메뉴 건너뛰기




Volumn 7, Issue , 2017, Pages

Proteomic signature of muscle fibre hyperplasia in response to faba bean intake in grass carp

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; FATTY ACID; FISH PROTEIN; PROTEOME;

EID: 85016832453     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep45950     Document Type: Article
Times cited : (80)

References (70)
  • 1
    • 85016768280 scopus 로고    scopus 로고
    • Food and agriculture organization of the united nations
    • Rome
    • Food and Agriculture Organization of the United Nations. "Aquaculture Big Numbers", http://www.fao.org/3/a-i6317e.pdf (Rome, 2016).
    • (2016) Aquaculture Big Numbers
  • 2
    • 0034729765 scopus 로고    scopus 로고
    • Effect of aquaculture on world fish supplies
    • Naylor, R. L. et al. Effect of aquaculture on world fish supplies. Nature 405, 1017-1024 (2000).
    • (2000) Nature , vol.405 , pp. 1017-1024
    • Naylor, R.L.1
  • 3
    • 84903898561 scopus 로고    scopus 로고
    • Molecular cloning of type i collagen cDNA and nutritional regulation of type i collagen mRNA expression in grass carp
    • Yu, E. M. et al. Molecular cloning of type I collagen cDNA and nutritional regulation of type I collagen mRNA expression in grass carp. J. Anim. Physiol. Anim. Nutr. 98, 755-765 (2014).
    • (2014) J. Anim. Physiol. Anim. Nutr , vol.98 , pp. 755-765
    • Yu, E.M.1
  • 4
    • 84918546340 scopus 로고    scopus 로고
    • Effect of feeding broad bean on growth and flesh quality of channel catfish
    • Zhu, Y. Q., Li, D. Y., Zhao, S. M. & Xiong, S. B. Effect of feeding broad bean on growth and flesh quality of channel catfish. J. Huazhong Agric. Univ. 31, 771-777 (2012).
    • (2012) J. Huazhong Agric. Univ , vol.31 , pp. 771-777
    • Zhu, Y.Q.1    Li, D.Y.2    Zhao, S.M.3    Xiong, S.B.4
  • 5
    • 85016777690 scopus 로고    scopus 로고
    • Effect of feeding broad bean on the growth, flesh quality and protease activity of allogynogenetic crucian carp
    • Li, B. S. et al. Effect of feeding broad bean on the growth, flesh quality and protease activity of allogynogenetic crucian carp. Chinese J. Anim. Nutr. 19, 631-635 (2007).
    • (2007) Chinese J. Anim. Nutr , vol.19 , pp. 631-635
    • Li, B.S.1
  • 6
    • 85016735822 scopus 로고    scopus 로고
    • Effect of feeding broad bean on muscle quality of tilapia
    • Lun, F., Leng, X. J., Meng, X. L. & Liu, X. M. Effect of feeding broad bean on muscle quality of tilapia. J. Shanghai Fish. Univers. 16, 83-86 (2007).
    • (2007) J. Shanghai Fish. Univers , vol.16 , pp. 83-86
    • Lun, F.1    Leng, X.J.2    Meng, X.L.3    Liu, X.M.4
  • 7
    • 55849136142 scopus 로고    scopus 로고
    • Effects of two protein sources and energy level of diet on the performance of young Marchigiana bulls.2. Meat quality
    • Cutrignelli, M. I. et al. Effects of two protein sources and energy level of diet on the performance of young Marchigiana bulls.2. Meat quality. Ital. J. Anim. Sci. 7, 271-285 (2008).
    • (2008) Ital. J. Anim. Sci , vol.7 , pp. 271-285
    • Cutrignelli, M.I.1
  • 8
    • 84918548814 scopus 로고    scopus 로고
    • Gene expression profiling of grass carp (Ctenopharyngodon idellus) and crisp grass carp
    • Yu, E. M. et al. Gene expression profiling of grass carp (Ctenopharyngodon idellus) and crisp grass carp. Int. J. Genomics. 2014, 639687, 10.1155/2014/639687 (2014).
    • (2014) Int. J. Genomics 2014 , pp. 639687
    • Yu, E.M.1
  • 9
    • 74849108510 scopus 로고    scopus 로고
    • Proteomic signature of muscle atrophy in rainbow trout
    • Salem, M., Kenney, P. B., Rexroad, C. E. & Yao, J. Proteomic signature of muscle atrophy in rainbow trout. J. Proteomics 73, 778-789 (2010).
    • (2010) J. Proteomics , vol.73 , pp. 778-789
    • Salem, M.1    Kenney, P.B.2    Rexroad, C.E.3    Yao, J.4
  • 10
    • 77449155964 scopus 로고    scopus 로고
    • Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes
    • Hwang, H. et al. Proteomics analysis of human skeletal muscle reveals novel abnormalities in obesity and type 2 diabetes. Diabetes 59, 33-42 (2010).
    • (2010) Diabetes , vol.59 , pp. 33-42
    • Hwang, H.1
  • 11
    • 21744437938 scopus 로고    scopus 로고
    • Differential proteome analysis of aging in rat skeletal muscle
    • Piec, I. et al. Differential proteome analysis of aging in rat skeletal muscle. FASEB J. 19, 1143-1145 (2005).
    • (2005) FASEB J , vol.19 , pp. 1143-1145
    • Piec, I.1
  • 12
    • 17044399794 scopus 로고    scopus 로고
    • Protein expression patterns in zebrafish skeletal muscle: Initial characterization and the effects of hypoxic exposure
    • Bosworth, C. A., Chou, C. W., Cole, R. B. & Rees, B. B. Protein expression patterns in zebrafish skeletal muscle: initial characterization and the effects of hypoxic exposure. Proteomics 5, 1362-1371 (2005).
    • (2005) Proteomics , vol.5 , pp. 1362-1371
    • Bosworth, C.A.1    Chou, C.W.2    Cole, R.B.3    Rees, B.B.4
  • 13
    • 84889680950 scopus 로고    scopus 로고
    • Muscle proteomics of the Indian major carp catla (Catla catla, Hamilton
    • Banerjee, S. et al. Muscle proteomics of the Indian major carp catla (Catla catla, Hamilton). J. Proteomics Bioinformatics 6, 252-263 (2013).
    • (2013) J. Proteomics Bioinformatics , vol.6 , pp. 252-263
    • Banerjee, S.1
  • 15
    • 83555162559 scopus 로고    scopus 로고
    • Proteome modifications of fingerling rainbow trout (Oncorhynchus mykiss) muscle as an effect of dietary nucleotides
    • Keyvanshokooh, S. & Tahmasebi-Kohyani, A. Proteome modifications of fingerling rainbow trout (Oncorhynchus mykiss) muscle as an effect of dietary nucleotides. Aquaculture 324, 79-84 (2012).
    • (2012) Aquaculture , vol.324 , pp. 79-84
    • Keyvanshokooh, S.1    Tahmasebi-Kohyani, A.2
  • 16
    • 84871731025 scopus 로고    scopus 로고
    • The sarcoplasmic fish proteome: Pathways, metabolic networks and potential bioactive peptides for nutritional inferences
    • Carrera, M., Cas, B. & Gallardo, J. M. The sarcoplasmic fish proteome: pathways, metabolic networks and potential bioactive peptides for nutritional inferences. J. Proteomics 78, 211-220 (2013)
    • (2013) J. Proteomics , vol.78 , pp. 211-220
    • Carrera, M.1    Cas, B.2    Gallardo, J.M.3
  • 17
    • 26844434498 scopus 로고    scopus 로고
    • The molecular regulation of exercised-induced muscle fibre hypertrophy in the common carp: Expression of MyoD, PCNA and components of the calcineurin-signalling pathway
    • Martin, C. I. & Johnston, I. A. The molecular regulation of exercised-induced muscle fibre hypertrophy in the common carp: expression of MyoD, PCNA and components of the calcineurin-signalling pathway. Comp. Biochem. Phys. B. 142, 324-334 (2005).
    • (2005) Comp. Biochem. Phys. B , vol.142 , pp. 324-334
    • Martin, C.I.1    Johnston, I.A.2
  • 18
    • 59149094476 scopus 로고    scopus 로고
    • Different changes in mastication between crisp grass carp (Ctenopharyngodon idellus C.et V) and grass carp (Ctenopharyngodon idellus) after heating: The relationship between texture and ultrastructure in muscle tissue
    • Lin, W. L., Zeng, Q. X. & Zhu, Z. W. Different changes in mastication between crisp grass carp (Ctenopharyngodon idellus C.et V) and grass carp (Ctenopharyngodon idellus) after heating: The relationship between texture and ultrastructure in muscle tissue. Food Res. Int. 42, 271-278 (2009).
    • (2009) Food Res. Int , vol.42 , pp. 271-278
    • Lin, W.L.1    Zeng, Q.X.2    Zhu, Z.W.3
  • 19
    • 84867869045 scopus 로고    scopus 로고
    • Quantitative iTRAQ LC-MS/MS proteomics reveals metabolic responses to biofuel ethanol in cyanobacterial Synechocystis sp. PCC 6803
    • Qiao, J. et al. Quantitative iTRAQ LC-MS/MS proteomics reveals metabolic responses to biofuel ethanol in cyanobacterial Synechocystis sp. PCC 6803. J. Proteome Res. 11, 5286-5300 (2012).
    • (2012) J. Proteome Res , vol.11 , pp. 5286-5300
    • Qiao, J.1
  • 20
    • 23944511338 scopus 로고    scopus 로고
    • Muscle cellularity and flesh quality of wild and farmed sea bass. Dicentrarchus labrax L
    • Periago, M. J. et al. Muscle cellularity and flesh quality of wild and farmed sea bass. Dicentrarchus labrax L. Aquaculture 249, 175-188 (2005).
    • (2005) Aquaculture , vol.249 , pp. 175-188
    • Periago, M.J.1
  • 21
    • 33646803435 scopus 로고    scopus 로고
    • Muscle and flesh quality traits in wild and farmed Atlantic salmon
    • Johnston, I. A. et al. Muscle and flesh quality traits in wild and farmed Atlantic salmon. Aquaculture 256, 323-336 (2006).
    • (2006) Aquaculture , vol.256 , pp. 323-336
    • Johnston, I.A.1
  • 22
    • 0029141850 scopus 로고
    • In vitro differentiation of myoblast from skeletal muscle of rainbow trout
    • Greenlee, A. R. et al. In vitro differentiation of myoblast from skeletal muscle of rainbow trout. J. Fish Biol. 46, 731-747 (1995).
    • (1995) J. Fish Biol , vol.46 , pp. 731-747
    • Greenlee, A.R.1
  • 23
    • 0030745789 scopus 로고    scopus 로고
    • Regeneration of skeletal muscle in two teleost fish: Sparus aurata and brachydanio rerio
    • Rowlerson, A., Radaelli, G., Mascarello, F. & Veggetti, A. Regeneration of skeletal muscle in two teleost fish: Sparus aurata and Brachydanio rerio. Cell Tissue Res. 289, 311-322 (1997).
    • (1997) Cell Tissue Res , vol.289 , pp. 311-322
    • Rowlerson, A.1    Radaelli, G.2    Mascarello, F.3    Veggetti, A.4
  • 24
    • 33847217997 scopus 로고    scopus 로고
    • Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle
    • Senetar, M. A., Moncman, C. L. & McCann, R. O. Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle. Cell Motil. Cytoskel. 64, 157-173 (2007).
    • (2007) Cell Motil. Cytoskel , vol.64 , pp. 157-173
    • Senetar, M.A.1    Moncman, C.L.2    McCann, R.O.3
  • 25
    • 67649970975 scopus 로고    scopus 로고
    • Regulation of slow and fast muscle myofibrillogenesis by Wnt/β-catenin and myostatinsignaling
    • Tee, J. M., Van Rooijen, C., Boonen, R. & Zivkovic, D. Regulation of slow and fast muscle myofibrillogenesis by Wnt/β-catenin and myostatinsignaling. PLoS One 4, e5880, http://dx.doi.org/10.1371/journal.pone.0005880 (2009).
    • (2009) PLoS One , vol.4 , pp. e5880
    • Tee, J.M.1    Van Rooijen, C.2    Boonen, R.3    Zivkovic, D.4
  • 26
    • 84979258025 scopus 로고    scopus 로고
    • Calcium-mediated regulation of recombinant hybrids of full-length Physarum myosin heavy chain with Physarum/scallop myosin light chains
    • Zhang, Y., Kawamichi, H., Kohama, K. & Nakamura, A. Calcium-mediated regulation of recombinant hybrids of full-length Physarum myosin heavy chain with Physarum/scallop myosin light chains. Acta. Bioch. Bioph. Sin. 48, 536-43 (2016).
    • (2016) Acta. Bioch. Bioph. Sin , vol.48 , pp. 536-543
    • Zhang, Y.1    Kawamichi, H.2    Kohama, K.3    Nakamura, A.4
  • 27
    • 84864468441 scopus 로고    scopus 로고
    • Calcium-dependent regulation of the motor activity of recombinant full-length Physarum myosin
    • Zhang, Y. et al. Calcium-dependent regulation of the motor activity of recombinant full-length Physarum myosin. J. Biochem. 152, 185-190 (2012).
    • (2012) J. Biochem , vol.152 , pp. 185-190
    • Zhang, Y.1
  • 28
    • 84864241713 scopus 로고    scopus 로고
    • Structure of the rigor actin-Tropomyosin-myosin complex
    • Behrmann, E. et al. Structure of the rigor actin-Tropomyosin-myosin complex. Cell 150, 327-338 (2012).
    • (2012) Cell , vol.150 , pp. 327-338
    • Behrmann, E.1
  • 29
    • 84855161243 scopus 로고    scopus 로고
    • Myosin binding protein-C: A regulator of actomyosin interaction in striated muscle
    • Ackermann, M. A. & Kontrogianni-Konstantopoulos, A. Myosin binding protein-C: A regulator of actomyosin interaction in striated muscle. J. Biomed. Biotechnol. 2011, 636403; 10.1155/2011/636403 (2011).
    • (2011) J. Biomed. Biotechnol 2011 , pp. 636403
    • Ackermann, M.A.1    Kontrogianni-Konstantopoulos, A.2
  • 30
    • 0018126953 scopus 로고
    • The binding of skeletal muscle C-protein to F-Actin, and its relation to the interaction of actin with myosin subfragment-1
    • Moos, C. et al. The binding of skeletal muscle C-protein to F-Actin, and its relation to the interaction of actin with myosin subfragment-1. J. Mol. Biol. 124, 571-586 (1978).
    • (1978) J. Mol. Biol , vol.124 , pp. 571-586
    • Moos, C.1
  • 31
    • 78751475039 scopus 로고    scopus 로고
    • Myosin binding protein c interaction with actin characterization and mapping of the binding site
    • Rybakova, I. N., Greaser, M. L. & Moss, R. L. Myosin binding protein c interaction with actin characterization and mapping of the binding site. J. Biol. Chem. 286, 2008-2016 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 2008-2016
    • Rybakova, I.N.1    Greaser, M.L.2    Moss, R.L.3
  • 32
    • 0017826080 scopus 로고
    • The interaction of C-protein with heavy meromyosin and subfragment-2
    • Starr, R. & Offer, G. The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem. J. 171, 813-816 (1978).
    • (1978) Biochem. J , vol.171 , pp. 813-816
    • Starr, R.1    Offer, G.2
  • 33
    • 0029812703 scopus 로고    scopus 로고
    • Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle
    • Weisberg, A. & Winegrad, S. Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. P. Natl Acad. Sci. USA 93, 8999-9003 (1996).
    • (1996) P. Natl Acad. Sci USA , vol.93 , pp. 8999-9003
    • Weisberg, A.1    Winegrad, S.2
  • 34
    • 85016824546 scopus 로고    scopus 로고
    • The functional role of the microtubule/microfilament cytoskeleton in the regulation of pulmonary vascular endothelial barrier
    • Alieva, I. B. & Verin, A. D. The functional role of the microtubule/microfilament cytoskeleton in the regulation of pulmonary vascular endothelial barrier. Endothel. Cytoskel. 6, 116-145 (2013).
    • (2013) Endothel. Cytoskel , vol.6 , pp. 116-145
    • Alieva, I.B.1    Verin, A.D.2
  • 35
    • 0027408247 scopus 로고
    • Identification of a ten-Amino acid proline-rich SH3 binding site
    • Ren, R., Mayer, B. J., Cicchetti, P. & Baltimore, D. Identification of a ten-Amino acid proline-rich SH3 binding site. Science 259, 1157-1161 (1993).
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 36
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: Implications for the signaling and assembly role of titin and nebulin
    • Ma, K. & Wang, K. Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett. 532, 273-278 (2002).
    • (2002) FEBS Lett , vol.532 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 37
    • 0028283285 scopus 로고
    • The muscle Z band: Lessons in stress management
    • Vigoreaux, J. O. The muscle Z band: lessons in stress management. J. Muscle Res. Cell Motil. 15, 237-255 (1994).
    • (1994) J. Muscle Res. Cell Motil , vol.15 , pp. 237-255
    • Vigoreaux, J.O.1
  • 38
    • 85016785656 scopus 로고    scopus 로고
    • The comparison of grass carp muscle nutrition composition and glucose-6-phosphate dehydrogenase content in red blood cells before and after embrittlement
    • Kuang, X. M. et al. The comparison of grass carp muscle nutrition composition and glucose-6-phosphate dehydrogenase content in red blood cells before and after embrittlement. Nat. Sci. J. Hainan Univers. 22, 258-261 (2004).
    • (2004) Nat. Sci. J. Hainan Univers , vol.22 , pp. 258-261
    • Kuang, X.M.1
  • 40
    • 37549026846 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency
    • Cappellini, M. D. & Fiorelli, G. Glucose-6-phosphate dehydrogenase deficiency. Lancet 371, 64-74 (2008).
    • (2008) Lancet , vol.371 , pp. 64-74
    • Cappellini, M.D.1    Fiorelli, G.2
  • 41
    • 0030908893 scopus 로고    scopus 로고
    • The two isoenzymes for yeast NAD+dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation
    • Ansell, R. et al. The two isoenzymes for yeast NAD+dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation. EMBO J. 16, 2179-2187 (1997).
    • (1997) EMBO J , vol.16 , pp. 2179-2187
    • Ansell, R.1
  • 42
    • 0032147165 scopus 로고    scopus 로고
    • The biological significance of plasmalogens in defense against oxidative damage
    • Brosche, T. & Platt, D. The biological significance of plasmalogens in defense against oxidative damage. Exp. Gerontol. 33, 363-369 (1998).
    • (1998) Exp. Gerontol , vol.33 , pp. 363-369
    • Brosche, T.1    Platt, D.2
  • 43
    • 84978815302 scopus 로고    scopus 로고
    • From the "old NEC" to the "new NECs
    • Puddu, M. et al. From the "old NEC" to the "new NECs". J. Pediatric Neonatal Individ. Med. 3, e030245, doi: 10.7363/030245 (2014).
    • (2014) J. Pediatric Neonatal Individ. Med , vol.3 , pp. e030245
    • Puddu, M.1
  • 44
    • 0028828562 scopus 로고
    • Heme degradation in the presence of glutathione A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells
    • Atamna, H. & Ginsburg, H. Heme degradation in the presence of glutathione A proposed mechanism to account for the high levels of non-heme iron found in the membranes of hemoglobinopathic red blood cells. J. Biol. Chem. 270, 24876-24883 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 24876-24883
    • Atamna, H.1    Ginsburg, H.2
  • 45
    • 0035425385 scopus 로고    scopus 로고
    • Antinutritional factors present in plant-derived alternate fish feed ingredients and their effects in fish
    • Francis, G., Makkar, H. P. S. & Becker, K. Antinutritional factors present in plant-derived alternate fish feed ingredients and their effects in fish. Aquaculture 199, 197-227 (2001).
    • (2001) Aquaculture , vol.199 , pp. 197-227
    • Francis, G.1    Makkar, H.P.S.2    Becker, K.3
  • 46
    • 85016733797 scopus 로고    scopus 로고
    • Preliminary study on the ecology, physiology and pathology of crisped grass carp (Ctenopharyngodon idellus C.et v)
    • Tan, Q. K. & Li, H. S. Preliminary study on the ecology, physiology and pathology of crisped grass carp (Ctenopharyngodon idellus C.et V). Acta Ecol. Sinica. 26, 2749-2756 (2006).
    • (2006) Acta Ecol. Sinica , vol.26 , pp. 2749-2756
    • Tan, Q.K.1    Li, H.S.2
  • 47
    • 9344243516 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility
    • Miki, K. et al. Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. P. Natl Acad. Sci. USA 101, 16501-16506 (2004).
    • (2004) P. Natl Acad. Sci USA , vol.101 , pp. 16501-16506
    • Miki, K.1
  • 48
    • 84862650731 scopus 로고    scopus 로고
    • Gene expression profiling of soft and firm Atlantic salmon fillet
    • Larsson, T. et al. Gene expression profiling of soft and firm Atlantic salmon fillet. PLoS One 7, e39219, http://dx.doi.org/10.1371/journal.pone.0039219 (2012).
    • (2012) PLoS One , vol.7 , pp. e39219
    • Larsson, T.1
  • 49
    • 84947246273 scopus 로고    scopus 로고
    • Effects of muscle fibre type on glycolytic potential and meat quality traits in different Tibetan pig muscles and their association with glycolysis-related gene expression
    • Shen, L. Y. et al. Effects of muscle fibre type on glycolytic potential and meat quality traits in different Tibetan pig muscles and their association with glycolysis-related gene expression. Genet. Mol. Res. 14, 14366-14378 (2015).
    • (2015) Genet. Mol. Res , vol.14 , pp. 14366-14378
    • Shen, L.Y.1
  • 50
    • 0034002793 scopus 로고    scopus 로고
    • Fatty-Acid synthase and human cancer: New perspectives on its role in tumor biology
    • Kuhajda, F. P. Fatty-Acid synthase and human cancer: new perspectives on its role in tumor biology. Nutrition 16, 202-208 (2000).
    • (2000) Nutrition , vol.16 , pp. 202-208
    • Kuhajda, F.P.1
  • 51
    • 65949095803 scopus 로고    scopus 로고
    • Autophagy regulates lipid metabolism
    • Singh, R. et al. Autophagy regulates lipid metabolism. Nature 458, 1131-1135 (2009).
    • (2009) Nature , vol.458 , pp. 1131-1135
    • Singh, R.1
  • 52
    • 2142817149 scopus 로고    scopus 로고
    • Biotechnological production and applications of the φ-3 polyunsaturated fatty acid docosahexaenoic acid
    • Sijtsma, L. & De Swaaf, M. E. Biotechnological production and applications of the φ-3 polyunsaturated fatty acid docosahexaenoic acid. Appl. Microbiol. Biot. 64, 146-153 (2004).
    • (2004) Appl. Microbiol. Biot , vol.64 , pp. 146-153
    • Sijtsma, L.1    De Swaaf, M.E.2
  • 53
    • 43249086785 scopus 로고    scopus 로고
    • Mammalian long-chain acyl-CoA synthetases
    • Soupene, E. & Kuypers, F. A. Mammalian long-chain acyl-CoA synthetases. Exp. Biol. Med. 233, 507-521 (2008).
    • (2008) Exp. Biol. Med , vol.233 , pp. 507-521
    • Soupene, E.1    Kuypers, F.A.2
  • 54
    • 0032004229 scopus 로고    scopus 로고
    • 2, 4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation
    • Hayashi, M., Toriyama, K., Kondo, M. & Nishimura, M. 2, 4-Dichlorophenoxybutyric acid-resistant mutants of Arabidopsis have defects in glyoxysomal fatty acid β-oxidation. Plant Cell 10, 183-195 (1998).
    • (1998) Plant Cell , vol.10 , pp. 183-195
    • Hayashi, M.1    Toriyama, K.2    Kondo, M.3    Nishimura, M.4
  • 55
    • 9144271149 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-Activated receptor δ induces fatty acid β-oxidation in skeletal muscle and attenuates metabolic syndrome
    • Tanaka, T. et al. Activation of peroxisome proliferator-Activated receptor δ induces fatty acid β-oxidation in skeletal muscle and attenuates metabolic syndrome. P. Natl Acad. Sci. USA 100, 15924-15929 (2003).
    • (2003) P. Natl Acad. Sci USA , vol.100 , pp. 15924-15929
    • Tanaka, T.1
  • 56
    • 0032940782 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis in plants: Carbon partitioning within the cytoplasmic pathway
    • Newman, J. D. & Chappell, J. Isoprenoid biosynthesis in plants: carbon partitioning within the cytoplasmic pathway. Crit. Rev. Biochem. Mol. 34, 95-106 (1999).
    • (1999) Crit. Rev. Biochem. Mol , vol.34 , pp. 95-106
    • Newman, J.D.1    Chappell, J.2
  • 57
    • 0029067630 scopus 로고
    • Phytanic acid oxidation in man: Identification of a new enzyme catalysing the formation of 2-ketophytanic acid from 2-hydroxyphytanic acid and its deficiency in the Zellweger syndrome
    • Wanders, R. J. A. et al. Phytanic acid oxidation in man: identification of a new enzyme catalysing the formation of 2-ketophytanic acid from 2-hydroxyphytanic acid and its deficiency in the Zellweger syndrome. J. Inherit. Metab. Dis. 18, 201-203 (1995).
    • (1995) J. Inherit. Metab. Dis , vol.18 , pp. 201-203
    • Wanders, R.J.A.1
  • 58
    • 0018637437 scopus 로고
    • Fatty acid α-hydroxylation and its relation to myelination
    • Kishimoto, Y., Akanuma, H. & Singh, I. Fatty acid α-hydroxylation and its relation to myelination. Mol. Cell. Biochem. 28, 93-105 (1979).
    • (1979) Mol. Cell. Biochem , vol.28 , pp. 93-105
    • Kishimoto, Y.1    Akanuma, H.2    Singh, I.3
  • 59
    • 84984777129 scopus 로고    scopus 로고
    • Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene
    • Jansen, G. A. et al. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat. Genet. 17, 190-193 (1997).
    • (1997) Nat. Genet , vol.17 , pp. 190-193
    • Jansen, G.A.1
  • 60
    • 0034725053 scopus 로고    scopus 로고
    • Identification and characterization of haox1, haox2, and haox3, three human peroxisomal 2-hydroxy acid oxidases
    • Jones, J. M., Morrell, J. C. & Gould, S. J. Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases. J. Biol. Chem. 275, 12590-12597 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 12590-12597
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.J.3
  • 61
    • 84893904500 scopus 로고    scopus 로고
    • Comparison and evaluation of nutrition composition in muscle of grass carp Ctenopharyngodon idellus fed with broad bean and common compound feed
    • Liu, B. H. et al. Comparison and evaluation of nutrition composition in muscle of grass carp Ctenopharyngodon idellus fed with broad bean and common compound feed. South China Fish. Sci. 7, 58-65 (2011).
    • (2011) South China Fish. Sci , vol.7 , pp. 58-65
    • Liu, B.H.1
  • 63
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee, S. J. & Alexandra, C. M. Regulation of myostatin activity and muscle growth. P. Natl Acad. Sci. 98, 9306-9311 (2001).
    • (2001) P. Natl Acad. Sci , vol.98 , pp. 9306-9311
    • Lee, S.J.1    Alexandra, C.M.2
  • 64
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: A hub for protein information
    • The UniProt Consortium
    • The UniProt Consortium. UniProt: A hub for protein information. Nucleic Acids Res. 43, 204-212 (2015).
    • (2015) Nucleic Acids Res , vol.43 , pp. 204-212
  • 65
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • Ashburner, M. et al. Gene ontology: Tool for the unification of biology. Nat. Genet. 25, 25-29 (2000).
    • (2000) Nat. Genet , vol.25 , pp. 25-29
    • Ashburner, M.1
  • 67
    • 84941051170 scopus 로고    scopus 로고
    • STRING v10: Protein-protein interaction networks, integrated over the tree of life
    • Szklarczyk, D. et al. STRING v10: protein-protein interaction networks, integrated over the tree of life. Nucleic Acids Res. 43, 447-452 (2015).
    • (2015) Nucleic Acids Res , vol.43 , pp. 447-452
    • Szklarczyk, D.1
  • 68
    • 80053463904 scopus 로고    scopus 로고
    • Medusa: A tool for exploring and clustering biological networks
    • Pavlopoulos, G. A. et al. Medusa: A tool for exploring and clustering biological networks. BMC Res. Notes. 4, 384, 10.1186/1756-0500-4-384 (2011).
    • (2011) BMC Res. Notes , vol.4 , pp. 384
    • Pavlopoulos, G.A.1
  • 69
    • 80054760368 scopus 로고    scopus 로고
    • Fiber types in mammalian skeletal muscles
    • Schiaffino, S. & Reggiani, C. Fiber types in mammalian skeletal muscles. Physiol. Rev. 91, 1447-1531 (2011).
    • (2011) Physiol. Rev , vol.91 , pp. 1447-1531
    • Schiaffino, S.1    Reggiani, C.2
  • 70
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: Sarcomere anchor for structure and signalling
    • Luther, P. K. The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. J. Muscle Res. Cell M. 30, 171-185 (2009).
    • (2009) J. Muscle Res. Cell M , vol.30 , pp. 171-185
    • Luther, P.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.