  • 24
    • 0035139227 scopus 로고    scopus 로고
    • Physiology of nitric oxide in skeletal muscle
    • Stamler, J. S., and Meissner, G. (2001) Physiology of nitric oxide in skeletal muscle. Physiol. Rev. 81, 209-237 (Pubitemid 32096176)
    • (2001) Physiological Reviews , vol.81 , Issue.1 , pp. 209-237
    • Stamler, J.S.1    Meissner, G.2
  • 25
    • 84878941111 scopus 로고    scopus 로고
    • Extranuclear localization of SIRT1 and PGC-1α. An insight into possible roles in diseases associated with mitochondrial dysfunction
    • Aquilano, K., Baldelli, S., Pagliei, B., and Ciriolo, M. R. (2013) Extranuclear localization of SIRT1 and PGC-1α. An insight into possible roles in diseases associated with mitochondrial dysfunction. Curr. Mol. Med. 13, 140-154
    • (2013) Curr. Mol. Med. , vol.13 , pp. 140-154
    • Aquilano, K.1    Baldelli, S.2    Pagliei, B.3    Ciriolo, M.R.4
  • 27
    • 84867895466 scopus 로고    scopus 로고
    • Citrulline and arginine utility in treating nitric oxide deficiency in mitochondrial disorders
    • El-Hattab, A. W., Emrick, L. T., Craigen, W. J., and Scaglia, F. (2012) Citrulline and arginine utility in treating nitric oxide deficiency in mitochondrial disorders. Mol. Genet. Metab. 107, 247-252
    • (2012) Mol. Genet. Metab. , vol.107 , pp. 247-252
    • El-Hattab, A.W.1    Emrick, L.T.2    Craigen, W.J.3    Scaglia, F.4
  • 28
    • 84858700111 scopus 로고    scopus 로고
    • Restoration of impaired nitric oxide production in MELAS syndrome with citrulline and arginine supplementation
    • El-Hattab, A. W., Hsu, J. W., Emrick, L. T., Wong, L. J., Craigen, W. J., Jahoor, F., and Scaglia, F. (2012) Restoration of impaired nitric oxide production in MELAS syndrome with citrulline and arginine supplementation. Mol. Genet. Metab. 105, 607-614
    • (2012) Mol. Genet. Metab. , vol.105 , pp. 607-614
    • El-Hattab, A.W.1    Hsu, J.W.2    Emrick, L.T.3    Wong, L.J.4    Craigen, W.J.5    Jahoor, F.6    Scaglia, F.7
  • 31
    • 77949770385 scopus 로고    scopus 로고
    • Golgi and sarcolemmal neuronal NOS differentially regulate contraction-induced fatigue and vasoconstriction in exercising mouse skeletal muscle
    • Percival, J. M., Anderson, K. N., Huang, P., Adams, M. E., and Froehner, S. C. (2010) Golgi and sarcolemmal neuronal NOS differentially regulate contraction-induced fatigue and vasoconstriction in exercising mouse skeletal muscle. J. Clin. Invest. 120, 816-826
    • (2010) J. Clin. Invest. , vol.120 , pp. 816-826
    • Percival, J.M.1    Anderson, K.N.2    Huang, P.3    Adams, M.E.4    Froehner, S.C.5
  • 32
    • 0037459338 scopus 로고    scopus 로고
    • Vasomodulation by skeletal muscle-derived nitric oxide requires α-syntrophin-mediated sarcolemmal localization of neuronal nitric oxide synthase
    • DOI 10.1161/01.RES.0000061570.83105.52
    • Thomas, G. D., Shaul, P. W., Yuhanna, I. S., Froehner, S. C., and Adams, M. E. (2003) Vasomodulation by skeletal muscle-derived nitric oxide requires α-syntrophin-mediated sarcolemmal localization of neuronal nitric oxide synthase. Circ. Res. 92, 554-560 (Pubitemid 36368669)
    • (2003) Circulation Research , vol.92 , Issue.5 , pp. 554-560
    • Thomas, G.D.1    Shaul, P.W.2    Yuhanna, I.S.3    Froehner, S.C.4    Adams, M.E.5
  • 33
    • 77954317937 scopus 로고    scopus 로고
    • NNOSα and nNOSβ localization to aggresome-like inclusions is dependent on HSP90 activity
    • Corso-Díaz, X., and Krukoff, T. L. (2010) nNOSα and nNOSβ localization to aggresome-like inclusions is dependent on HSP90 activity. J. Neurochem. 114, 864-872
    • (2010) J. Neurochem. , vol.114 , pp. 864-872
    • Corso-Díaz, X.1    Krukoff, T.L.2
  • 35
    • 48349092316 scopus 로고    scopus 로고
    • Glutathione and copper, zinc superoxide dismutase are modulated by overexpression of neuronal nitric oxide synthase
    • Baldelli, S., Aquilano, K., Rotilio, G., and Ciriolo, M. R. (2008) Glutathione and copper, zinc superoxide dismutase are modulated by overexpression of neuronal nitric oxide synthase. Int. J. Biochem. Cell Biol. 40, 2660-2670
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2660-2670
    • Baldelli, S.1    Aquilano, K.2    Rotilio, G.3    Ciriolo, M.R.4
  • 36
    • 33845602614 scopus 로고    scopus 로고
    • Mitochondrial damage due to SOD1 deficiency in SH-SY5Y neuroblastoma cells. A rationale for the redundancy of SOD1
    • Aquilano, K., Vigilanza, P., Rotilio, G., and Ciriolo, M. R. (2006) Mitochondrial damage due to SOD1 deficiency in SH-SY5Y neuroblastoma cells. A rationale for the redundancy of SOD1. FASEB J. 20, 1683-1685
    • (2006) FASEB J. , vol.20 , pp. 1683-1685
    • Aquilano, K.1    Vigilanza, P.2    Rotilio, G.3    Ciriolo, M.R.4
  • 37
    • 84887447290 scopus 로고    scopus 로고
    • FoxO1 controls lysosomal acid lipase in adipocytes. Implication of lipophagy during nutrient restriction and metformin treatment
    • Lettieri Barbato, D., Tatulli, G., Aquilano, K., and Ciriolo, M. R. (2013) FoxO1 controls lysosomal acid lipase in adipocytes. Implication of lipophagy during nutrient restriction and metformin treatment. Cell Death Dis. 4, e861
    • (2013) Cell Death Dis. , vol.4
    • Lettieri Barbato, D.1    Tatulli, G.2    Aquilano, K.3    Ciriolo, M.R.4
  • 38
    • 84872684916 scopus 로고    scopus 로고
    • Garlicderived diallyl disulfide modulates peroxisome proliferator activated receptor gamma co-activator 1α in neuroblastoma cells
    • Pagliei, B., Aquilano, K., Baldelli, S., and Ciriolo, M. R. (2013) Garlicderived diallyl disulfide modulates peroxisome proliferator activated receptor gamma co-activator 1α in neuroblastoma cells. Biochem. Pharmacol. 85, 335-344
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 335-344
    • Pagliei, B.1    Aquilano, K.2    Baldelli, S.3    Ciriolo, M.R.4
  • 41
    • 79953131110 scopus 로고    scopus 로고
    • Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells
    • Aquilano, K., Baldelli, S., Cardaci, S., Rotilio, G., and Ciriolo, M. R. (2011) Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells. J. Cell Sci. 124, 1043-1054
    • (2011) J. Cell Sci. , vol.124 , pp. 1043-1054
    • Aquilano, K.1    Baldelli, S.2    Cardaci, S.3    Rotilio, G.4    Ciriolo, M.R.5
  • 43
    • 0038494557 scopus 로고    scopus 로고
    • Nitric oxide signaling regulates mitochondrial number and function
    • DOI 10.1038/sj.cdd.4401244
    • Bossy-Wetzel, E., and Lipton, S. A. (2003) Nitric oxide signaling regulates mitochondrial number and function. Cell Death Differ. 10, 757-760 (Pubitemid 36850236)
    • (2003) Cell Death and Differentiation , vol.10 , Issue.7 , pp. 757-760
    • Bossy-Wetzel, E.1    Lipton, S.A.2
  • 44
    • 0037066459 scopus 로고    scopus 로고
    • Regulation of mitochondrial biogenesis in skeletal muscle by caMK
    • DOI 10.1126/science.1071163
    • Wu, H., Kanatous, S. B., Thurmond, F. A., Gallardo, T., Isotani, E., Bassel-Duby, R., and Williams, R. S. (2002) Regulation of mitochondrial biogenesis in skeletal muscle by CaMK. Science 296, 349-352 (Pubitemid 34303690)
    • (2002) Science , vol.296 , Issue.5566 , pp. 349-352
    • Wu, H.1    Kanatous, S.B.2    Thurmond, F.A.3    Gallardo, T.4    Isotani, E.5    Bassel-Duby, R.6    Williams, R.S.7
  • 45
    • 30744455255 scopus 로고    scopus 로고
    • A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons
    • DOI 10.1016/j.molcel.2005.12.006, PII S1097276505018484
    • Riccio, A., Alvania, R. S., Lonze, B. E., Ramanan, N., Kim, T., Huang, Y., Dawson, T. M., Snyder, S. H., and Ginty, D. D. (2006) A nitric oxide signaling pathway controls CREB-mediated gene expression in neurons. Mol. Cell 21, 283-294 (Pubitemid 43099943)
    • (2006) Molecular Cell , vol.21 , Issue.2 , pp. 283-294
    • Riccio, A.1    Alvania, R.S.2    Lonze, B.E.3    Ramanan, N.4    Kim, T.5    Huang, Y.6    Dawson, T.M.7    Snyder, S.H.8    Ginty, D.D.9
  • 46
    • 33748585194 scopus 로고    scopus 로고
    • Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix
    • DOI 10.1016/j.yexcr.2006.06.002, PII S0014482706002151
    • Fuentes-Mera, L., Rodríguez-Muñoz, R., González- Ramírez, R., García-Sierra, F., González, E., Mornet, D., and Cisneros, B. (2006) Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells. Members of the nuclear DAPC associate with the nuclear matrix. Exp. Cell Res. 312, 3023-3035 (Pubitemid 44376478)
    • (2006) Experimental Cell Research , vol.312 , Issue.16 , pp. 3023-3035
    • Fuentes-Mera, L.1    Rodriguez-Munoz, R.2    Gonzalez-Ramirez, R.3    Garcia-Sierra, F.4    Gonzalez, E.5    Mornet, D.6    Cisneros, B.7
  • 49
    • 67349195437 scopus 로고    scopus 로고
    • NO-sensitive guanylyl cyclase beta1 subunit is peripherally associated to chromosomes during mitosis. Novel role in chromatin condensation and cell cycle progression
    • Pifarré, P., Baltrons, M. A., Földi, I., and García, A. (2009) NO-sensitive guanylyl cyclase beta1 subunit is peripherally associated to chromosomes during mitosis. Novel role in chromatin condensation and cell cycle progression. Int. J. Biochem. Cell Biol. 41, 1719-1730
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1719-1730
    • Pifarré, P.1    Baltrons, M.A.2    Földi, I.3    García, A.4
  • 50
    • 0026756560 scopus 로고
    • Calcium and calmodulin function in the cell nucleus
    • Bachs, O., Agell, N., and Carafoli, E. (1992) Calcium and calmodulin function in the cell nucleus. Biochim. Biophys. Acta 1113, 259-270
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 259-270
    • Bachs, O.1    Agell, N.2    Carafoli, E.3
  • 52
    • 84861927963 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase regulates endothelial inflammation
    • Chakrabarti, S., Chan, C. K., Jiang, Y., and Davidge, S. T. (2012) Neuronal nitric oxide synthase regulates endothelial inflammation. J. Leukocyte Biol. 91, 947-956
    • (2012) J. Leukocyte Biol. , vol.91 , pp. 947-956
    • Chakrabarti, S.1    Chan, C.K.2    Jiang, Y.3    Davidge, S.T.4
  • 54
    • 23944499856 scopus 로고    scopus 로고
    • The cAMP signalling pathway activates CREB through PKA, p38 and MSK1 in NIH 3T3 cells
    • DOI 10.1016/j.cellsig.2005.02.003, PII S0898656805000367
    • Delghandi, M. P., Johannessen, M., and Moens, U. (2005) The cAMP signalling pathway activates CREB through PKA, p38 and MSK1 in NIH 3T3 cells. Cell Signal. 17, 1343-1351 (Pubitemid 41206644)
    • (2005) Cellular Signalling , vol.17 , Issue.11 , pp. 1343-1351
    • Delghandi, M.P.1    Johannessen, M.2    Moens, U.3
  • 55
    • 0036319419 scopus 로고    scopus 로고
    • Akt pathway mediates a cGMP-dependent survival role of nitric oxide in cerebellar granule neurones
    • DOI 10.1046/j.1471-4159.2002.00857.x
    • Ciani, E., Virgili, M., and Contestabile, A. (2002) Akt pathway mediates a cGMP-dependent survival role of nitric oxide in cerebellar granule neurones. J. Neurochem. 81, 218-228 (Pubitemid 34809347)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.2 , pp. 218-228
    • Ciani, E.1    Virgili, M.2    Contestabile, A.3
  • 57
    • 79960130365 scopus 로고    scopus 로고
    • α-Syntrophin modulates myogenin expression in differentiating myoblasts
    • Kim, M. J., Hwang, S. H., Lim, J. A., Froehner, S. C., Adams, M. E., and Kim, H. S. (2010) α-Syntrophin modulates myogenin expression in differentiating myoblasts. PLoS One 5, e15355
    • (2010) PLoS One , vol.5
    • Kim, M.J.1    Hwang, S.H.2    Lim, J.A.3    Froehner, S.C.4    Adams, M.E.5    Kim, H.S.6
  • 58
    • 54849413581 scopus 로고    scopus 로고
    • Nuclear and nuclear envelope localization of dystrophin Dp71 and dystrophin-associated proteins (DAPs) in the C2C12 muscle cells. DAPs nuclear localization is modulated during myogenesis
    • González-Ramírez, R., Morales-Lázaro, S. L., Tapia-Ramírez, V., Mornet, D., and Cisneros, B. (2008) Nuclear and nuclear envelope localization of dystrophin Dp71 and dystrophin-associated proteins (DAPs) in the C2C12 muscle cells. DAPs nuclear localization is modulated during myogenesis. J. Cell Biochem. 105, 735-745
    • (2008) J. Cell Biochem. , vol.105 , pp. 735-745
    • González-Ramírez, R.1    Morales-Lázaro, S.L.2    Tapia-Ramírez, V.3    Mornet, D.4    Cisneros, B.5
  • 59
    • 84892172072 scopus 로고    scopus 로고
    • Dystrophin complex functions as a scaffold for signalling proteins
    • 10.1016/j.bbamem.2013.08.023
    • Constantin, B. (2013) Dystrophin complex functions as a scaffold for signalling proteins. Biochim. Biophys. Acta 10.1016/j.bbamem.2013.08.023
    • (2013) Biochim. Biophys. Acta
    • Constantin, B.1
  • 60
    • 84879603100 scopus 로고    scopus 로고
    • Syntrophin proteins as Santa Claus. Role (s) in cell signal transduction
    • Bhat, H. F., Adams, M. E., and Khanday, F. A. (2013) Syntrophin proteins as Santa Claus. Role (s) in cell signal transduction. Cell Mol. Life Sci. 70, 2533-2554
    • (2013) Cell Mol. Life Sci. , vol.70 , pp. 2533-2554
    • Bhat, H.F.1    Adams, M.E.2    Khanday, F.A.3
  • 61
    • 28844465125 scopus 로고    scopus 로고
    • Mitochondrial myopathies: Diagnosis, exercise intolerance, and treatment options
    • DOI 10.1249/01.mss.0000177341.89478.06
    • Tarnopolsky, M. A., and Raha, S. (2005) Mitochondrial myopathies. Diagnosis, exercise intolerance, and treatment options. Med. Sci. Sports Exerc. 37, 2086-2093 (Pubitemid 41780735)
    • (2005) Medicine and Science in Sports and Exercise , vol.37 , Issue.12 , pp. 2086-2093
    • Tarnopolsky, M.A.1    Raha, S.2
  • 64
    • 0034683669 scopus 로고    scopus 로고
    • Absence of α-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin
    • Adams, M. E., Kramarcy, N., Krall, S. P., Rossi, S. G., Rotundo, R. L., Sealock, R., and Froehner, S. C. (2000) Absence of α-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin. J. Cell Biol. 150, 1385-1398
    • (2000) J. Cell Biol. , vol.150 , pp. 1385-1398
    • Adams, M.E.1    Kramarcy, N.2    Krall, S.P.3    Rossi, S.G.4    Rotundo, R.L.5    Sealock, R.6    Froehner, S.C.7
  • 65
    • 0033593119 scopus 로고    scopus 로고
    • α1-Syntrophin gene disruption results in the absence of neuronal-type nitric-oxide synthase at the sarcolemma but does not induce muscle degeneration
    • Kameya, S., Miyagoe, Y., Nonaka, I., Ikemoto, T., Endo, M., Hanaoka, K., Nabeshima, Y., and Takeda, S. (1999) α1-Syntrophin gene disruption results in the absence of neuronal-type nitric-oxide synthase at the sarcolemma but does not induce muscle degeneration. J. Biol. Chem. 274, 2193-2200
    • (1999) J. Biol. Chem. , vol.274 , pp. 2193-2200
    • Kameya, S.1    Miyagoe, Y.2    Nonaka, I.3    Ikemoto, T.4    Endo, M.5    Hanaoka, K.6    Nabeshima, Y.7    Takeda, S.8
  • 66
    • 84865516906 scopus 로고    scopus 로고
    • Fatigue and muscle atrophy in a mouse model of myasthenia gravis is paralleled by loss of sarcolemmal nNOS
    • Meinen, S., Lin, S., Rüegg, M. A., and Punga, A. R. (2012) Fatigue and muscle atrophy in a mouse model of myasthenia gravis is paralleled by loss of sarcolemmal nNOS. PLoS One 7, e44148
    • (2012) PLoS One , vol.7
    • Meinen, S.1    Lin, S.2    Rüegg, M.A.3    Punga, A.R.4
  • 68
    • 84871200918 scopus 로고    scopus 로고
    • Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition
    • Percival, J. M., Siegel, M. P., Knowels, G., and Marcinek, D. J. (2013) Defects in mitochondrial localization and ATP synthesis in the mdx mouse model of Duchenne muscular dystrophy are not alleviated by PDE5 inhibition. Hum. Mol. Genet. 22, 153-167
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 153-167
    • Percival, J.M.1    Siegel, M.P.2    Knowels, G.3    Marcinek, D.J.4
  • 69
    • 84868122492 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma coactivator1-gene α transfer restores mitochondrial biomass and improves mitochondrial calcium handling in post-necrotic mdx mouse skeletal muscle
    • Godin, R., Daussin, F., Matecki, S., Li, T., Petrof, B. J., and Burelle, Y. (2012) Peroxisome proliferator-activated receptor gamma coactivator1-gene α transfer restores mitochondrial biomass and improves mitochondrial calcium handling in post-necrotic mdx mouse skeletal muscle. J. Physiol. 590, 5487-5502
    • (2012) J. Physiol. , vol.590 , pp. 5487-5502
    • Godin, R.1    Daussin, F.2    Matecki, S.3    Li, T.4    Petrof, B.J.5    Burelle, Y.6
  • 70
    • 34147109662 scopus 로고    scopus 로고
    • PGC-1α regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophy
    • DOI 10.1101/gad.1525107
    • Handschin, C., Kobayashi, Y. M., Chin, S., Seale, P., Campbell, K. P., and Spiegelman, B. M. (2007) PGC-1α regulates the neuromuscular junction program and ameliorates Duchenne muscular dystrophy. Genes Dev. 21, 770-783 (Pubitemid 46572357)
    • (2007) Genes and Development , vol.21 , Issue.7 , pp. 770-783
    • Handschin, C.1    Kobayashi, Y.M.2    Chin, S.3    Seale, P.4    Campbell, K.P.5    Spiegelman, B.M.6
  • 71
    • 33646234945 scopus 로고    scopus 로고
    • Persistent and improved functional gain in mdx dystrophic mice after treatment with L-arginine and deflazacort
    • DOI 10.1096/fj.05-4821fje
    • Archer, J. D., Vargas, C. C., and Anderson, J. E. (2006) Persistent and improved functional gain in mdx dystrophic mice after treatment with L-arginine and deflazacort. FASEB J. 20, 738-740 (Pubitemid 46671199)
    • (2006) FASEB Journal , vol.20 , Issue.6 , pp. 738-740
    • Archer, J.D.1    Vargas, C.C.2    Anderson, J.E.3
  • 72
    • 84856119982 scopus 로고    scopus 로고
    • Nitric oxide sustains long-term skeletal muscle regeneration by regulating fate of satellite cells via signaling pathways requiring Vangl2 and cyclic GMP
    • Buono, R., Vantaggiato, C., Pisa, V., Azzoni, E., Bassi, M. T., Brunelli, S., Sciorati, C., and Clementi, E. (2012) Nitric oxide sustains long-term skeletal muscle regeneration by regulating fate of satellite cells via signaling pathways requiring Vangl2 and cyclic GMP. Stem Cells 30, 197-209
    • (2012) Stem Cells , vol.30 , pp. 197-209
    • Buono, R.1    Vantaggiato, C.2    Pisa, V.3    Azzoni, E.4    Bassi, M.T.5    Brunelli, S.6    Sciorati, C.7    Clementi, E.8


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