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Volumn 29, Issue 3, 2012, Pages 461-471

SILAM for quantitative proteomics of liver Akt1/PKBα after burn injury

Author keywords

Akt1 PKB ; Burn injury; MS MS; SILAM

Indexed keywords

ALBUMIN; AMYLOID P COMPONENT; CYSTINE; LEUCINE; LIVER EXTRACT; PROTEIN KINASE B; PROTEIN KINASE B ALPHA; UNCLASSIFIED DRUG;

EID: 84856193454     PISSN: 11073756     EISSN: 1791244X     Source Type: Journal    
DOI: 10.3892/ijmm.2011.861     Document Type: Article
Times cited : (4)

References (63)
  • 1
    • 16344389629 scopus 로고    scopus 로고
    • Metabolic labeling of proteins for proteomics
    • DOI 10.1074/mcp.R400010-MCP200
    • Beynon RJ and Pratt JM: Metabolic labeling of proteins for proteomics. Mol Cell Proteomics 4: 857-872, 2005. (Pubitemid 41309145)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.7 , pp. 857-872
    • Beynon, R.J.1    Pratt, J.M.2
  • 2
    • 40649095957 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture
    • DOI 10.1038/nprot.2008.2, PII NPROT.2008.2
    • Harsha HC, Molina H and Pandey A: Quantitative proteomics using stable isotope labeling with amino acids in cell culture. Nat Protoc 3: 505-516, 2008. (Pubitemid 351372235)
    • (2008) Nature Protocols , vol.3 , Issue.3 , pp. 505-516
    • Harsha, H.C.1    Molina, H.2    Pandey, A.3
  • 3
    • 16344363793 scopus 로고    scopus 로고
    • The dynamics of the proteome: Strategies for measuring protein turnover on a proteome-wide scale
    • Beynon RJ: The dynamics of the proteome: strategies for measuring protein turnover on a proteome-wide scale. Brief Funct Genomic Proteomic 3: 382-390, 2005.
    • (2005) Brief Funct Genomic Proteomic , vol.3 , pp. 382-390
    • Beynon, R.J.1
  • 4
    • 51749107767 scopus 로고    scopus 로고
    • Quantitative mass spectrometry as a tool for nutritional proteomics
    • Moresco JJ, Dong MQ and Yates JR: Quantitative mass spectrometry as a tool for nutritional proteomics. Am J Clin Nutr 88: 597-604, 2008.
    • (2008) Am J Clin Nutr , vol.88 , pp. 597-604
    • Moresco, J.J.1    Dong, M.Q.2    Yates, J.R.3
  • 7
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • Doherty MK, Whitehead C, McCormack H, Gaskell SJ and Beynon-RJ: Proteome dynamics in complex organisms: using stable isotopes to monitor individual protein turnover rates. Proteomics 5: 522-533, 2005.
    • (2005) Proteomics , vol.5 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 9
    • 4444346217 scopus 로고    scopus 로고
    • Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis
    • Wu CC, MacCoss MJ, Howell KE, Matthews DE and Yates-JR-III: Metabolic labeling of mammalian organisms with stable isotopes for quantitative proteomic analysis. Anal Chem 76: 4951-4959, 2004.
    • (2004) Anal Chem , vol.76 , pp. 4951-4959
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Matthews, D.E.4    Yates III, J.R.5
  • 10
    • 47549099572 scopus 로고    scopus 로고
    • SILAC Mouse for Quantitative Proteomics Uncovers Kindlin-3 as an Essential Factor for Red Blood Cell Function
    • DOI 10.1016/j.cell.2008.05.033, PII S0092867408006958
    • Kruger M, Moser M, Ussar S, Thievessen I, Luber CA, Former-F, Schmidt-S, Zanivan S, Fassler R and Mann M: SILAC mouse for quantitative proteomics uncovers kindling-3 as an essential factor for red blood cell function. Cell 134: 353-364, 2008. (Pubitemid 352010327)
    • (2008) Cell , vol.134 , Issue.2 , pp. 353-364
    • Kruger, M.1    Moser, M.2    Ussar, S.3    Thievessen, I.4    Luber, C.A.5    Forner, F.6    Schmidt, S.7    Zanivan, S.8    Fassler, R.9    Mann, M.10
  • 12
    • 34249650777 scopus 로고    scopus 로고
    • Comparison of full versus partial metabolic labeling for quantitative proteomics analysis in Arabidopsis thaliana
    • Huttlin EL, Hegeman AD, Harms AC and Sussman-MR: Comparison of full versus partial metabolic labeling for quantitative proteomics analysis in Arabidopsis thaliana. Mol Cell Proteomics 6: 860-881, 2007.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 860-881
    • Huttlin, E.L.1    Hegeman, A.D.2    Harms, A.C.3    Sussman, M.R.4
  • 14
    • 58149385852 scopus 로고    scopus 로고
    • Quantitative analysis of brain nuclear phosphoproteins identifies developmentally regulated phosphorylation events
    • Liao L, McClatchy DB, Park SK, Xu T, Lu B and Yates JR-III: Quantitative analysis of brain nuclear phosphoproteins identifies developmentally regulated phosphorylation events. J Proteome Res 7: 4743-4755, 2008.
    • (2008) J Proteome Res , vol.7 , pp. 4743-4755
    • Liao, L.1    McClatchy, D.B.2    Park, S.K.3    Xu, T.4    Lu, B.5    Yates III, J.R.6
  • 15
    • 48849097164 scopus 로고    scopus 로고
    • Quantitative proteomics as a new piece of the systems biology puzzle
    • Bachi A and Bonaldi T: Quantitative proteomics as a new piece of the systems biology puzzle. J Proteomics 71: 357-367, 2008.
    • (2008) J Proteomics , vol.71 , pp. 357-367
    • Bachi, A.1    Bonaldi, T.2
  • 16
    • 0036324823 scopus 로고    scopus 로고
    • Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients
    • Biolo G, Fleming RY, Maggi SP, Nguyen TT, Herndon DN and Wolfe-RR: Inverse regulation of protein turnover and amino acid transport in skeletal muscle of hypercatabolic patients. J Clin Endocrinol Metab 87: 3378-3384, 2002.
    • (2002) J Clin Endocrinol Metab , vol.87 , pp. 3378-3384
    • Biolo, G.1    Fleming, R.Y.2    Maggi, S.P.3    Nguyen, T.T.4    Herndon, D.N.5    Wolfe, R.R.6
  • 18
    • 0040973209 scopus 로고    scopus 로고
    • Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS- 2 in IRS-1-deficient cells
    • Bruning JC, Winnay J, Cheatham B and Kahn CR: Differential signaling by insulin receptor substrate 1 (IRS-1) and IRS-2 in IRS-1-deficient cells. Mol Cell Biol 17: 1513-1521, 1997. (Pubitemid 27097381)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.3 , pp. 1513-1521
    • Bruning, J.C.1    Winnay, J.2    Cheatham, B.3    Kahn, C.R.4
  • 19
    • 0034055787 scopus 로고    scopus 로고
    • Insulin resistance in fat cells from obese Zucker rats - Evidence for an impaired activation and translocation of protein kinase B and glucose transporter 4
    • Carvalho E, Rondinone C and Smith U: Insulin resistance in fat cells from obese Zucker rats - evidence for an impaired activation and translocation of protein kinase B and glucose transporter 4. Mol Cell Biochem 206: 7-16, 2000. (Pubitemid 30246501)
    • (2000) Molecular and Cellular Biochemistry , vol.206 , Issue.1-2 , pp. 7-16
    • Carvalho, E.1    Rondinone, C.2    Smith, U.3
  • 20
    • 0028032895 scopus 로고
    • Alternative pathway of insulin signalling in mice with targeted disruption of the IRS-1 gene
    • DOI 10.1038/372186a0
    • Araki E, Lipes MA, Patti ME, Bruning JC, Haag B, Johnson-RS and Kahn CR: Alternative pathway of insulin signaling in mice with targeted disruption of the IRS-1 gene. Nature 372: 186-190, 1994. (Pubitemid 24347839)
    • (1994) Nature , vol.372 , Issue.6502 , pp. 186-190
    • Araki, E.1    Lipes, M.A.2    Patti, M.-E.3    Bruning, J.C.4    Haag III, B.5    Johnson, R.S.6    Kahn, C.R.7
  • 22
    • 16644388074 scopus 로고    scopus 로고
    • Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue
    • Carter EA, Burks D, Fischman AJ, White M and Tompkins-RG: Insulin resistance in thermally-injured rats is associated with post-receptor alterations in skeletal muscle, liver and adipose tissue. Int J Mol Med 14: 653-658, 2004.
    • (2004) Int J Mol Med , vol.14 , pp. 653-658
    • Carter, E.A.1    Burks, D.2    Fischman, A.J.3    White, M.4    Tompkins, R.G.5
  • 23
    • 0036213392 scopus 로고    scopus 로고
    • Insulin: A wonder drug in the critically ill?
    • Groeneveld AB, Beishuizen A and Visser FC: Insulin: a wonder drug in the critically ill? Critical Care 6: 102-105, 2002. (Pubitemid 34296333)
    • (2002) Critical Care , vol.6 , Issue.2 , pp. 102-105
    • Groeneveld, A.B.J.1    Beishuizen, A.2    Visser, F.C.3
  • 24
  • 25
    • 0344305782 scopus 로고    scopus 로고
    • Insulin signaling in health and disease
    • White MF: Insulin signaling in health and disease. Science 302: 1710-1711, 2003.
    • (2003) Science , vol.302 , pp. 1710-1711
    • White, M.F.1
  • 26
    • 26444436274 scopus 로고    scopus 로고
    • Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: Role of IRS phosphorylation
    • Zhang Q, Carter EA, Ma BY, White M, Fischman AJ and Tompkins-RG: Molecular mechanism(s) of burn-induced insulin resistance in murine skeletal muscle: role of IRS phosphorylation. Life Sci 77: 3068-3077, 2005.
    • (2005) Life Sci , vol.77 , pp. 3068-3077
    • Zhang, Q.1    Carter, E.A.2    Ma, B.Y.3    White, M.4    Fischman, A.J.5    Tompkins, R.G.6
  • 27
    • 27844435600 scopus 로고    scopus 로고
    • Minireview: Recent developments in the regulation of glucose transporter-4 traffic: New signals, locations, and partners
    • DOI 10.1210/en.2005-0850
    • Ishiki M and Klip A: Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners. Endocrinology 146: 5071-5078, 2005. (Pubitemid 41653019)
    • (2005) Endocrinology , vol.146 , Issue.12 , pp. 5071-5078
    • Ishiki, M.1    Klip, A.2
  • 29
    • 17144395975 scopus 로고    scopus 로고
    • The activation of Akt/PKB signaling pathway and cell survival
    • Song G, Quyang G and Bao S: The activation of Akt/PKB signaling pathway and cell survival. J Cell Mol Med 9: 59-71, 2005.
    • (2005) J Cell Mol Med , vol.9 , pp. 59-71
    • Song, G.1    Quyang, G.2    Bao, S.3
  • 30
    • 33745480146 scopus 로고    scopus 로고
    • A new way to burn fat
    • DOI 10.1126/science.1130476
    • Neels JG and Olefsky JM: A new way to burn fat. Science 312: 1756-1758, 2006. (Pubitemid 43962882)
    • (2006) Science , vol.312 , Issue.5781 , pp. 1756-1758
    • Neels, J.G.1    Olefsky, J.M.2
  • 31
    • 13444265870 scopus 로고    scopus 로고
    • Another role for celebrity, Akt and insulin resistance
    • Tian R: Another role for celebrity, Akt and insulin resistance. Circ Res 96: 139-140, 2006.
    • (2006) Circ Res , vol.96 , pp. 139-140
    • Tian, R.1
  • 32
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin responses?
    • Lawlor MA and Alessi DR: PKB/Akt: a key mediator of cell proliferation, survival and insulin responses? J Cell Sci 114: 2903-2910, 2001. (Pubitemid 32821530)
    • (2001) Journal of Cell Science , vol.114 , Issue.16 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 33
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • DOI 10.1016/S1097-2765(02)00550-6
    • Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings-BA and Barford D: Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation. Mol Cell 9: 1227-1240, 2002. (Pubitemid 34722302)
    • (2002) Molecular Cell , vol.9 , Issue.6 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 34
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase-B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J, Cron P, Good VM, Thompson V, Hemmings BA and Barford-D: Crystal structure of an activated Akt/protein kinase-B ternary complex with GSK3-peptide and AMP-PNP. Nat Structure Biol 9: 940-944, 2002.
    • (2002) Nat Structure Biol , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 35
    • 6444244485 scopus 로고    scopus 로고
    • Crystal structure of an inactive Akt2 kinase domain
    • DOI 10.1016/S0969-2126(02)00937-1, PII S0969212602009371
    • Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao-H and Zhu-X: Crystal structure of an inactive Akt2 kinase domain. Structure 11: 21-30, 2003. (Pubitemid 36071494)
    • (2003) Structure , vol.11 , Issue.1 , pp. 21-30
    • Huang, X.1    Begley, M.2    Morgenstern, K.A.3    Gu, Y.4    Rose, P.5    Zhao, H.6    Zhu, X.7
  • 36
    • 27844553839 scopus 로고    scopus 로고
    • AKT crystal structure and AKT-specific inhibitors
    • DOI 10.1038/sj.onc.1209087, PII 1209087
    • Kumar CC and Madison V: Akt crystal structure and Akt-specific inhibitors. Oncogene 24: 7493-7501, 2005. (Pubitemid 41637989)
    • (2005) Oncogene , vol.24 , Issue.50 , pp. 7493-7501
    • Kumar, C.C.1    Madison, V.2
  • 38
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signaling: AKTion on multiple fronts
    • Brazil DP, Yang ZZ and Hemmings BA: Advances in protein kinase B signaling: AKTion on multiple fronts. Trends Biochem Sci 29: 233-242, 2005.
    • (2005) Trends Biochem Sci , vol.29 , pp. 233-242
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 39
    • 0036849331 scopus 로고    scopus 로고
    • PKB binding proteins: Getting in on the Akt
    • DOI 10.1016/S0092-8674(02)01083-8
    • Brazil DP, Park J and Hemmings BA: PKB binding proteins: getting in on the Akt. Cell 111: 293-303, 2002. (Pubitemid 35341386)
    • (2002) Cell , vol.111 , Issue.3 , pp. 293-303
    • Brazil, D.P.1    Park, J.2    Hemmings, B.A.3
  • 40
    • 33745610132 scopus 로고    scopus 로고
    • Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry
    • DOI 10.1074/mcp.M600026-MCP200
    • Huang BX and Kim HY: Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry. Mol Cellular Proteomics 5: 1045-1053, 2006. (Pubitemid 43985929)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.6 , pp. 1045-1053
    • Huang, B.X.1    Kim, H.-Y.2
  • 42
    • 15944378147 scopus 로고    scopus 로고
    • S-nitrosation of the insulin receptor, insulin receptor substrate 1, and protein kinase B/Akt: A novel mechanism of insulin resistance
    • DOI 10.2337/diabetes.54.4.959
    • Carvalho-Filho MA, Ueno M, Hirabara SM, Seabra-AB, Carvalheira-JB, de Oliveira MG, Velloso LA, Curi R and Saad-MJ: S-nitrosation of the insulin receptor, insulin receptor substrate 1, and protein kinase B/Akt: a novel mechanism of insulin resistance. Diabetes 54: 959-967, 2005. (Pubitemid 40446309)
    • (2005) Diabetes , vol.54 , Issue.4 , pp. 959-967
    • Carvalho-Filho, M.A.1    Ueno, M.2    Hirabara, S.M.3    Seabra, A.B.4    Carvalheira, J.B.C.5    De Oliveira, M.G.6    Velloso, L.A.7    Curi, R.8    Saad, M.J.A.9
  • 43
    • 14844300857 scopus 로고    scopus 로고
    • S-Nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance
    • Yasukawa T, Tokunaga, E, Ota H, Sugita H, Martyn JA and Kaneki-M: S-Nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance. J Biol Chem 280: 7511-7518, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 7511-7518
    • Yasukawa, T.1    Tokunaga, E.2    Ota, H.3    Sugita, H.4    Martyn, J.A.5    Kaneki, M.6
  • 45
    • 1242263882 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates
    • DOI 10.1023/B:JNMR.0000013836.62154.c2
    • Auguin D, Barthe P, Auge-Senegas MT, Stern MH, Noguchi-M and Roumestand C: Solution structure and backbone dynamics of the Pleckstrin homology domain of the human protein kinase B (PKB/Akt). Interaction with inositol phosphates. J Biomol NMR 28: 137-155, 2004. (Pubitemid 38232793)
    • (2004) Journal of Biomolecular NMR , vol.28 , Issue.2 , pp. 137-155
    • Auguin, D.1    Barthe, P.2    Auge-Senegas, M.-T.3    Stern, M.-H.4    Noguchi, M.5    Roumestand, C.6
  • 46
    • 0346749513 scopus 로고    scopus 로고
    • Glotaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata H, Ihara Y, Nakamura H, Yodoi J, Sumikawa K and Kondo-T: Glotaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 278: 50226-50233, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 47
    • 19544387641 scopus 로고    scopus 로고
    • micro
    • DOI 10.1002/jms.826
    • Lu XM, Lu M, Fischman AJ and Tompkins RG: A new approach for sequencing human IRS1 phosphotyrosine-containing peptides using CapLC-Q-TOF micro mass spectrometry. J Mass Spectrom 40: 599-607, 2005. (Pubitemid 40733317)
    • (2005) Journal of Mass Spectrometry , vol.40 , Issue.5 , pp. 599-607
    • Lu, X.-M.1    Lu, M.Y.2    Fischman, A.J.3    Tompkins, R.G.4
  • 48
    • 25144521807 scopus 로고    scopus 로고
    • micro mass spectrometry
    • DOI 10.1002/jms.885
    • Lu XM, Lu M, Tompkins RG and Fischman AJ: Site-specific detection of S-nitrosylated PKBa/Akt1 from rat soleus muscle using CapLC-Q-TOF micro mass spectrometry. J Mass Spectrom 40: 1140-1148, 2005. (Pubitemid 41337242)
    • (2005) Journal of Mass Spectrometry , vol.40 , Issue.9 , pp. 1140-1148
    • Lu, X.-M.1    Lu, M.2    Tompkins, R.G.3    Fischman, A.J.4
  • 50
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for detection of S-nitrosylated proteins
    • Jaffrey SR and Snyder SH: The biotin switch method for detection of S-nitrosylated proteins. Science STKE 86: 1-9, 2001.
    • (2001) Science STKE , vol.86 , pp. 1-9
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 52
    • 32244445145 scopus 로고    scopus 로고
    • SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures
    • Hao G, Derakhshan B, Shi L, Campagne F and Gross-SS: SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures. Proc Natl Acad Sci USA 103: 1012-1017, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1012-1017
    • Hao, G.1    Derakhshan, B.2    Shi, L.3    Campagne, F.4    Gross, S.S.5
  • 54
    • 1042267391 scopus 로고    scopus 로고
    • Detection and proteomic identification of S-nitrosylated proteins in endothelial cells
    • DOI 10.1016/j.abb.2003.12.006
    • Martinez-Ruiz A and Lamas S: Detection and proteomic identification of S-nitrosylated proteins in endothelial cells. Arch Biochem Biophys 423: 192-199, 2004. (Pubitemid 38198228)
    • (2004) Archives of Biochemistry and Biophysics , vol.423 , Issue.1 , pp. 192-199
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 55
    • 0029783344 scopus 로고    scopus 로고
    • Thermal injury in rats alters glucose utilization by skin, wound, and small intestine, but not by skeletal muscle
    • Carter EA, Tompkins RG, Babich JW, Correia J, Bailey EM and Fischman-AJ: Thermal injury in rats alters glucose utilization by skin, wound, and small intestine, but not by skeletal muscle. Metabolism 45: 1161-1167, 1996.
    • (1996) Metabolism , vol.45 , pp. 1161-1167
    • Carter, E.A.1    Tompkins, R.G.2    Babich, J.W.3    Correia, J.4    Bailey, E.M.5    Fischman, A.J.6
  • 58
    • 0035914388 scopus 로고    scopus 로고
    • Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice
    • Cho H, Thorvaldsen JL, Chu Q, Feng F and Brinbaum MJ: Akt1/PKBalpha is required for normal growth but dispensable for maintenance of glucose homeostasis in mice. J Biol Chem 276: 38349-38352, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 38349-38352
    • Cho, H.1    Thorvaldsen, J.L.2    Chu, Q.3    Feng, F.4    Brinbaum, M.J.5
  • 60
    • 34247171304 scopus 로고    scopus 로고
    • Selective control of skeletal muscle differentiation by Akt1
    • DOI 10.1074/jbc.C600315200
    • Wilson EM and Rotwein P: Selective control of skeletal muscle differentiation by Akt1. J Biol Chem 282: 5106-5110, 2007. (Pubitemid 47093711)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5106-5110
    • Wilson, E.M.1    Rotwein, P.2
  • 61
    • 62149108988 scopus 로고    scopus 로고
    • Distinct actions of Akt1 and Akt2 in skeletal muscle differentiation
    • Rotwein P and Wilson EM: Distinct actions of Akt1 and Akt2 in skeletal muscle differentiation. J Cell Physiol 219: 503-511, 2009.
    • (2009) J Cell Physiol , vol.219 , pp. 503-511
    • Rotwein, P.1    Wilson, E.M.2
  • 63
    • 3042842603 scopus 로고    scopus 로고
    • Inflammation and nitric oxide production in skeletal muscle of type 2 diabetic patients
    • DOI 10.1677/joe.0.1810419
    • Torres SH, Sanctis JB, de L Briceno M, Hernandez N and Finol-HJ: Inflammation and nitric oxide production in skeletal muscle of type 2 diabetic patients. J Endocrinol 181: 419-427, 2004. (Pubitemid 38868192)
    • (2004) Journal of Endocrinology , vol.181 , Issue.3 , pp. 419-427
    • Torres, S.H.1    De Sanctis, J.B.2    De L, B.M.3    Hernandez, N.4    Finol, H.J.5


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