메뉴 건너뛰기




Volumn 4, Issue 2, 2006, Pages 210-220

Erratum: Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic β cells (PLoS Biology 4,2, DOI: 10.1371/journal.pbio.0040031);Sirt1 regulates insulin secretion by repressing UCP2 in pancreatic β cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUCOSE; HOMOLOG OF THE YEAST SILENCING INFORMATION REGULATOR 2 PROTEIN; INSULIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINIC ACID DERIVATIVE; PROTEIN DERIVATIVE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN 2; ADENOSINE DIPHOSPHATE; ION CHANNEL; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL UNCOUPLING PROTEIN 2; SIRT1 PROTEIN, MOUSE; SIRT1 PROTEIN, RAT; SIRTUIN;

EID: 33244486764     PISSN: 15457885     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.0040295     Document Type: Erratum
Times cited : (653)

References (61)
  • 1
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • Saltiel AR, Kahn CR (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414: 799-806.
    • (2001) Nature , vol.414 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 2
    • 0002458132 scopus 로고
    • The effect of retarded growth upon the length of life span and upon the ultimate body size
    • McCay CM, Crowell MF, Maynard LA (1935) The effect of retarded growth upon the length of life span and upon the ultimate body size. J Nutr 10: 63-79.
    • (1935) J Nutr , vol.10 , pp. 63-79
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 3
    • 0037166274 scopus 로고    scopus 로고
    • Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels
    • Anderson RM, Bitterman KJ, Wood JG, Medvedik O, Cohen H, et al. (2002) Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels. J Biol Chem 277: 18881-18890.
    • (2002) J Biol Chem , vol.277 , pp. 18881-18890
    • Anderson, R.M.1    Bitterman, K.J.2    Wood, J.G.3    Medvedik, O.4    Cohen, H.5
  • 5
    • 85053097739 scopus 로고
    • Dietary restriction and life extension, biological mechanisms
    • Moment GB, editor. Boca Raton (Florida): CRC Press
    • Barrows CH, Kokkonen GC (1982) Dietary restriction and life extension, biological mechanisms. In: Moment GB, editor. Nutritional approaches to aging research. Boca Raton (Florida): CRC Press. pp. 219-243.
    • (1982) Nutritional Approaches to Aging Research , pp. 219-243
    • Barrows, C.H.1    Kokkonen, G.C.2
  • 6
    • 0037942739 scopus 로고    scopus 로고
    • Extended longevity in mice lacking the insulin receptor in adipose tissue
    • Bluher M, Kahn BB, Kahn CR (2003) Extended longevity in mice lacking the insulin receptor in adipose tissue. Science 299: 572-574.
    • (2003) Science , vol.299 , pp. 572-574
    • Bluher, M.1    Kahn, B.B.2    Kahn, C.R.3
  • 7
    • 4043164343 scopus 로고    scopus 로고
    • Effect of a C/EBP gene replacement on mitochondrial biogenesis in fat cells
    • Chiu CH, Lin WD, Huang SY, Lee YH (2004) Effect of a C/EBP gene replacement on mitochondrial biogenesis in fat cells. Genes Dev 18: 1970-1975.
    • (2004) Genes Dev , vol.18 , pp. 1970-1975
    • Chiu, C.H.1    Lin, W.D.2    Huang, S.Y.3    Lee, Y.H.4
  • 8
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein M, McVey M, Guarente L (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev 13: 2570-2580.
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 9
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum HA, Guarente L (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410: 227-230.
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 10
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • Lin SJ, Defossez PA, Guarente L (2000) Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289: 2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 11
    • 0037130175 scopus 로고    scopus 로고
    • Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration
    • Lin SJ, Kaeberlein M, Andalis AA, Sturtz LA, Defossez PA, et al. (2002) Calorie restriction extends Saccharomyces cerevisiae lifespan by increasing respiration. Nature 418: 344-348.
    • (2002) Nature , vol.418 , pp. 344-348
    • Lin, S.J.1    Kaeberlein, M.2    Andalis, A.A.3    Sturtz, L.A.4    Defossez, P.A.5
  • 12
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 13
    • 0034705129 scopus 로고    scopus 로고
    • The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
    • U S A
    • Landry J, Sutton A, Tafrov ST, Heller RC, Stebbins J, et al. (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc Natl Acad Sci U S A 97: 5807-5811.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 5807-5811
    • Landry, J.1    Sutton, A.2    Tafrov, S.T.3    Heller, R.C.4    Stebbins, J.5
  • 14
    • 12944283150 scopus 로고    scopus 로고
    • A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family
    • U S A
    • Smith JS, Brachmann CB, Celic I, Kenna MA, Muhammad S, et al. (2000) A phylogenetically conserved NAD+-dependent protein deacetylase activity in the Sir2 protein family. Proc Natl Acad Sci U S A 97: 6658-6663.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6658-6663
    • Smith, J.S.1    Brachmann, C.B.2    Celic, I.3    Kenna, M.A.4    Muhammad, S.5
  • 15
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin SJ, Ford E, Haigis M, Liszt G, Guarente L (2004) Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev 18: 12-16.
    • (2004) Genes Dev , vol.18 , pp. 12-16
    • Lin, S.J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 16
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • U S A
    • Rogina B, Helfand SL (2004) Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc Natl Acad Sci U S A 101: 15998-16003.
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 17
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, et al. (2004) Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430: 686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4    Helfand, S.L.5
  • 18
    • 3042681042 scopus 로고    scopus 로고
    • Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma
    • Picard F, Kurtev M, Chung N, Topark-Ngarm A, Senawong T, et al. (2004) Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma. Nature 429: 771-776.
    • (2004) Nature , vol.429 , pp. 771-776
    • Picard, F.1    Kurtev, M.2    Chung, N.3    Topark-Ngarm, A.4    Senawong, T.5
  • 19
    • 1342264308 scopus 로고    scopus 로고
    • Mammalian SIRT1 represses forkhead transcription factors
    • Motta MC, Divecha N, Lemieux M, Kamel C, Chen D, et al. (2004) Mammalian SIRT1 represses forkhead transcription factors. Cell 116: 551-563.
    • (2004) Cell , vol.116 , pp. 551-563
    • Motta, M.C.1    Divecha, N.2    Lemieux, M.3    Kamel, C.4    Chen, D.5
  • 20
    • 12144290563 scopus 로고    scopus 로고
    • Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
    • Brunet A, Sweeney LB, Sturgill JF, Chua KF, Greer PL, et al. (2004) Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase. Science 303: 2011-2015.
    • (2004) Science , vol.303 , pp. 2011-2015
    • Brunet, A.1    Sweeney, L.B.2    Sturgill, J.F.3    Chua, K.F.4    Greer, P.L.5
  • 21
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • Rodgers JT, Lerin C, Haas W, Gygi SP, Spiegelman BM, et al. (2005) Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434: 113-118.
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5
  • 22
    • 0035913903 scopus 로고    scopus 로고
    • hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • Vaziri H, Dessain SK, Ng Eaton E, Imai SI, Frye RA, et al. (2001) hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase. Cell 107: 149-159.
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1    Dessain, S.K.2    Ng Eaton, E.3    Imai, S.I.4    Frye, R.A.5
  • 23
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo J, Nikolaev AY, Imai S, Chen D, Su F, et al. (2001) Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell 107: 137-148.
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5
  • 24
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, et al. (2004) Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305: 390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3    Wall, N.R.4    Hekking, B.5
  • 25
    • 3142742707 scopus 로고    scopus 로고
    • FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)
    • van der Horst A, Tertoolen LG, de Vries-Smits LM, Frye RA, Medema RH, et al. (2004) FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J Biol Chem 279: 28873-28879.
    • (2004) J Biol Chem , vol.279 , pp. 28873-28879
    • Van Der Horst, A.1    Tertoolen, L.G.2    De Vries-Smits, L.M.3    Frye, R.A.4    Medema, R.H.5
  • 26
    • 0022379399 scopus 로고
    • Mitochondrial uncoupling protein from mouse brown fat. Molecular cloning, genetic mapping, and mRNA expression
    • Jacobsson A, Stadler U, Glotzer MA, Kozak LP (1985) Mitochondrial uncoupling protein from mouse brown fat. Molecular cloning, genetic mapping, and mRNA expression. J Biol Chem 260: 16250-16254.
    • (1985) J Biol Chem , vol.260 , pp. 16250-16254
    • Jacobsson, A.1    Stadler, U.2    Glotzer, M.A.3    Kozak, L.P.4
  • 27
    • 0342334561 scopus 로고
    • Molecular approach to thermogenesis in brown adipose tissue: CDNA cloning of the mitochondrial uncoupling protein
    • U S A
    • Bouillaud F, Ricquier D, Thibault J, Weissenbach J (1985) Molecular approach to thermogenesis in brown adipose tissue: cDNA cloning of the mitochondrial uncoupling protein. Proc Natl Acad Sci U S A 82: 445-448.
    • (1985) Proc Natl Acad Sci , vol.82 , pp. 445-448
    • Bouillaud, F.1    Ricquier, D.2    Thibault, J.3    Weissenbach, J.4
  • 28
    • 0034650763 scopus 로고    scopus 로고
    • The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP
    • Ricquier D, Bouillaud F (2000) The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. Biochem J 345: 161-179.
    • (2000) Biochem J , vol.345 , pp. 161-179
    • Ricquier, D.1    Bouillaud, F.2
  • 29
    • 0034668852 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins: From mitochondria to the regulation of energy balance
    • Ricquier D, Bouillaud F (2000) Mitochondrial uncoupling proteins: From mitochondria to the regulation of energy balance. J Physiol 529: 3-10.
    • (2000) J Physiol , vol.529 , pp. 3-10
    • Ricquier, D.1    Bouillaud, F.2
  • 30
    • 0035852755 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3 are highly active H(+) transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone)
    • U S A
    • Echtay KS, Winkler E, Frischmuth K, Klingenberg M (2001) Uncoupling proteins 2 and 3 are highly active H(+) transporters and highly nucleotide sensitive when activated by coenzyme Q (ubiquinone). Proc Natl Acad Sci U S A 98: 1416-1421.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 1416-1421
    • Echtay, K.S.1    Winkler, E.2    Frischmuth, K.3    Klingenberg, M.4
  • 31
    • 0031019249 scopus 로고    scopus 로고
    • Uncoupling protein-2: A novel gene linked to obesity and hyperinsulinemia
    • Fleury C, Neverova M, Collins S, Raimbault S, Champigny O, et al. (1997) Uncoupling protein-2: A novel gene linked to obesity and hyperinsulinemia. Nat Genet 15: 269-272.
    • (1997) Nat Genet , vol.15 , pp. 269-272
    • Fleury, C.1    Neverova, M.2    Collins, S.3    Raimbault, S.4    Champigny, O.5
  • 32
    • 0037773721 scopus 로고    scopus 로고
    • Transport function and regulation of mitochondrial uncoupling proteins 2 and 3
    • Jaburek M, Varecha M, Gimeno RE, Dembski M, Jezek P, et al. (1999) Transport function and regulation of mitochondrial uncoupling proteins 2 and 3. J Biol Chem 274: 26003-26007.
    • (1999) J Biol Chem , vol.274 , pp. 26003-26007
    • Jaburek, M.1    Varecha, M.2    Gimeno, R.E.3    Dembski, M.4    Jezek, P.5
  • 33
    • 0344678342 scopus 로고    scopus 로고
    • Retinoids activate proton transport by the uncoupling proteins UCP1 and UCP2
    • Rial E, Gonzalez-Barroso M, Fleury C, Iturrizaga S, Sanchis D, et al. (1999) Retinoids activate proton transport by the uncoupling proteins UCP1 and UCP2. Embo J 18: 5827-5833.
    • (1999) Embo J , vol.18 , pp. 5827-5833
    • Rial, E.1    Gonzalez-Barroso, M.2    Fleury, C.3    Iturrizaga, S.4    Sanchis, D.5
  • 34
    • 0034891713 scopus 로고    scopus 로고
    • Uncoupling proteins: Their roles in adaptive thermogenesis and substrate metabolism reconsidered
    • Dulloo AG, Samec S (2001) Uncoupling proteins: Their roles in adaptive thermogenesis and substrate metabolism reconsidered. Br J Nutr 86: 123-139.
    • (2001) Br J Nutr , vol.86 , pp. 123-139
    • Dulloo, A.G.1    Samec, S.2
  • 35
    • 0033667705 scopus 로고    scopus 로고
    • Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
    • Arsenijevic D, Onuma H, Pecqueur C, Raimbault S, Manning BS, et al. (2000) Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nat Genet 26: 435-439.
    • (2000) Nat Genet , vol.26 , pp. 435-439
    • Arsenijevic, D.1    Onuma, H.2    Pecqueur, C.3    Raimbault, S.4    Manning, B.S.5
  • 36
    • 0035875087 scopus 로고    scopus 로고
    • Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, beta cell dysfunction, and type 2 diabetes
    • Zhang CY, Baffy G, Perret P, Krauss S, Peroni O, et al. (2001) Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, beta cell dysfunction, and type 2 diabetes. Cell 105: 745-755.
    • (2001) Cell , vol.105 , pp. 745-755
    • Zhang, C.Y.1    Baffy, G.2    Perret, P.3    Krauss, S.4    Peroni, O.5
  • 37
    • 0034990987 scopus 로고    scopus 로고
    • Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: Mechanism of action
    • Chan CB, De Leo D, Joseph JW, McQuaid TS, Ha XF, et al. (2001) Increased uncoupling protein-2 levels in beta-cells are associated with impaired glucose-stimulated insulin secretion: Mechanism of action. Diabetes 50: 1302-1310.
    • (2001) Diabetes , vol.50 , pp. 1302-1310
    • Chan, C.B.1    De Leo, D.2    Joseph, J.W.3    McQuaid, T.S.4    Ha, X.F.5
  • 38
    • 0032991716 scopus 로고    scopus 로고
    • Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets
    • Chan CB, MacDonald PE, Saleh MC, Johns DC, Marban E, et al. (1999) Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets. Diabetes 48: 1482-1486.
    • (1999) Diabetes , vol.48 , pp. 1482-1486
    • Chan, C.B.1    MacDonald, P.E.2    Saleh, M.C.3    Johns, D.C.4    Marban, E.5
  • 39
    • 0037207475 scopus 로고    scopus 로고
    • The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis
    • McBurney MW, Yang X, Jardine K, Hixon M, Boekelheide K, et al. (2003) The mammalian SIR2alpha protein has a role in embryogenesis and gametogenesis. Mol Cell Biol 23: 38-54.
    • (2003) Mol Cell Biol , vol.23 , pp. 38-54
    • McBurney, M.W.1    Yang, X.2    Jardine, K.3    Hixon, M.4    Boekelheide, K.5
  • 40
    • 0141814680 scopus 로고    scopus 로고
    • Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice
    • U S A
    • Cheng HL, Mostoslavsky R, Saito S, Manis JP, Gu Y, et al. (2003) Developmental defects and p53 hyperacetylation in Sir2 homolog (SIRT1)-deficient mice. Proc Natl Acad Sci U S A 100: 10794-10799.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 10794-10799
    • Cheng, H.L.1    Mostoslavsky, R.2    Saito, S.3    Manis, J.P.4    Gu, Y.5
  • 41
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277: 45099-45107.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 42
    • 0034698030 scopus 로고    scopus 로고
    • Measurement of glucose uptake and intracellular calcium concentration in single, living pancreatic beta-cells
    • Yamada K, Nakata M, Horimoto N, Saito M, Matsuoka H, et al. (2000) Measurement of glucose uptake and intracellular calcium concentration in single, living pancreatic beta-cells. J Biol Chem 275: 22278-22283.
    • (2000) J Biol Chem , vol.275 , pp. 22278-22283
    • Yamada, K.1    Nakata, M.2    Horimoto, N.3    Saito, M.4    Matsuoka, H.5
  • 43
    • 25844526509 scopus 로고    scopus 로고
    • 2-NBDG as a fluorescent indicator for direct glucose uptake measurement
    • Zou C, Wang Y, Shen Z (2005) 2-NBDG as a fluorescent indicator for direct glucose uptake measurement. J Biochem Biophys Methods 64: 207-215.
    • (2005) J Biochem Biophys Methods , vol.64 , pp. 207-215
    • Zou, C.1    Wang, Y.2    Shen, Z.3
  • 44
    • 0033524937 scopus 로고    scopus 로고
    • Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes
    • Kulkarni RN, Bruning JC, Winnay JN, Postic C, Magnuson MA, et al. (1999) Tissue-specific knockout of the insulin receptor in pancreatic beta cells creates an insulin secretory defect similar to that in type 2 diabetes. Cell 96: 329-339.
    • (1999) Cell , vol.96 , pp. 329-339
    • Kulkarni, R.N.1    Bruning, J.C.2    Winnay, J.N.3    Postic, C.4    Magnuson, M.A.5
  • 45
    • 0037178854 scopus 로고    scopus 로고
    • Regulation of cellular oncosis by uncoupling protein 2
    • Mills EM, Xu D, Fergusson MM, Combs CA, Xu Y, et al. (2002) Regulation of cellular oncosis by uncoupling protein 2. J Biol Chem 277: 27385-27392.
    • (2002) J Biol Chem , vol.277 , pp. 27385-27392
    • Mills, E.M.1    Xu, D.2    Fergusson, M.M.3    Combs, C.A.4    Xu, Y.5
  • 46
    • 0020788928 scopus 로고
    • Flow-cytometric monitoring of intracellular flavins simultaneously with NAD(P)H levels
    • Thorell B (1983) Flow-cytometric monitoring of intracellular flavins simultaneously with NAD(P)H levels. Cytometry 4: 61-65.
    • (1983) Cytometry , vol.4 , pp. 61-65
    • Thorell, B.1
  • 47
    • 0035815650 scopus 로고    scopus 로고
    • Transcriptional regulation of the mouse uncoupling protein-2 gene. Double E-box motif is required for peroxisome proliferator-activated receptor-gamma-dependent activation
    • Medvedev AV, Snedden SK, Raimbault S, Ricquier D, Collins S (2001) Transcriptional regulation of the mouse uncoupling protein-2 gene. Double E-box motif is required for peroxisome proliferator-activated receptor-gamma-dependent activation. J Biol Chem 276: 10817-10823.
    • (2001) J Biol Chem , vol.276 , pp. 10817-10823
    • Medvedev, A.V.1    Snedden, S.K.2    Raimbault, S.3    Ricquier, D.4    Collins, S.5
  • 49
    • 4344590155 scopus 로고    scopus 로고
    • Small molecules that regulate lifespan: Evidence for xenohormesis
    • Lamming DW, Wood JG, Sinclair DA (2004) Small molecules that regulate lifespan: Evidence for xenohormesis. Mol Microbiol 53: 1003-1009.
    • (2004) Mol Microbiol , vol.53 , pp. 1003-1009
    • Lamming, D.W.1    Wood, J.G.2    Sinclair, D.A.3
  • 50
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • Fulco M, Schiltz RL, Iezzi S, King MT, Zhao P, et al. (2003) Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol Cell 12: 51-62.
    • (2003) Mol Cell , vol.12 , pp. 51-62
    • Fulco, M.1    Schiltz, R.L.2    Iezzi, S.3    King, M.T.4    Zhao, P.5
  • 51
    • 7044239977 scopus 로고    scopus 로고
    • Uncoupled and surviving: Individual mice with high metabolism have greater mitochondrial uncoupling and live longer
    • Speakman JR, Talbot DA, Selman C, Snart S, McLaren JS, et al. (2004) Uncoupled and surviving: Individual mice with high metabolism have greater mitochondrial uncoupling and live longer. Aging Cell 3: 87-95.
    • (2004) Aging Cell , vol.3 , pp. 87-95
    • Speakman, J.R.1    Talbot, D.A.2    Selman, C.3    Snart, S.4    McLaren, J.S.5
  • 52
    • 23944494249 scopus 로고    scopus 로고
    • Targeted expression of the human uncoupling protein 2 (hUCP2) to adult neurons extends life span in the fly
    • Fridell YW, Sanchez-Blanco A, Silvia BA, Helfand SL (2005) Targeted expression of the human uncoupling protein 2 (hUCP2) to adult neurons extends life span in the fly. Cell Metab 1: 145-152.
    • (2005) Cell Metab , vol.1 , pp. 145-152
    • Fridell, Y.W.1    Sanchez-Blanco, A.2    Silvia, B.A.3    Helfand, S.L.4
  • 53
    • 0034717015 scopus 로고    scopus 로고
    • Energy metabolism in uncoupling protein 3 gene knockout mice
    • Vidal-Puig AJ, Grujic D, Zhang CY, Hagen T, Boss O, et al. (2000) Energy metabolism in uncoupling protein 3 gene knockout mice. J Biol Chem 275: 16258-16266.
    • (2000) J Biol Chem , vol.275 , pp. 16258-16266
    • Vidal-Puig, A.J.1    Grujic, D.2    Zhang, C.Y.3    Hagen, T.4    Boss, O.5
  • 54
    • 0034717074 scopus 로고    scopus 로고
    • Lack of obesity and normal response to fasting and thyroid hormone in mice lacking uncoupling protein-3
    • Gong DW, Monemdjou S, Gavrilova O, Leon LR, Marcus-Samuels B, et al. (2000) Lack of obesity and normal response to fasting and thyroid hormone in mice lacking uncoupling protein-3. J Biol Chem 275: 16251-16257.
    • (2000) J Biol Chem , vol.275 , pp. 16251-16257
    • Gong, D.W.1    Monemdjou, S.2    Gavrilova, O.3    Leon, L.R.4    Marcus-Samuels, B.5
  • 55
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone L, Guarente L (2005) Calorie restriction, SIRT1 and metabolism: Understanding longevity. Nat Rev Mol Cell Biol 6: 298-305.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 56
    • 0035937856 scopus 로고    scopus 로고
    • Uncoupling protein 2, in vivo distribution, induction upon oxidative stress, and evidence for translational regulation
    • Pecqueur C, Alves-Guerra MC, Gelly C, Levi-Meyrueis C, Couplan E, et al. (2001) Uncoupling protein 2, in vivo distribution, induction upon oxidative stress, and evidence for translational regulation. J Biol Chem 276: 8705-8712.
    • (2001) J Biol Chem , vol.276 , pp. 8705-8712
    • Pecqueur, C.1    Alves-Guerra, M.C.2    Gelly, C.3    Levi-Meyrueis, C.4    Couplan, E.5
  • 57
    • 2942598147 scopus 로고    scopus 로고
    • Expression of lung uncoupling protein-2 mRNA is modulated developmentally and by caloric intake
    • Maywood
    • Xiao H, Massaro D, Massaro GD, Clerch LB (2004) Expression of lung uncoupling protein-2 mRNA is modulated developmentally and by caloric intake. Exp Biol Med (Maywood) 229: 479-485.
    • (2004) Exp Biol Med , vol.229 , pp. 479-485
    • Xiao, H.1    Massaro, D.2    Massaro, G.D.3    Clerch, L.B.4
  • 58
    • 0030988140 scopus 로고    scopus 로고
    • Uncoupling protein-3: A new member of the mitochondrial carrier family with tissue-specific expression
    • Boss O, Samec S, Paoloni-Giacobino A, Rossier C, Dulloo A, et al. (1997) Uncoupling protein-3: A new member of the mitochondrial carrier family with tissue-specific expression. FEBS Lett 408: 39-42.
    • (1997) FEBS Lett , vol.408 , pp. 39-42
    • Boss, O.1    Samec, S.2    Paoloni-Giacobino, A.3    Rossier, C.4    Dulloo, A.5
  • 59
    • 0037180424 scopus 로고    scopus 로고
    • Progesterone receptor knockout mice have an improved glucose homeostasis secondary to beta-cell proliferation
    • U S A
    • Picard F, Wanatabe M, Schoonjans K, Lydon J, O'Malley BW, et al. (2002) Progesterone receptor knockout mice have an improved glucose homeostasis secondary to beta-cell proliferation. Proc Natl Acad Sci U S A 99: 15644-15648.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 15644-15648
    • Picard, F.1    Wanatabe, M.2    Schoonjans, K.3    Lydon, J.4    O'Malley, B.W.5
  • 60
    • 0037184960 scopus 로고    scopus 로고
    • SRC-1 and TIF2 control energy balance between white and brown adipose tissues
    • Picard F, Gehin M, Annicotte J, Rocchi S, Champy MF, et al. (2002) SRC-1 and TIF2 control energy balance between white and brown adipose tissues. Cell 111: 931-941.
    • (2002) Cell , vol.111 , pp. 931-941
    • Picard, F.1    Gehin, M.2    Annicotte, J.3    Rocchi, S.4    Champy, M.F.5
  • 61
    • 0021996231 scopus 로고
    • Simultaneous extraction and reverse phase high performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells
    • Stocchi V, Cucchiarini L, Magnani M, Palma P, Crescentini G (1985) Simultaneous extraction and reverse phase high performance liquid chromatographic determination of adenine and pyridine nucleotides in human red blood cells. Anal Biochem 146: 118-124.
    • (1985) Anal Biochem , vol.146 , pp. 118-124
    • Stocchi, V.1    Cucchiarini, L.2    Magnani, M.3    Palma, P.4    Crescentini, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.