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Volumn 2014, Issue , 2014, Pages

Vitamin D signaling in myogenesis: Potential for treatment of sarcopenia

Author keywords

[No Author keywords available]

Indexed keywords

CALCIFEDIOL; CAVEOLIN 1; COLECALCIFEROL; GLUCOSE TRANSPORTER 4; PHOSPHATIDYLINOSITOL 3 KINASE; VITAMIN D; VITAMIN D RECEPTOR; CALCITRIOL RECEPTOR;

EID: 84904695640     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2014/121254     Document Type: Review
Times cited : (70)

References (141)
  • 1
    • 0024430754 scopus 로고
    • Summary comments: Epidemiological and methodological problems in determining nutritional status of older persons
    • 2-s2.0-0024430754
    • Rosenberg I. H., Summary comments: epidemiological and methodological problems in determining nutritional status of older persons. The American Journal of Clinical Nutrition 1989 50 5 1231 1233 2-s2.0-0024430754
    • (1989) The American Journal of Clinical Nutrition , vol.50 , Issue.5 , pp. 1231-1233
    • Rosenberg, I.H.1
  • 2
    • 0030968884 scopus 로고    scopus 로고
    • Sarcopenia: Origins and clinical relevance
    • Rosenberg I. H., Sarcopenia: origins and clinical relevance. Journal of Nutrition 1997 127 5, supplement 990S 991S 2-s2.0-0030968884 (Pubitemid 27209486)
    • (1997) Journal of Nutrition , vol.127 , Issue.5 SUPPL.
    • Rosenberg, I.H.1
  • 3
    • 77953870112 scopus 로고    scopus 로고
    • Sarcopenia: European consensus on definition and diagnosis: Report of the European Working Group on Sarcopenia in Older People
    • Cruz-Jentoft A. J., Baeyens J. P., Bauer J. M., Sarcopenia: European consensus on definition and diagnosis: report of the European Working Group on Sarcopenia in Older People. Age Ageing 2010 39 4 412 423
    • (2010) Age Ageing , vol.39 , Issue.4 , pp. 412-423
    • Cruz-Jentoft, A.J.1    Baeyens, J.P.2    Bauer, J.M.3
  • 5
    • 34247568590 scopus 로고    scopus 로고
    • Alternative definitions of sarcopenia, lower extremity performance, and functional impairment with aging in older men and women
    • DOI 10.1111/j.1532-5415.2007.01140.x
    • Delmonico M. J., Harris T. B., Lee J.-S., Visser M., Nevitt M., Kritchevsky S. B., Tylavsky F. A., Newman A. B., Alternative definitions of sarcopenia, lower extremity performance, and functional impairment with aging in older men and women. Journal of the American Geriatrics Society 2007 55 5 769 774 2-s2.0-34247568590 10.1111/j.1532-5415.2007.01140.x (Pubitemid 46668965)
    • (2007) Journal of the American Geriatrics Society , vol.55 , Issue.5 , pp. 769-774
    • Delmonico, M.J.1    Harris, T.B.2    Lee, J.-S.3    Visser, M.4    Nevitt, M.5    Kritchevsky, S.B.6    Tylavsky, F.A.7    Newman, A.B.8
  • 7
    • 0036073319 scopus 로고    scopus 로고
    • Longitudinal changes in body composition in older men and women: Role of body weight change and physical activity
    • Hughes V. A., Frontera W. R., Roubenoff R., Evans W. J., Fiatarone Singh M. A., Longitudinal changes in body composition in older men and women: role of body weight change and physical activity. The American Journal of Clinical Nutrition 2002 76 2 473 481 2-s2.0-0036073319 (Pubitemid 34804075)
    • (2002) American Journal of Clinical Nutrition , vol.76 , Issue.2 , pp. 473-481
    • Hughes, V.A.1    Frontera, W.R.2    Roubenoff, R.3    Evans, W.J.4    Fiatarone Singh, M.A.5
  • 9
    • 84866502856 scopus 로고    scopus 로고
    • Sarcopenia, dynapenia, and the impact of advancing age on human skeletal muscle size and strength; A quantitative review
    • 2-s2.0-84866502856 10.3389/fphys.2012.00260
    • Mitchell W. K., Williams J., Atherton P., Larvin M., Lund J., Narici M., Sarcopenia, dynapenia, and the impact of advancing age on human skeletal muscle size and strength; a quantitative review. Frontiers in Physiology 2012 3, article 260 2-s2.0-84866502856 10.3389/fphys.2012.00260
    • (2012) Frontiers in Physiology , vol.3260
    • Mitchell, W.K.1    Williams, J.2    Atherton, P.3    Larvin, M.4    Lund, J.5    Narici, M.6
  • 10
    • 69949109492 scopus 로고    scopus 로고
    • Invertebrate models of age-related muscle degeneration
    • 2-s2.0-69949109492 10.1016/j.bbagen.2009.06.011
    • Augustin H., Partridge L., Invertebrate models of age-related muscle degeneration. Biochimica et Biophysica Acta-General Subjects 2009 1790 10 1084 1094 2-s2.0-69949109492 10.1016/j.bbagen.2009.06.011
    • (2009) Biochimica et Biophysica Acta - General Subjects , vol.1790 , Issue.10 , pp. 1084-1094
    • Augustin, H.1    Partridge, L.2
  • 11
    • 84888363022 scopus 로고    scopus 로고
    • Mechanisms of skeletal muscle aging: Insights from Drosophila and mammalian models
    • Demontis F., Piccirillo R., Goldberg A. L., Perrimon N., Mechanisms of skeletal muscle aging: insights from Drosophila and mammalian models. Disease Models & Mechanisms 2013 6 6 1339 1352
    • (2013) Disease Models & Mechanisms , vol.6 , Issue.6 , pp. 1339-1352
    • Demontis, F.1    Piccirillo, R.2    Goldberg, A.L.3    Perrimon, N.4
  • 13
    • 0036246979 scopus 로고    scopus 로고
    • Low relative skeletal muscle mass (sarcopenia) in older persons is associated with functional impairment and physical disability
    • DOI 10.1046/j.1532-5415.2002.50216.x
    • Janssen I., Heymsfield S. B., Ross R., Low relative skeletal muscle mass (sarcopenia) in older persons is associated with functional impairment and physical disability. Journal of the American Geriatrics Society 2002 50 5 889 896 2-s2.0-0036246979 10.1046/j.1532-5415.2002.50216.x (Pubitemid 34496687)
    • (2002) Journal of the American Geriatrics Society , vol.50 , Issue.5 , pp. 889-896
    • Janssen, I.1    Heymsfield, S.B.2    Ross, R.3
  • 16
    • 33645141176 scopus 로고    scopus 로고
    • Influence of sarcopenia on the development of physical disability: The cardiovascular health study
    • 2-s2.0-33645141176 10.1111/j.1532-5415.2005.00540.x
    • Janssen I., Influence of sarcopenia on the development of physical disability: the cardiovascular health study. Journal of the American Geriatrics Society 2006 54 1 56 62 2-s2.0-33645141176 10.1111/j.1532-5415.2005.00540.x
    • (2006) Journal of the American Geriatrics Society , vol.54 , Issue.1 , pp. 56-62
    • Janssen, I.1
  • 17
    • 79955612531 scopus 로고    scopus 로고
    • An overview of sarcopenia: Facts and numbers on prevalence and clinical impact
    • 2-s2.0-79955612531 10.1007/s13539-010-0014-2
    • von Haehling S., Morley J. E., Anker S. D., An overview of sarcopenia: facts and numbers on prevalence and clinical impact. Journal of Cachexia, Sarcopenia and Muscle 2010 1 2 129 133 2-s2.0-79955612531 10.1007/s13539-010- 0014-2
    • (2010) Journal of Cachexia, Sarcopenia and Muscle , vol.1 , Issue.2 , pp. 129-133
    • Von Haehling, S.1    Morley, J.E.2    Anker, S.D.3
  • 18
    • 0346499181 scopus 로고    scopus 로고
    • The Healthcare Costs of Sarcopenia in the United States
    • DOI 10.1111/j.1532-5415.2004.52014.x
    • Janssen I., Shepard D. S., Katzmarzyk P. T., Roubenoff R., The healthcare costs of sarcopenia in the United States. Journal of the American Geriatrics Society 2004 52 1 80 85 2-s2.0-0346499181 10.1111/j.1532-5415.2004.52014.x (Pubitemid 38090394)
    • (2004) Journal of the American Geriatrics Society , vol.52 , Issue.1 , pp. 80-85
    • Janssen, I.1    Shepard, D.S.2    Katzmarzyk, P.T.3    Roubenoff, R.4
  • 20
    • 84904654136 scopus 로고    scopus 로고
    • World Population Ageing 1950-2050, Department of Economic and Social Affairs, United Nations, 2001
    • World Population Ageing 1950-2050, Department of Economic and Social Affairs, United Nations, 2001, http://www.un.org/esa/population/publications/ worldageing19502050/
  • 23
  • 24
    • 79951646427 scopus 로고    scopus 로고
    • Is the vitamin D receptor found in muscle?
    • 2-s2.0-79951646427 10.1210/en.2010-1109
    • Wang Y., DeLuca H. F., Is the vitamin D receptor found in muscle? Endocrinology 2011 152 2 354 363 2-s2.0-79951646427 10.1210/en.2010-1109
    • (2011) Endocrinology , vol.152 , Issue.2 , pp. 354-363
    • Wang, Y.1    Deluca, H.F.2
  • 25
    • 84861577440 scopus 로고    scopus 로고
    • Where is the vitamin D receptor?
    • 2-s2.0-84861577440 10.1016/j.abb.2012.04.001
    • Wang Y., Zhu J., DeLuca H. F., Where is the vitamin D receptor? Archives of Biochemistry and Biophysics 2012 523 1 123 133 2-s2.0-84861577440 10.1016/j.abb.2012.04.001
    • (2012) Archives of Biochemistry and Biophysics , vol.523 , Issue.1 , pp. 123-133
    • Wang, Y.1    Zhu, J.2    Deluca, H.F.3
  • 29
    • 84865131204 scopus 로고    scopus 로고
    • 12 cells and regenerating skeletal muscle: Potential role in suppression of myoblast proliferation
    • 2-s2.0-84865131204 10.1152/ajpcell.00014.2012
    • 12 cells and regenerating skeletal muscle: potential role in suppression of myoblast proliferation. American Journal of Physiology-Cell Physiology 2012 303 4 C396 C405 2-s2.0-84865131204 10.1152/ajpcell.00014.2012
    • (2012) American Journal of Physiology - Cell Physiology , vol.303 , Issue.4
    • Srikuea, R.1    Zhang, X.2    Park-Sarge, O.-K.3    Esser, K.A.4
  • 30
    • 84877107028 scopus 로고    scopus 로고
    • Dose-dependent effects of vitamin D on transdifferentiation of skeletal muscle cells to adipose cells
    • 2-s2.0-84877107028 10.1530/JOE-12-0234
    • Ryan K. J., Daniel Z. C., Craggs L. J., Parr T., Brameld J. M., Dose-dependent effects of vitamin D on transdifferentiation of skeletal muscle cells to adipose cells. Journal of Endocrinology 2013 217 1 45 58 2-s2.0-84877107028 10.1530/JOE-12-0234
    • (2013) Journal of Endocrinology , vol.217 , Issue.1 , pp. 45-58
    • Ryan, K.J.1    Daniel, Z.C.2    Craggs, L.J.3    Parr, T.4    Brameld, J.M.5
  • 31
    • 84898779463 scopus 로고    scopus 로고
    • Vitamin D receptor gene silencing effects on differentiation of myogenic cell lines
    • Tanaka M., Kishimoto K. N., Okuno H., Saito H., Itoi E., Vitamin D receptor gene silencing effects on differentiation of myogenic cell lines. Muscle & Nerve 2014 49 5 700 708
    • (2014) Muscle & Nerve , vol.49 , Issue.5 , pp. 700-708
    • Tanaka, M.1    Kishimoto, K.N.2    Okuno, H.3    Saito, H.4    Itoi, E.5
  • 33
    • 0031755168 scopus 로고    scopus 로고
    • Current understanding of the molecular actions of vitamin D
    • Jones G., Strugnell S. A., DeLuca H. F., Current understanding of the molecular actions of vitamin D. Physiological Reviews 1998 78 4 1193 1231 2-s2.0-0031755168 (Pubitemid 28491953)
    • (1998) Physiological Reviews , vol.78 , Issue.4 , pp. 1193-1231
    • Jones, G.1    Strugnell, S.A.2    DeLuca, H.F.3
  • 34
    • 0037224484 scopus 로고    scopus 로고
    • Nongenomic actions of steroid hormones
    • DOI 10.1038/nrm1009
    • Lösel R., Wehling M., Nongenomic actions of steroid hormones. Nature Reviews Molecular Cell Biology 2003 4 1 46 56 2-s2.0-0037224484 10.1038/nrm1009 (Pubitemid 36077256)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.1 , pp. 46-56
    • Losel, R.1    Wehling, M.2
  • 35
    • 34548202165 scopus 로고    scopus 로고
    • Vitamin D signalling pathways in cancer: Potential for anticancer therapeutics
    • DOI 10.1038/nrc2196, PII NRC2196
    • Deeb K. K., Trump D. L., Johnson C. S., Vitamin D signalling pathways in cancer: potential for anticancer therapeutics. Nature Reviews Cancer 2007 7 9 684 700 2-s2.0-34548202165 10.1038/nrc2196 (Pubitemid 47327412)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.9 , pp. 684-700
    • Deeb, K.K.1    Trump, D.L.2    Johnson, C.S.3
  • 36
    • 84874368830 scopus 로고    scopus 로고
    • The roles of vitamin D in skeletal muscle: Form, function, and metabolism
    • 2-s2.0-84874368830 10.1210/er.2012-1012
    • Girgis C. M., Clifton-Bligh R. J., Hamrick M. W., Holick M. F., Gunton J. E., The roles of vitamin D in skeletal muscle: form, function, and metabolism. Endocrine Reviews 2013 34 1 33 83 2-s2.0-84874368830 10.1210/er.2012-1012
    • (2013) Endocrine Reviews , vol.34 , Issue.1 , pp. 33-83
    • Girgis, C.M.1    Clifton-Bligh, R.J.2    Hamrick, M.W.3    Holick, M.F.4    Gunton, J.E.5
  • 37
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • 2-s2.0-0028988403
    • Bouillon R., Okamura W. H., Norman A. W., Structure-function relationships in the vitamin D endocrine system. Endocrine Reviews 1995 16 2 200 257 2-s2.0-0028988403
    • (1995) Endocrine Reviews , vol.16 , Issue.2 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 41
    • 0021285079 scopus 로고
    • 3 metabolites on calcium fluxes in intact chicken skeletal muscle and myoblasts cultured in vitro
    • 3 metabolites on calcium fluxes in intact chicken skeletal muscle and myoblasts cultured in vitro. Calcified Tissue International 1984 36 2 200 205 2-s2.0-0021285079 (Pubitemid 14026354)
    • (1984) Calcified Tissue International , vol.36 , Issue.2 , pp. 200-205
    • Giuliani, D.L.1    Boland, R.L.2
  • 43
    • 0024465164 scopus 로고
    • Modulation of DNA synthesis in cultured muscle cells by 1,25-dihydroxyvitamin D-3
    • DOI 10.1016/0167-4889(89)90022-0
    • Drittanti L., de Boland A. R., Boland R., Modulation of DNA synthesis in cultured muscle cells by 1,25-dihydroxyvitamin D-3. Biochimica et Biophysica Acta-Molecular Cell Research 1989 1014 2 112 119 2-s2.0-0024465164 (Pubitemid 19283086)
    • (1989) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1014 , Issue.2 , pp. 112-119
    • Drittanti, L.1    De Boland, A.R.2    Boland, R.3
  • 44
    • 0345517254 scopus 로고    scopus 로고
    • 3 regulation of chick myoblast proliferation and differentiation
    • DOI 10.1016/S0303-7207(99)00093-3, PII S0303720799000933
    • 3 regulation of chick myoblast proliferation and differentiation. Molecular and Cellular Endocrinology 1999 153 1-2 39 45 2-s2.0-0345517254 10.1016/S0303-7207(99)00093-3 (Pubitemid 29339155)
    • (1999) Molecular and Cellular Endocrinology , vol.153 , Issue.1-2 , pp. 39-45
    • Capiati, D.A.1    Tellez-Inon, M.T.2    Boland, R.L.3
  • 45
    • 0036280792 scopus 로고    scopus 로고
    • 12 skeletal muscle cells
    • DOI 10.1080/15216540212334
    • 12 skeletal muscle cells. IUBMB Life 2002 53 3 175 181 2-s2.0-0036280792 10.1080/15216540212334 (Pubitemid 34686059)
    • (2002) IUBMB Life , vol.53 , Issue.3 , pp. 175-181
    • Stio, M.1    Celli, A.2    Treves, C.3
  • 46
    • 0344943235 scopus 로고    scopus 로고
    • Deletion of Vitamin D Receptor Gene in Mice Results in Abnormal Skeletal Muscle Development with Deregulated Expression of Myoregulatory Transcription Factors
    • DOI 10.1210/en.2003-0502
    • Endo I., Inoue D., Mitsui T., Umaki Y., Akaike M., Yoshizawa T., Kato S., Matsumoto T., Deletion of vitamin D receptor gene in mice results in abnormal skeletal muscle development with deregulated expression of myoregulatory transcription factors. Endocrinology 2003 144 12 5138 5144 2-s2.0-0344943235 10.1210/en.2003-0502 (Pubitemid 37476038)
    • (2003) Endocrinology , vol.144 , Issue.12 , pp. 5138-5144
    • Endo, I.1    Inoue, D.2    Mitsui, T.3    Umaki, Y.4    Akaike, M.5    Yoshizawa, T.6    Kato, S.7    Matsumoto, T.8
  • 48
    • 77957686086 scopus 로고    scopus 로고
    • Regulation of skeletal myogenesis by Notch
    • 2-s2.0-77957686086 10.1016/j.yexcr.2010.05.002
    • Buas M. F., Kadesch T., Regulation of skeletal myogenesis by Notch. Experimental Cell Research 2010 316 18 3028 3033 2-s2.0-77957686086 10.1016/j.yexcr.2010.05.002
    • (2010) Experimental Cell Research , vol.316 , Issue.18 , pp. 3028-3033
    • Buas, M.F.1    Kadesch, T.2
  • 49
    • 0030701537 scopus 로고    scopus 로고
    • Identification of a novel suppressive vitamin D response sequence in the 5'-Flanking region of the murine Id1 gene
    • DOI 10.1074/jbc.272.47.29865
    • Ezura Y., Tournay O., Nifuji A., Noda M., Identification of a novel suppressive vitamin D response sequence in the 5′-Flanking region of the murine Id1 gene. The Journal of Biological Chemistry 1997 272 47 29865 29872 2-s2.0-0030701537 10.1074/jbc.272.47.29865 (Pubitemid 27508085)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29865-29872
    • Ezura, Y.1    Tournay, O.2    Nifuji, A.3    Noda, M.4
  • 51
    • 84894527757 scopus 로고    scopus 로고
    • The ID proteins: Master regulators of cancer stem cells and tumour aggressiveness
    • Lasorella A., Benezra R., Iavarone A., The ID proteins: master regulators of cancer stem cells and tumour aggressiveness. Nature Reviews. Cancer 2014 14 2 77 91
    • (2014) Nature Reviews. Cancer , vol.14 , Issue.2 , pp. 77-91
    • Lasorella, A.1    Benezra, R.2    Iavarone, A.3
  • 52
    • 0026765031 scopus 로고
    • Overexpression of Id protein inhibits the muscle differentiation program: In vivo association of Id with E2A proteins
    • 2-s2.0-0026765031
    • Jen Y., Weintraub H., Benezra R., Overexpression of Id protein inhibits the muscle differentiation program: in vivo association of Id with E2A proteins. Genes & Development 1992 6 8 1466 1479 2-s2.0-0026765031
    • (1992) Genes & Development , vol.6 , Issue.8 , pp. 1466-1479
    • Jen, Y.1    Weintraub, H.2    Benezra, R.3
  • 53
    • 0035986599 scopus 로고    scopus 로고
    • 3 induces translocation of the vitamin D receptor (VDR) to the plasma membrane in skeletal muscle cells
    • DOI 10.1002/jcb.10191
    • 3 induces translocation of the vitamin D receptor (VDR) to the plasma membrane in skeletal muscle cells. Journal of Cellular Biochemistry 2002 86 1 128 135 2-s2.0-0035986599 10.1002/jcb.10191 (Pubitemid 34595019)
    • (2002) Journal of Cellular Biochemistry , vol.86 , Issue.1 , pp. 128-135
    • Nemere, I.1    Larsson, D.2
  • 55
    • 77954762255 scopus 로고    scopus 로고
    • 3-dependent modulation of Src, MAPK cascades and VDR localization in skeletal muscle cells
    • 2-s2.0-77954762255 10.1016/j.jsbmb.2010.03.002
    • 3-dependent modulation of Src, MAPK cascades and VDR localization in skeletal muscle cells. The Journal of Steroid Biochemistry and Molecular Biology 2010 121 1-2 169 175 2-s2.0-77954762255 10.1016/j.jsbmb.2010.03.002
    • (2010) The Journal of Steroid Biochemistry and Molecular Biology , vol.121 , Issue.1-2 , pp. 169-175
    • Buitrago, C.1    Boland, R.2
  • 57
    • 34247555889 scopus 로고    scopus 로고
    • 3-MARRS receptor: Multiple functional roles in diverse cell systems
    • DOI 10.2174/092986707780362871
    • 3-MARRS receptor: multiple functional roles in diverse cell systems. Current Medicinal Chemistry 2007 14 10 1087 1093 2-s2.0-34247555889 10.2174/092986707780362871 (Pubitemid 46672627)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.10 , pp. 1087-1093
    • Khanal, R.C.1    Nemere, I.2
  • 60
    • 0037715153 scopus 로고    scopus 로고
    • 3 regulation of the mitogen-activated protein kinase pathway in muscle cells
    • DOI 10.1074/jbc.M205732200
    • 3 regulation of the mitogen-activated protein kinase pathway in muscle cells. The Journal of Biological Chemistry 2003 278 4 2199 2205 2-s2.0-0037715153 10.1074/jbc. M205732200 (Pubitemid 36801286)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2199-2205
    • Buitrago, C.G.1    Gonzalez Pardo, V.2    De Boland, A.R.3    Boland, R.4
  • 61
    • 0033979243 scopus 로고    scopus 로고
    • Regulation of JNK by Src during Drosophila development
    • DOI 10.1126/science.287.5451.324
    • Tateno M., Nishida Y., Adachi-Yamada T., Regulation of JNK by Src during Drosophila development. Science 2000 287 5451 324 327 2-s2.0-0033979243 10.1126/science.287.5451.324 (Pubitemid 30046764)
    • (2000) Science , vol.287 , Issue.5451 , pp. 324-327
    • Tateno, M.1    Nishida, Y.2    Adachi-Yamada, T.3
  • 62
    • 0035203194 scopus 로고    scopus 로고
    • ERK1/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion
    • Jones N. C., Fedorov Y. V., Rosenthal R. S., Olwin B. B., ERK1/2 is required for myoblast proliferation but is dispensable for muscle gene expression and cell fusion. Journal of Cellular Physiology 2001 186 1 104 115
    • (2001) Journal of Cellular Physiology , vol.186 , Issue.1 , pp. 104-115
    • Jones, N.C.1    Fedorov, Y.V.2    Rosenthal, R.S.3    Olwin, B.B.4
  • 63
    • 0033548233 scopus 로고    scopus 로고
    • Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis
    • DOI 10.1074/jbc.274.7.4341
    • 12 myogenesis. The Journal of Biological Chemistry 1999 274 7 4341 4346 2-s2.0-0033548233 10.1074/jbc.274.7.4341 (Pubitemid 29090970)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.7 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 64
    • 0033582459 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation: Participation of the MEF2C transcription factor
    • DOI 10.1074/jbc.274.8.5193
    • Zetser A., Gredinger E., Bengal E., p38 mitogen-activated protein kinase pathway promotes skeletal muscle differentiation: participation of the MEF2C transcription factor. The Journal of Biological Chemistry 1999 274 8 5193 5200 2-s2.0-0033582459 10.1074/jbc.274.8.5193 (Pubitemid 29113429)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.8 , pp. 5193-5200
    • Zetser, A.1    Gredinger, E.2    Bengal, E.3
  • 65
    • 0034067079 scopus 로고    scopus 로고
    • P38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps
    • DOI 10.1128/MCB.20.11.3951-3964.2000
    • Wu Z., Woodring P. J., Bhakta K. S., Tamura K., Wen F., Feramisco J. R., Karin M., Wang J. Y. J., Puri P. L., p38 and extracellular signal-regulated kinases regulate the myogenic program at multiple steps. Molecular and Cellular Biology 2000 20 11 3951 3964 2-s2.0-0034067079 10.1128/MCB.20.11.3951-3964.2000 (Pubitemid 30314494)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.11 , pp. 3951-3964
    • Wu, Z.1    Woodring, P.J.2    Bhakta, K.S.3    Tamura, K.4    Wen, F.5    Feramisco, J.R.6    Karin, M.7    Wang, J.Y.J.8    Puri, P.L.9
  • 66
    • 34548431604 scopus 로고    scopus 로고
    • Regulation of myostatin signaling by c-Jun N-terminal kinase in C2C12 cells
    • DOI 10.1016/j.cellsig.2007.07.002, PII S0898656807002057
    • 12 cells. Cellular Signalling 2007 19 11 2286 2295 2-s2.0-34548431604 10.1016/j.cellsig.2007.07.002 (Pubitemid 47361684)
    • (2007) Cellular Signalling , vol.19 , Issue.11 , pp. 2286-2295
    • Huang, Z.1    Chen, D.2    Zhang, K.3    Yu, B.4    Chen, X.5    Meng, J.6
  • 67
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member
    • McPherron A. C., Lawler A. M., Lee S.-J., Regulation of skeletal muscle mass in mice by a new TGF- β superfamily member. Nature 1997 387 6628 83 90 2-s2.0-0031010050 (Pubitemid 27202654)
    • (1997) Nature , vol.387 , Issue.6628 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.-J.3
  • 68
    • 34247171304 scopus 로고    scopus 로고
    • Selective control of skeletal muscle differentiation by Akt1
    • DOI 10.1074/jbc.C600315200
    • Wilson E. M., Rotwein P., Selective control of skeletal muscle differentiation by Akt1. The Journal of Biological Chemistry 2007 282 8 5106 5110 2-s2.0-34247171304 10.1074/jbc.C600315200 (Pubitemid 47093711)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5106-5110
    • Wilson, E.M.1    Rotwein, P.2
  • 70
    • 34447514029 scopus 로고    scopus 로고
    • Medical progress: Vitamin D deficiency
    • DOI 10.1056/NEJMra070553
    • Holick M. F., Vitamin D deficiency. The New England Journal of Medicine 2007 357 3 266 281 2-s2.0-34447514029 10.1056/NEJMra070553 (Pubitemid 47080391)
    • (2007) New England Journal of Medicine , vol.357 , Issue.3 , pp. 266-281
    • Holick, M.F.1
  • 73
    • 0018958337 scopus 로고
    • Histochemical and ultrastructural aspects of M. Vastus lateralis in sedentary old people (age 65-89 years)
    • DOI 10.1007/BF00690450
    • Scelsi R., Marchetti C., Poggi P., Histochemical and ultrastructural aspects of M. vastus lateralis in sedentary old people (age 65-89 years). Acta Neuropathologica 1980 51 2 99 105 2-s2.0-0018958337 (Pubitemid 10039116)
    • (1980) Acta Neuropathologica , vol.51 , Issue.2 , pp. 99-105
    • Scelsi, R.1    Marchetti, C.2    Poggi, P.3
  • 74
    • 0038137389 scopus 로고    scopus 로고
    • Muscle fibre type adaptation in the elderly human muscle
    • DOI 10.1034/j.1600-0838.2003.00299.x
    • Andersen J. L., Muscle fibre type adaptation in the elderly human muscle. Scandinavian Journal of Medicine & Science in Sports 2003 13 1 40 47 2-s2.0-0038137389 10.1034/j.1600-0838.2003.00299.x (Pubitemid 37463578)
    • (2003) Scandinavian Journal of Medicine and Science in Sports , vol.13 , Issue.1 , pp. 40-47
    • Andersen, J.L.1
  • 75
    • 0347989458 scopus 로고    scopus 로고
    • Cellular and Molecular Regulation of Muscle Regeneration
    • DOI 10.1152/physrev.00019.2003
    • Chargé S. B. P., Rudnicki M. A., Cellular and molecular regulation of muscle regeneration. Physiological Reviews 2004 84 1 209 238 2-s2.0-0347989458 10.1152/physrev.00019.2003 (Pubitemid 38049880)
    • (2004) Physiological Reviews , vol.84 , Issue.1 , pp. 209-238
    • Charge, S.B.P.1    Rudnicki, M.A.2
  • 77
    • 0034764260 scopus 로고    scopus 로고
    • Human skeletal muscle fiber type classifications
    • Scott W., Stevens J., Binder-Macleod S. A., Human skeletal muscle fiber type classifications. Physical Therapy 2001 81 11 1810 1816 2-s2.0-0034764260 (Pubitemid 33027477)
    • (2001) Physical Therapy , vol.81 , Issue.11 , pp. 1810-1816
    • Scott, W.1    Stevens, J.2    Binder-Macleod, S.A.3
  • 78
    • 84881130275 scopus 로고    scopus 로고
    • 3-dependent non-genomic activation of MAPKs, Src and Akt in skeletal muscle cells
    • 2-s2.0-84881130275 10.1016/j.jsbmb.2013.02.013
    • 3-dependent non-genomic activation of MAPKs, Src and Akt in skeletal muscle cells. The Journal of Steroid Biochemistry and Molecular Biology 2013 136 1 125 130 2-s2.0-84881130275 10.1016/j.jsbmb.2013.02.013
    • (2013) The Journal of Steroid Biochemistry and Molecular Biology , vol.136 , Issue.1 , pp. 125-130
    • Buitrago, C.1    Pardo, V.G.2    Boland, R.3
  • 79
    • 36248973631 scopus 로고    scopus 로고
    • Intrinsic changes and extrinsic influences of myogenic stem cell function during aging
    • DOI 10.1007/s12015-007-9000-2, PII SCR33226
    • Brack A. S., Rando T. A., Intrinsic changes and extrinsic influences of myogenic stem cell function during aging. Stem Cell Reviews 2007 3 3 226 237 2-s2.0-36248973631 10.1007/s12015-007-9000-2 (Pubitemid 350129709)
    • (2007) Stem Cell Reviews , vol.3 , Issue.3 , pp. 226-237
    • Brack, A.S.1    Rando, T.A.2
  • 80
    • 78650239733 scopus 로고    scopus 로고
    • Impact of ageing on muscle cell regeneration
    • 2-s2.0-78650239733 10.1016/j.arr.2009.08.001
    • Carosio S., Berardinelli M. G., Aucello M., Musarò A., Impact of ageing on muscle cell regeneration. Ageing Research Reviews 2011 10 1 35 42 2-s2.0-78650239733 10.1016/j.arr.2009.08.001
    • (2011) Ageing Research Reviews , vol.10 , Issue.1 , pp. 35-42
    • Carosio, S.1    Berardinelli, M.G.2    Aucello, M.3    Musarò, A.4
  • 81
    • 84867410773 scopus 로고    scopus 로고
    • Skeletal muscle stem cells: Effects of aging and metabolism on muscle regenerative function
    • 2-s2.0-84867410773 10.1101/sqb.2011.76.010652
    • Jang Y. C., Sinha M., Cerletti M., Dall'osso C., Wagers A. J., Skeletal muscle stem cells: effects of aging and metabolism on muscle regenerative function. Cold Spring Harbor Symposia on Quantitative Biology 2011 76 101 111 2-s2.0-84867410773 10.1101/sqb.2011.76.010652
    • (2011) Cold Spring Harbor Symposia on Quantitative Biology , vol.76 , pp. 101-111
    • Jang, Y.C.1    Sinha, M.2    Cerletti, M.3    Dall'Osso, C.4    Wagers, A.J.5
  • 82
    • 84864317860 scopus 로고    scopus 로고
    • Satellite cells are essential for skeletal muscle regeneration: The cell on the edge returns centre stage
    • 2-s2.0-84864317860 10.1242/dev.069088
    • Relaix F., Zammit P. S., Satellite cells are essential for skeletal muscle regeneration: the cell on the edge returns centre stage. Development 2012 139 16 2845 2856 2-s2.0-84864317860 10.1242/dev.069088
    • (2012) Development , vol.139 , Issue.16 , pp. 2845-2856
    • Relaix, F.1    Zammit, P.S.2
  • 83
    • 44449140897 scopus 로고
    • The structure of the sarcolemma of the frog skeletal muscle fiber
    • 2-s2.0-44449140897
    • Mauro A., Adams W. R., The structure of the sarcolemma of the frog skeletal muscle fiber. The Journal of Biophysical and Biochemical Cytology 1961 10 4, supplement 177 185 2-s2.0-44449140897
    • (1961) The Journal of Biophysical and Biochemical Cytology , vol.10 , Issue.4 SUPPLEMENT , pp. 177-185
    • Mauro, A.1    Adams, W.R.2
  • 84
    • 0034918907 scopus 로고    scopus 로고
    • Myogenic satellite cells: Physiology to molecular biology
    • Hawke T. J., Garry D. J., Myogenic satellite cells: physiology to molecular biology. Journal of Applied Physiology 2001 91 2 534 551 2-s2.0-0034918907 (Pubitemid 32681081)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.2 , pp. 534-551
    • Hawke, T.J.1    Garry, D.J.2
  • 85
    • 84874547126 scopus 로고    scopus 로고
    • Vitamin D increases cellular turnover and functionally restores the skeletal muscle after crush injury in rats
    • 2-s2.0-84874547126 10.1016/j.ajpath.2012.11.006
    • Stratos I., Li Z., Herlyn P., Rotter R., Behrendt A.-K., Mittlmeier T., Vollmar B., Vitamin D increases cellular turnover and functionally restores the skeletal muscle after crush injury in rats. American Journal of Pathology 2013 182 3 895 904 2-s2.0-84874547126 10.1016/j.ajpath.2012.11.006
    • (2013) American Journal of Pathology , vol.182 , Issue.3 , pp. 895-904
    • Stratos, I.1    Li, Z.2    Herlyn, P.3    Rotter, R.4    Behrendt, A.-K.5    Mittlmeier, T.6    Vollmar, B.7
  • 86
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • DOI 10.1038/414782a
    • Zimmet P., Alberti K. G., Shaw J., Global and societal implications of the diabetes epidemic. Nature 2001 414 6865 782 787 2-s2.0-0035856920 10.1038/414782a (Pubitemid 34000780)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.M.M.2    Shaw, J.3
  • 87
    • 70449358688 scopus 로고    scopus 로고
    • Excessive loss of skeletal muscle mass in older adults with type 2 diabetes
    • 2-s2.0-70449358688 10.2337/dc09-0264
    • Park S. W., Goodpaster B. H., Lee J. S., Excessive loss of skeletal muscle mass in older adults with type 2 diabetes. Diabetes Care 2009 32 11 1993 1997 2-s2.0-70449358688 10.2337/dc09-0264
    • (2009) Diabetes Care , vol.32 , Issue.11 , pp. 1993-1997
    • Park, S.W.1    Goodpaster, B.H.2    Lee, J.S.3
  • 88
    • 80052600114 scopus 로고    scopus 로고
    • Vitamin D and type 2 diabetes: A systematic review
    • 2-s2.0-80052600114 10.1038/ejcn.2011.118
    • Mitri J., Muraru M. D., Pittas A. G., Vitamin D and type 2 diabetes: a systematic review. European Journal of Clinical Nutrition 2011 65 9 1005 1015 2-s2.0-80052600114 10.1038/ejcn.2011.118
    • (2011) European Journal of Clinical Nutrition , vol.65 , Issue.9 , pp. 1005-1015
    • Mitri, J.1    Muraru, M.D.2    Pittas, A.G.3
  • 89
    • 21644436729 scopus 로고    scopus 로고
    • Invited review: Contraction signaling to glucose transport in skeletal muscle
    • DOI 10.1152/japplphysiol.00175.2005
    • Jessen N., Goodyear L. J., Contraction signaling to glucose transport in skeletal muscle. Journal of Applied Physiology 2005 99 1 330 337 2-s2.0-21644436729 10.1152/japplphysiol.00175.2005 (Pubitemid 40934499)
    • (2005) Journal of Applied Physiology , vol.99 , Issue.1 , pp. 330-337
    • Jessen, N.1    Goodyear, L.J.2
  • 90
    • 84871282327 scopus 로고    scopus 로고
    • 2S formation in 3T3L1 adipocytes
    • 2-s2.0-84871282327 10.1074/jbc.M112.407833
    • 2S formation in 3T3L1 adipocytes. The Journal of Biological Chemistry 2012 287 50 42324 42332 2-s2.0-84871282327 10.1074/jbc.M112.407833
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.50 , pp. 42324-42332
    • Manna, P.1    Jain, S.K.2
  • 91
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • 2-s2.0-77954579286 10.1074/jbc.R110.128363
    • Kabil O., Banerjee R., Redox biochemistry of hydrogen sulfide. The Journal of Biological Chemistry 2010 285 29 21903 21907 2-s2.0-77954579286 10.1074/jbc.R110.128363
    • (2010) The Journal of Biological Chemistry , vol.285 , Issue.29 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 94
    • 0029064123 scopus 로고
    • Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin
    • 2-s2.0-0029064123 10.1073/pnas.92.13.5817
    • Lund S., Holman G. D., Schmitz O., Pedersen O., Contraction stimulates translocation of glucose transporter GLUT4 in skeletal muscle through a mechanism distinct from that of insulin. Proceedings of the National Academy of Sciences of the United States of America 1995 92 13 5817 5821 2-s2.0-0029064123 10.1073/pnas.92.13.5817
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.13 , pp. 5817-5821
    • Lund, S.1    Holman, G.D.2    Schmitz, O.3    Pedersen, O.4
  • 95
    • 0018578621 scopus 로고
    • 3 in intestinal tract, stomach, kidney, skin, pituitary, and parathyroid
    • 3 in intestinal tract, stomach, kidney, skin, pituitary, and parathyroid. Science 1979 206 4423 1188 1190 2-s2.0-0018578621 (Pubitemid 10159658)
    • (1979) Science , vol.206 , Issue.4423 , pp. 1188-1190
    • Stumpf, W.E.1    Sar, M.2    Reid, F.A.3
  • 96
    • 0019169417 scopus 로고
    • Organ distribution of the cytoplasmic 1,25-dihydroxycholecalciferol receptor in various mouse tissues
    • Colston K., Hirst M., Feldman D., Organ distribution of the cytoplasmic 1,25-dihydroxycholecalciferol receptor in various mouse tissues. Endocrinology 1980 107 6 1916 1922 2-s2.0-0019169417 (Pubitemid 11194706)
    • (1980) Endocrinology , vol.107 , Issue.6 , pp. 1916-1922
    • Colston, K.1    Hirst, M.2    Feldman, D.3
  • 99
    • 0022972788 scopus 로고
    • 3 receptors and hormonal responses in cloned human skeletal muscle cells
    • 3 receptors and hormonal responses in cloned human skeletal muscle cells. Endocrinology 1986 119 5 2214 2220 2-s2.0-0022972788 (Pubitemid 17171405)
    • (1986) Endocrinology , vol.119 , Issue.5 , pp. 2214-2220
    • Costa, E.M.1    Blau, H.M.2    Feldman, D.3
  • 105
    • 75549087005 scopus 로고    scopus 로고
    • Identification of a highly specific and versatile vitamin D receptor antibody
    • 2-s2.0-75549087005 10.1016/j.abb.2009.11.029
    • Wang Y., Becklund B. R., DeLuca H. F., Identification of a highly specific and versatile vitamin D receptor antibody. Archives of Biochemistry and Biophysics 2010 494 2 166 177 2-s2.0-75549087005 10.1016/j.abb.2009.11.029
    • (2010) Archives of Biochemistry and Biophysics , vol.494 , Issue.2 , pp. 166-177
    • Wang, Y.1    Becklund, B.R.2    Deluca, H.F.3
  • 108
    • 84861575206 scopus 로고    scopus 로고
    • Extrarenal expression of the 25-hydroxyvitamin D-1-hydroxylase
    • 2-s2.0-84861575206 10.1016/j.abb.2012.02.016
    • Adams J. S., Hewison M., Extrarenal expression of the 25-hydroxyvitamin D-1-hydroxylase. Archives of Biochemistry and Biophysics 2012 523 1 95 102 2-s2.0-84861575206 10.1016/j.abb.2012.02.016
    • (2012) Archives of Biochemistry and Biophysics , vol.523 , Issue.1 , pp. 95-102
    • Adams, J.S.1    Hewison, M.2
  • 111
    • 77957679990 scopus 로고    scopus 로고
    • Genetic regulation of skeletal muscle development
    • 2-s2.0-77957679990 10.1016/j.yexcr.2010.08.018
    • Bismuth K., Relaix F., Genetic regulation of skeletal muscle development. Experimental Cell Research 2010 316 18 3081 3086 2-s2.0-77957679990 10.1016/j.yexcr.2010.08.018
    • (2010) Experimental Cell Research , vol.316 , Issue.18 , pp. 3081-3086
    • Bismuth, K.1    Relaix, F.2
  • 112
    • 0026437438 scopus 로고
    • Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death
    • 2-s2.0-0026437438 10.1016/0092-8674(92)90507-9
    • Braun T., Rudnicki M. A., Arnold H.-H., Jaenisch R., Targeted inactivation of the muscle regulatory gene Myf-5 results in abnormal rib development and perinatal death. Cell 1992 71 3 369 382 2-s2.0-0026437438 10.1016/0092-8674(92)90507-9
    • (1992) Cell , vol.71 , Issue.3 , pp. 369-382
    • Braun, T.1    Rudnicki, M.A.2    Arnold, H.-H.3    Jaenisch, R.4
  • 113
    • 0026440992 scopus 로고
    • Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development
    • 2-s2.0-0026440992 10.1016/0092-8674(92)90508-A
    • Rudnicki M. A., Braun T., Hinuma S., Jaenisch R., Inactivation of MyoD in mice leads to up-regulation of the myogenic HLH gene Myf-5 and results in apparently normal muscle development. Cell 1992 71 3 383 390 2-s2.0-0026440992 10.1016/0092-8674(92)90508-A
    • (1992) Cell , vol.71 , Issue.3 , pp. 383-390
    • Rudnicki, M.A.1    Braun, T.2    Hinuma, S.3    Jaenisch, R.4
  • 114
    • 0027258162 scopus 로고
    • Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene
    • DOI 10.1038/364501a0
    • Hasty P., Bradley A., Morris J. H., Edmondson D. G., Venuti J. M., Olson E. N., Klein W. H., Muscle deficiency and neonatal death in mice with a targeted mutation in the myogenin gene. Nature 1993 364 6437 501 506 2-s2.0-0027258162 10.1038/364501a0 (Pubitemid 23273093)
    • (1993) Nature , vol.364 , Issue.6437 , pp. 501-506
    • Hasty, P.1    Bradley, A.2    Morris, J.H.3    Edmondson, D.G.4    Venuti, J.M.5    Olson, E.N.6    Klein, W.H.7
  • 115
    • 0027297310 scopus 로고
    • Myogenin gene disruption results in perinatal lethality because of severe muscle defect
    • DOI 10.1038/364532a0
    • Nabeshima Y., Hanaoka K., Hayasaka M., Esumi E., Li S., Nonaka I., Nabeshima-Y. I., Myogenin gene disruption results in perinatal lethality because of severe muscle defect. Nature 1993 364 6437 532 535 2-s2.0-0027297310 10.1038/364532a0 (Pubitemid 23273098)
    • (1993) Nature , vol.364 , Issue.6437 , pp. 532-535
    • Nabeshima, Y.1    Hanaoka, K.2    Hayasaka, M.3    Esumi, E.4    Li, S.5    Nonaka, I.6    Nabeshima -, Y.I.7
  • 116
    • 0031927208 scopus 로고    scopus 로고
    • Overlapping functions of the myogenic bHLH genes MRF4 and MyoD revealed in double mutant mice
    • Rawls A., Valdez M. R., Zhang W., Richardson J., Klein W. H., Olson E. N., Overlapping functions of the myogenic bHLH genes MRF4 and MyoD revealed in double mutant mice. Development 1998 125 13 2349 2358 2-s2.0-0031927208 (Pubitemid 28362395)
    • (1998) Development , vol.125 , Issue.13 , pp. 2349-2358
    • Rawls, A.1    Valdez, M.R.2    Zhang, W.3    Richardson, J.4    Klein, W.H.5    Olson, E.N.6
  • 117
    • 0025808242 scopus 로고
    • Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo
    • Lassar A. B., Davis R. L., Wright W. E., Kadesch T., Murre C., Voronova A., Baltimore D., Weintraub H., Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. Cell 1991 66 2 305 315 2-s2.0-0025808242 10.1016/0092-8674(91)90620-E (Pubitemid 121001368)
    • (1991) Cell , vol.66 , Issue.2 , pp. 305-315
    • Lassar, A.B.1    Davis, R.L.2    Wright, W.E.3    Kadesch, T.4    Murre, C.5    Voronova, A.6    Baltimore, D.7    Weintraub, H.8
  • 118
    • 0026020867 scopus 로고
    • An inhibitory domain of E12 transcription factor prevents DNA binding in E12 homodimers but not in E12 heterodimers
    • Sun X.-H., Baltimore D., An inhibitory domain of E12 transcription factor prevents DNA binding in E12 homodimers but not in E12 heterodimers. Cell 1991 64 2 459 470 2-s2.0-0026020867 (Pubitemid 121001269)
    • (1991) Cell , vol.64 , Issue.2 , pp. 459-470
    • Sun, X.-H.1    Baltimore, D.2
  • 121
    • 0032079521 scopus 로고    scopus 로고
    • A negative vitamin D response DNA element in the human parathyroid hormone-related peptide gene binds to vitamin D receptor along with Ku antigen to mediate negative gene regulation by vitamin D
    • DOI 10.1074/jbc.273.18.10901
    • Nishishita T., Okazaki T., Ishikawa T., Igarashi T., Hata K., Ogata E., Fujita T., A negative vitamin D response DNA element in the human parathyroid hormone-related peptide gene binds to vitamin D receptor along with Ku antigen to mediate negative gene regulation by vitamin D. The Journal of Biological Chemistry 1998 273 18 10901 10907 2-s2.0-0032079521 10.1074/jbc.273.18.10901 (Pubitemid 28204927)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 10901-10907
    • Nishishita, T.1    Okazaki, T.2    Ishikawa, T.3    Igarashi, T.4    Hata, K.5    Ogata, E.6    Fujita, T.7
  • 122
    • 0036290224 scopus 로고    scopus 로고
    • Localization of a negative vitamin D response sequence in the human growth hormone gene
    • DOI 10.1006/bbrc.2002.6641
    • Seoane S., Alonso M., Segura C., Pérez-Fernández R., Localization of a negative vitamin D response sequence in the human growth hormone gene. Biochemical and Biophysical Research Communications 2002 292 1 250 255 2-s2.0-0036290224 10.1006/bbrc.2002.6641 (Pubitemid 34687356)
    • (2002) Biochemical and Biophysical Research Communications , vol.292 , Issue.1 , pp. 250-255
    • Seoane, S.1    Alonso, M.2    Segura, C.3    Perez-Fernandez, R.4
  • 123
    • 0034738420 scopus 로고    scopus 로고
    • P21(WAF1/Cip1): More than a break to the cell cycle?
    • 2-s2.0-0034738420 10.1016/S0304-419X(00)00019-6
    • Dotto G. P., p21(WAF1/Cip1): more than a break to the cell cycle? Biochimica et Biophysica Acta-Reviews on Cancer 2000 1471 1 M43 M56 2-s2.0-0034738420 10.1016/S0304-419X(00)00019-6
    • (2000) Biochimica et Biophysica Acta - Reviews on Cancer , vol.1471 , Issue.1
    • Dotto, G.P.1
  • 124
    • 0033564697 scopus 로고    scopus 로고
    • 1-phase progression
    • Sherr C. J., Roberts J. M., CDK inhibitors: positive and negative regulators of G1-phase progression. Genes & Development 1999 13 12 1501 1512 2-s2.0-0033564697 (Pubitemid 29297917)
    • (1999) Genes and Development , vol.13 , Issue.12 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 125
    • 0026526437 scopus 로고
    • E2F: A link between the Rb tumor suppressor protein and viral oncoproteins
    • 2-s2.0-0026526437
    • Nevins J. R., E2F: a link between the Rb tumor suppressor protein and viral oncoproteins. Science 1992 258 5081 424 429 2-s2.0-0026526437
    • (1992) Science , vol.258 , Issue.5081 , pp. 424-429
    • Nevins, J.R.1
  • 126
    • 0029849620 scopus 로고    scopus 로고
    • Cancer cell cycles
    • DOI 10.1126/science.274.5293.1672
    • Sherr C. J., Cancer cell cycles. Science 1996 274 5293 1672 1677 2-s2.0-0029849620 10.1126/science.274.5293.1672 (Pubitemid 26414890)
    • (1996) Science , vol.274 , Issue.5293 , pp. 1672-1674
    • Sherr, C.J.1
  • 127
    • 2342515391 scopus 로고    scopus 로고
    • Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis
    • DOI 10.1016/j.ydbio.2004.01.046, PII S0012160604001186
    • Amthor H., Nicholas G., McKinnell I., Kemp C. F., Sharma M., Kambadur R., Patel K., Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis. Developmental Biology 2004 270 1 19 30 2-s2.0-2342515391 10.1016/j.ydbio.2004.01.046 (Pubitemid 38596926)
    • (2004) Developmental Biology , vol.270 , Issue.1 , pp. 19-30
    • Amthor, H.1    Nicholas, G.2    McKinnell, I.3    Kemp, C.F.4    Sharma, M.5    Kambadur, R.6    Patel, K.7
  • 128
    • 0036301718 scopus 로고    scopus 로고
    • IGF-I, IGF-II, and IGF-receptor-1 transcript and IGF-II protein expression in myostatin knockout mice tissues
    • DOI 10.1002/mus.10160
    • Kocamis H., Gahr S. A., Batelli L., Hubbs A. F., Killefer J., IGF-I, IGF-II, and IGF-receptor-1 transcript and IGF-II protein expression in myostatin knockout mice tissues. Muscle & Nerve 2002 26 1 55 63 2-s2.0-0036301718 10.1002/mus.10160 (Pubitemid 34734396)
    • (2002) Muscle and Nerve , vol.26 , Issue.1 , pp. 55-63
    • Kocamis, H.1    Gahr, S.A.2    Batelli, L.3    Hubbs, A.F.4    Killefer, J.5
  • 129
  • 131
    • 67650071006 scopus 로고    scopus 로고
    • Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin
    • 2-s2.0-67650071006 10.1152/ajpendo.00193.2009
    • Gilson H., Schakman O., Kalista S., Lause P., Tsuchida K., Thissen J.-P., Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. American Journal of Physiology-Endocrinology and Metabolism 2009 297 1 E157 E164 2-s2.0-67650071006 10.1152/ajpendo.00193.2009
    • (2009) American Journal of Physiology - Endocrinology and Metabolism , vol.297 , Issue.1
    • Gilson, H.1    Schakman, O.2    Kalista, S.3    Lause, P.4    Tsuchida, K.5    Thissen, J.-P.6
  • 132
    • 77953080864 scopus 로고    scopus 로고
    • Myostatin down-regulates the IGF-2 expression via ALK-Smad signaling during myogenesis in cattle
    • 2-s2.0-77953080864 10.1111/j.1740-0929.2009.00725.x
    • Miyake M., Hayashi S., Taketa Y., Iwasaki S., Watanabe K., Ohwada S., Aso H., Yamaguchi T., Myostatin down-regulates the IGF-2 expression via ALK-Smad signaling during myogenesis in cattle. Animal Science Journal 2010 81 2 223 229 2-s2.0-77953080864 10.1111/j.1740-0929.2009.00725.x
    • (2010) Animal Science Journal , vol.81 , Issue.2 , pp. 223-229
    • Miyake, M.1    Hayashi, S.2    Taketa, Y.3    Iwasaki, S.4    Watanabe, K.5    Ohwada, S.6    Aso, H.7    Yamaguchi, T.8
  • 133
    • 78650843513 scopus 로고    scopus 로고
    • Endocrine actions of myostatin: Systemic regulation of the igf and igf binding protein axis
    • 2-s2.0-78650843513 10.1210/en.2010-0488
    • Williams N. G., Interlichia J. P., Jackson M. F., Hwang D., Cohen P., Rodgers B. D., Endocrine actions of myostatin: systemic regulation of the igf and igf binding protein axis. Endocrinology 2011 152 1 172 180 2-s2.0-78650843513 10.1210/en.2010-0488
    • (2011) Endocrinology , vol.152 , Issue.1 , pp. 172-180
    • Williams, N.G.1    Interlichia, J.P.2    Jackson, M.F.3    Hwang, D.4    Cohen, P.5    Rodgers, B.D.6
  • 134
    • 77953356748 scopus 로고    scopus 로고
    • Insulin-like growth factors (IGFs), IGF receptors, and IGF-binding proteins: Roles in skeletal muscle growth and differentiation
    • 2-s2.0-77953356748 10.1016/j.ygcen.2010.04.009
    • Duan C., Ren H., Gao S., Insulin-like growth factors (IGFs), IGF receptors, and IGF-binding proteins: roles in skeletal muscle growth and differentiation. General and Comparative Endocrinology 2010 167 3 344 351 2-s2.0-77953356748 10.1016/j.ygcen.2010.04.009
    • (2010) General and Comparative Endocrinology , vol.167 , Issue.3 , pp. 344-351
    • Duan, C.1    Ren, H.2    Gao, S.3
  • 135
    • 84887117034 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and regeneration: Interplay between the myogenic regulatory factors (MRFs) and insulin-like growth factors (IGFs) pathways
    • 2-s2.0-84875489909 10.1007/s00018-013-1330-4
    • Zanou N., Gailly P., Skeletal muscle hypertrophy and regeneration: interplay between the myogenic regulatory factors (MRFs) and insulin-like growth factors (IGFs) pathways. Cellular and Molecular Life Sciences 2013 70 21 4117 4130 2-s2.0-84875489909 10.1007/s00018-013-1330-4
    • (2013) Cellular and Molecular Life Sciences , vol.70 , Issue.21 , pp. 4117-4130
    • Zanou, N.1    Gailly, P.2
  • 136
    • 12244273711 scopus 로고    scopus 로고
    • Genome-wide examination of myoblast cell cycle withdrawal during differentiation
    • DOI 10.1002/dvdy.10200
    • Shen X., Collier J. M., Hlaing M., Zhang L., Delshad E. H., Bristow J., Bernstein H. S., Genome-wide examination of myoblast cell cycle withdrawal during differentiation. Developmental Dynamics 2003 226 1 128 138 2-s2.0-12244273711 10.1002/dvdy.10200 (Pubitemid 36043470)
    • (2003) Developmental Dynamics , vol.226 , Issue.1 , pp. 128-138
    • Shen, X.1    Collier, J.M.2    Hlaing, M.3    Zhang, L.4    Delshad, E.H.5    Bristow, J.6    Bernstein, H.S.7
  • 137
    • 58149471229 scopus 로고    scopus 로고
    • Down-regulation of Akt/mammalian target of rapamycin signaling pathway in response to myostatin overexpression in skeletal muscle
    • 2-s2.0-58149471229 10.1210/en.2008-0959
    • Amirouche A., Durieux A.-C., Banzet S., Koulmann N., Bonnefoy R., Mouret C., Bigard X., Peinnequin A., Freyssenet D., Down-regulation of Akt/mammalian target of rapamycin signaling pathway in response to myostatin overexpression in skeletal muscle. Endocrinology 2009 150 1 286 294 2-s2.0-58149471229 10.1210/en.2008-0959
    • (2009) Endocrinology , vol.150 , Issue.1 , pp. 286-294
    • Amirouche, A.1    Durieux, A.-C.2    Banzet, S.3    Koulmann, N.4    Bonnefoy, R.5    Mouret, C.6    Bigard, X.7    Peinnequin, A.8    Freyssenet, D.9
  • 139
    • 66749188280 scopus 로고    scopus 로고
    • Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size
    • 2-s2.0-66749188280 10.1152/ajpcell.00105.2009
    • Trendelenburg A. U., Meyer A., Rohner D., Boyle J., Hatakeyama S., Glass D. J., Myostatin reduces Akt/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size. American Journal of Physiology-Cell Physiology 2009 296 6 C1258 C1270 2-s2.0-66749188280 10.1152/ajpcell.00105.2009
    • (2009) American Journal of Physiology - Cell Physiology , vol.296 , Issue.6
    • Trendelenburg, A.U.1    Meyer, A.2    Rohner, D.3    Boyle, J.4    Hatakeyama, S.5    Glass, D.J.6
  • 140
    • 77952957076 scopus 로고    scopus 로고
    • Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice
    • 2-s2.0-77952957076 10.1016/j.febslet.2010.04.039
    • Lipina C., Kendall H., McPherron A. C., Taylor P. M., Hundal H. S., Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice. FEBS Letters 2010 584 11 2403 2408 2-s2.0-77952957076 10.1016/j.febslet.2010.04.039
    • (2010) FEBS Letters , vol.584 , Issue.11 , pp. 2403-2408
    • Lipina, C.1    Kendall, H.2    McPherron, A.C.3    Taylor, P.M.4    Hundal, H.S.5
  • 141
    • 27544500981 scopus 로고    scopus 로고
    • Growing roles for the mTOR pathway
    • DOI 10.1016/j.ceb.2005.09.009, PII S0955067405001481
    • Sarbassov D. D., Ali S. M., Sabatini D. M., Growing roles for the mTOR pathway. Current Opinion in Cell Biology 2005 17 6 596 603 2-s2.0-27544500981 10.1016/j.ceb.2005.09.009 (Pubitemid 41540408)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.6 , pp. 596-603
    • Sarbassov, D.D.1    Ali, S.M.2    Sabatini, D.M.3


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