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Volumn 6, Issue 3, 2005, Pages 248-261

The mitochondrial uncoupling-protein homologues

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; FLAVINE ADENINE NUCLEOTIDE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; PURINE NUCLEOSIDE; PURINE NUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SUPEROXIDE; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 1; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 3;

EID: 14644439938     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1592     Document Type: Review
Times cited : (591)

References (114)
  • 3
    • 0030809576 scopus 로고    scopus 로고
    • Reactive oxygen species, mitochondria, apoptosis and aging
    • Papa, S. & Skulachev, V. P. Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174, 305-319 (1997).
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 305-319
    • Papa, S.1    Skulachev, V.P.2
  • 4
    • 0035174486 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in mammals and plants
    • Borecky, J., Maia, I. G. & Arruda, P. Mitochondrial uncoupling proteins in mammals and plants. Biosci. Rep. 21, 201-212 (2001).
    • (2001) Biosci. Rep. , vol.21 , pp. 201-212
    • Borecky, J.1    Maia, I.G.2    Arruda, P.3
  • 5
    • 0036932298 scopus 로고    scopus 로고
    • The mitochondrial uncoupling proteins
    • REVIEWS30 15
    • Ledesma, A., de Lacoba, M. G. & Rial, E. The mitochondrial uncoupling proteins. Genome Biol. 3, REVIEWS3015 (2002).
    • (2002) Genome Biol. 3 , vol.3
    • Ledesma, A.1    De Lacoba, M.G.2    Rial, E.3
  • 6
    • 0031019249 scopus 로고    scopus 로고
    • Uncoupling protein-2: A novel gene linked to obesity and hyperinsulinemia
    • Fleury, C. et al. Uncoupling protein-2: a novel gene linked to obesity and hyperinsulinemia. Nature Genet. 15, 269-272 (1997).
    • (1997) Nature Genet. , vol.15 , pp. 269-272
    • Fleury, C.1
  • 7
    • 15144356206 scopus 로고    scopus 로고
    • Cloning and characterization of an uncoupling protein homolog: A potential molecular mediator of human thermogenesis
    • Gimeno, R. E. et al. Cloning and characterization of an uncoupling protein homolog: a potential molecular mediator of human thermogenesis. Diabetes 46, 900-906 (1997).
    • (1997) Diabetes , vol.46 , pp. 900-906
    • Gimeno, R.E.1
  • 8
    • 0030988140 scopus 로고    scopus 로고
    • Uncoupling protein-3: A new member of the mitochondrial carrier family with tissue-specific expression
    • Boss, O. et al. Uncoupling protein-3: a new member of the mitochondrial carrier family with tissue-specific expression. FEBS Lett. 408, 39-42 (1997).
    • (1997) FEBS Lett. , vol.408 , pp. 39-42
    • Boss, O.1
  • 9
    • 0031560941 scopus 로고    scopus 로고
    • UCP3: An uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue
    • Vidal-Puig, A., Solanes, G., Grujic, D., Flier, J. S. & Lowell, B. B. UCP3: an uncoupling protein homologue expressed preferentially and abundantly in skeletal muscle and brown adipose tissue. Biochem. Biophys. Res. Commun. 235, 79-82 (1997).
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 79-82
    • Vidal-Puig, A.1    Solanes, G.2    Grujic, D.3    Flier, J.S.4    Lowell, B.B.5
  • 10
    • 0030869755 scopus 로고    scopus 로고
    • Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, β3-adrenergic agonists, and leptin
    • Gong, D. W., He, Y., Karas, M. & Reitman, M. Uncoupling protein-3 is a mediator of thermogenesis regulated by thyroid hormone, β3-adrenergic agonists, and leptin. J. Biol. Chem. 272, 24129-24132 (1997). References 6-10 are the original papers that describe the discovery of UCP2 and UCP3.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24129-24132
    • Gong, D.W.1    He, Y.2    Karas, M.3    Reitman, M.4
  • 11
    • 0024539333 scopus 로고
    • The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups
    • Klingenberg, M. & Appel, M. The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups. Eur. J. Biochem. 180, 123-131 (1989).
    • (1989) Eur. J. Biochem. , vol.180 , pp. 123-131
    • Klingenberg, M.1    Appel, M.2
  • 12
    • 0021322138 scopus 로고
    • Thermogenic mechanisms in brown fat
    • Nicholls, D. G. & Locke, R. M. Thermogenic mechanisms in brown fat. Physiol. Rev. 64, 1-64 (1984). A classic review of UCP1 and BAT biochemistry and physiology.
    • (1984) Physiol. Rev. , vol.64 , pp. 1-64
    • Nicholls, D.G.1    Locke, R.M.2
  • 13
    • 0347989317 scopus 로고    scopus 로고
    • Brown adipose tissue: Function and physiological significance
    • Cannon, B. & Nedergaard, J. Brown adipose tissue: function and physiological significance. Physiol. Rev. 84, 277-359 (2004). A comprehensive, up-to-date review of BAT physiology, which includes a detailed discussion of the role of UCP1 in thermogenesis.
    • (2004) Physiol. Rev. , vol.84 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 14
    • 0024465138 scopus 로고
    • Stimulation of glucose transport by insulin and norepinephrine in isolated rat brown adipocytes
    • Marette, A. & Bukowiecki, L. J. Stimulation of glucose transport by insulin and norepinephrine in isolated rat brown adipocytes. Am. J. Physiol. 257, C714-C721 (1989).
    • (1989) Am. J. Physiol. , vol.257
    • Marette, A.1    Bukowiecki, L.J.2
  • 15
    • 0026678142 scopus 로고
    • Insulin and noradrenaline independently stimulate the translocation of glucose transporters from intracellular stores to the plasma membrane in mouse brown adipocytes
    • Omatsu-Kanbe, M. & Kitasato, H. Insulin and noradrenaline independently stimulate the translocation of glucose transporters from intracellular stores to the plasma membrane in mouse brown adipocytes. FEBS Lett. 314, 246-250 (1992).
    • (1992) FEBS Lett. , vol.314 , pp. 246-250
    • Omatsu-Kanbe, M.1    Kitasato, H.2
  • 16
    • 0017744488 scopus 로고
    • Purification and properties of mitochondrial adenosine triphosphatase of hamster brown adipose tissue
    • Houstek, J. & Drahota, Z. Purification and properties of mitochondrial adenosine triphosphatase of hamster brown adipose tissue. Biochim. Bophys. Acta 484, 127-139 (1977).
    • (1977) Biochim. Bophys Acta , vol.484 , pp. 127-139
    • Houstek, J.1    Drahota, Z.2
  • 17
    • 0017371154 scopus 로고
    • The mitochondrial ATPase of brown adipose tissue. Purification and comparison with the mitochondrial ATPase from beef heart
    • Cannon, B. & Vogel, G. The mitochondrial ATPase of brown adipose tissue. Purification and comparison with the mitochondrial ATPase from beef heart. FEBS Lett. 76, 284-289 (1977).
    • (1977) FEBS Lett. , vol.76 , pp. 284-289
    • Cannon, B.1    Vogel, G.2
  • 18
    • 0032901360 scopus 로고    scopus 로고
    • Structure and function of the uncoupling protein from brown adipose tissue
    • Klingenberg, M. & Huang, S. G. Structure and function of the uncoupling protein from brown adipose tissue. Biochim. Biophys. Acta 1415, 271-296 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 271-296
    • Klingenberg, M.1    Huang, S.G.2
  • 19
    • 0027980820 scopus 로고
    • + transport activity of the reconstituted uncoupling protein
    • + transport activity of the reconstituted uncoupling protein. J. Biol. Chem. 269, 2508-2515 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 2508-2515
    • Winkler, E.1    Klingenberg, M.2
  • 20
    • 0032582799 scopus 로고    scopus 로고
    • The mechanism of proton transport mediated by mitochondrial uncoupling proteins
    • Garlid, K. D., Jaburek, M. & Jezek, P. The mechanism of proton transport mediated by mitochondrial uncoupling proteins. FEBS Lett. 438, 10-14 (1998).
    • (1998) FEBS Lett. , vol.438 , pp. 10-14
    • Garlid, K.D.1    Jaburek, M.2    Jezek, P.3
  • 21
    • 0025930608 scopus 로고
    • Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation
    • Skulachev, V. P. Fatty acid circuit as a physiological mechanism of uncoupling of oxidative phosphorylation. FEBS Lett. 294, 158-162 (1991).
    • (1991) FEBS Lett. , vol.294 , pp. 158-162
    • Skulachev, V.P.1
  • 22
    • 0028110005 scopus 로고
    • Transport of anions and protons by the mitochondrial uncoupling protein and its regulation by nucleotides and fatty acids. A new look at old hypotheses
    • Jezek, P., Orosz, D. E., Modriansky, M. & Garlid, K. D. Transport of anions and protons by the mitochondrial uncoupling protein and its regulation by nucleotides and fatty acids. A new look at old hypotheses. J. Biol. Chem. 269, 26184-26190 (1994). References 21 and 22 outline the development of the fatty-acid-cycling model of UCP function.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26184-26190
    • Jezek, P.1    Orosz, D.E.2    Modriansky, M.3    Garlid, K.D.4
  • 23
    • 0030039607 scopus 로고    scopus 로고
    • On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein
    • Garlid, K. D., Orosz, D. E., Modriansky, M., Vassanelli, S., & Jezek, P. On the mechanism of fatty acid-induced proton transport by mitochondrial uncoupling protein. J. Biol. Chem. 271, 2615-2620 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 2615-2620
    • Garlid, K.D.1    Orosz, D.E.2    Modriansky, M.3    Vassanelli, S.4    Jezek, P.5
  • 25
    • 0343900275 scopus 로고    scopus 로고
    • The uncoupling protein UCP 1 does not increase the proton conductance of the inner mitochondrial membrane by functioning as a fatty acid anion transporter
    • Gonzalez-Barroso, M. M., Fleury, C., Bouillaud, F., Nicholls, D. G. & Rial, E. The uncoupling protein UCP1 does not increase the proton conductance of the inner mitochondrial membrane by functioning as a fatty acid anion transporter. J. Biol. Chem. 273, 15528-15532 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 15528-15532
    • Gonzalez-Barroso, M.M.1    Fleury, C.2    Bouillaud, F.3    Nicholls, D.G.4    Rial, E.5
  • 28
    • 1042286448 scopus 로고    scopus 로고
    • Alkylsulfonates activate the uncoupling protein UCP1: Implications for the transport mechanism
    • Rial, E., Aguirregoitia, E., Jimenez-Jimenez, J. & Ledesma, A. Alkylsulfonates activate the uncoupling protein UCP1: implications for the transport mechanism. Biochim. Biophys. Acta 1608, 122-130 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1608 , pp. 122-130
    • Rial, E.1    Aguirregoitia, E.2    Jimenez-Jimenez, J.3    Ledesma, A.4
  • 29
    • 0034735799 scopus 로고    scopus 로고
    • Coenzyme Q is an obligatory cofactor for uncoupling protein function
    • Echtay, K. S., Winkler, E. & Klingenberg, M. Coenzyme Q is an obligatory cofactor for uncoupling protein function. Nature 408, 609-613 (2000).
    • (2000) Nature , vol.408 , pp. 609-613
    • Echtay, K.S.1    Winkler, E.2    Klingenberg, M.3
  • 30
    • 0018358214 scopus 로고
    • Brown adipose tissue mitochondria
    • Nicholls, D. G. Brown adipose tissue mitochondria. Biochim. Biophys. Acta 549, 1-29 (1979).
    • (1979) Biochim. Biophys. Acta , vol.549 , pp. 1-29
    • Nicholls, D.G.1
  • 31
    • 0025154843 scopus 로고
    • - translocating pathway of the uncoupling protein of brown adipose tissue mitochondria
    • - translocating pathway of the uncoupling protein of brown adipose tissue mitochondria. J. Biol. Chem. 265, 19303-19311 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 19303-19311
    • Jezek, P.1    Garlid, K.D.2
  • 32
    • 0017817970 scopus 로고
    • Brown-adipose-tissue mitochondria: Photoaffinity labelling of the regulatory site of energy dissipation
    • Heaton, G. M., Wagenvoord, R. J., Kemp, A. Jr & Nicholls, D. G. Brown-adipose-tissue mitochondria: photoaffinity labelling of the regulatory site of energy dissipation. Eur. J. Biochem. 82, 515-521 (1978). A classic paper describing identification of UCP1.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 515-521
    • Heaton, G.M.1    Wagenvoord, R.J.2    Kemp Jr., A.3    Nicholls, D.G.4
  • 33
    • 85047686497 scopus 로고    scopus 로고
    • A history of UCP1
    • Nicholls, D. G. A history of UCP1. Biochem. Soc. Trans 29, 751-755 (2001). A mini-review giving an historic perspective on the discovery of UCP1.
    • (2001) Biochem. Soc. Trans , vol.29 , pp. 751-755
    • Nicholls, D.G.1
  • 34
    • 0017264191 scopus 로고
    • Hamster brown-adipose-tissue mitochondria. Purine nucleotide control of the ion conductance of the inner membrane, the nature of the nucleotide binding site
    • Nicholls, D. G. Hamster brown-adipose-tissue mitochondria. Purine nucleotide control of the ion conductance of the inner membrane, the nature of the nucleotide binding site. Eur. J. Biochem. 62, 223-228 (1976).
    • (1976) Eur. J. Biochem. , vol.62 , pp. 223-228
    • Nicholls, D.G.1
  • 35
    • 0034673976 scopus 로고    scopus 로고
    • Uncoupling proteins 1 and 3 are regulated differently
    • Hagen, T., Zhang, C. Y., Vianna, C. R. & Lowell, B. B. Uncoupling proteins 1 and 3 are regulated differently. Biochemistry 39, 5845-5851 (2000).
    • (2000) Biochemistry , vol.39 , pp. 5845-5851
    • Hagen, T.1    Zhang, C.Y.2    Vianna, C.R.3    Lowell, B.B.4
  • 36
    • 0032980686 scopus 로고    scopus 로고
    • Fasting and leptin modulate adipose and muscle uncoupling protein: Divergent effects between messenger ribonucleic acid and protein expression
    • Sivitz, W. I., Fink, B. D. & Donohoue, P. A. Fasting and leptin modulate adipose and muscle uncoupling protein: divergent effects between messenger ribonucleic acid and protein expression. Endocrinology 140, 1511-1519 (1999).
    • (1999) Endocrinology , vol.140 , pp. 1511-1519
    • Sivitz, W.I.1    Fink, B.D.2    Donohoue, P.A.3
  • 37
    • 0035937856 scopus 로고    scopus 로고
    • Uncoupling protein 2, in vivo distribution, induction upon oxidative stress, and evidence for translational regulation
    • Pecqueur, C. et al. Uncoupling protein 2, in vivo distribution, induction upon oxidative stress, and evidence for translational regulation. J. Biol. Chem. 276, 8705-8712 (2001). References 36 and 37 clearly show that the amount of UCP2 mRNA, in different tissues and in different physiological states, does not predict the amount or presence of UCP2 protein.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8705-8712
    • Pecqueur, C.1
  • 39
    • 0034650763 scopus 로고    scopus 로고
    • The uncoupling protein homologues: UCP1, UCP2, UCP 3, StUCP and AtUCR
    • Ricquier, D. & Bouillaud, F. The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCR Biochem. J. 345, 161-179 (2000).
    • (2000) Biochem. J. , vol.345 , pp. 161-179
    • Ricquier, D.1    Bouillaud, F.2
  • 40
    • 0037253404 scopus 로고    scopus 로고
    • The 'novel' 'uncoupling' proteins UCP2 and UCP3; what do they realty do? Pros and cons for suggested functions
    • Nedergaard, J. & Cannon, B. The 'novel' 'uncoupling' proteins UCP2 and UCP3; what do they realty do? Pros and cons for suggested functions. Exp. Physiol. 88, 65-84 (2003).
    • (2003) Exp. Physiol. , vol.88 , pp. 65-84
    • Nedergaard, J.1    Cannon, B.2
  • 41
    • 0038168520 scopus 로고    scopus 로고
    • Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10
    • Jaburek, M. & Garlid, K. D. Reconstitution of recombinant uncoupling proteins: UCP1, -2, and -3 have similar affinities for ATP and are unaffected by coenzyme Q10. J. Biol. Chem. 278, 25825-25831 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 25825-25831
    • Jaburek, M.1    Garlid, K.D.2
  • 43
    • 0006877856 scopus 로고    scopus 로고
    • Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean
    • Clapham, J. C. et al. Mice overexpressing human uncoupling protein-3 in skeletal muscle are hyperphagic and lean. Nature 406, 415-418 (2000).
    • (2000) Nature , vol.406 , pp. 415-418
    • Clapham, J.C.1
  • 44
    • 0035875366 scopus 로고    scopus 로고
    • A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast
    • Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B. & Brand, M. D. A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast. Biochem. J. 356, 779-789 (2001).
    • (2001) Biochem. J. , vol.356 , pp. 779-789
    • Stuart, J.A.1    Harper, J.A.2    Brindle, K.M.3    Jekabsons, M.B.4    Brand, M.D.5
  • 45
    • 0035947694 scopus 로고    scopus 로고
    • Physiological levels of mammalian uncoupling protein 2 do not uncouple yeast mitochondria
    • Stuart, J. A., Harper, J. A., Brindle, K. M., Jekabsons, M. B. & Brand, M. D. Physiological levels of mammalian uncoupling protein 2 do not uncouple yeast mitochondria. J. Biol. Chem. 276, 18633-18639 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 18633-18639
    • Stuart, J.A.1    Harper, J.A.2    Brindle, K.M.3    Jekabsons, M.B.4    Brand, M.D.5
  • 46
    • 0036182511 scopus 로고    scopus 로고
    • Artifactual uncoupling by uncoupling protein 3 in yeast mitochondria at the concentrations found in mouse and rat skeletal-muscle mitochondria
    • Harper, J. A. et al. Artifactual uncoupling by uncoupling protein 3 in yeast mitochondria at the concentrations found in mouse and rat skeletal-muscle mitochondria. Biochem. J. 361, 49-56 (2002).
    • (2002) Biochem. J. , vol.361 , pp. 49-56
    • Harper, J.A.1
  • 47
    • 0037169484 scopus 로고    scopus 로고
    • The basal proton conductance of skeletal muscle mitochondria from transgenic mice overexpressing or lacking uncoupling protein-3
    • Cadenas, S. et al. The basal proton conductance of skeletal muscle mitochondria from transgenic mice overexpressing or lacking uncoupling protein-3. J. Biol. Chem. 277, 2773-2778 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 2773-2778
    • Cadenas, S.1
  • 48
    • 18244379331 scopus 로고    scopus 로고
    • Superoxide activates mitochondrial uncoupling proteins
    • Echtay, K. S. et al. Superoxide activates mitochondrial uncoupling proteins. Nature 415, 96-99 (2002). Seminal work on the regulation of uncoupling proteins by superoxide.
    • (2002) Nature , vol.415 , pp. 96-99
    • Echtay, K.S.1
  • 49
    • 0037039366 scopus 로고    scopus 로고
    • A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2
    • Krauss, S., Zhang, C. Y. & Lowell, B. B. A significant portion of mitochondrial proton leak in intact thymocytes depends on expression of UCP2. Proc. Natl Acad. Sci. USA 99, 118-122 (2002). Shows that endogenous UCP2 mediates proton leak in intact cells.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 118-122
    • Krauss, S.1    Zhang, C.Y.2    Lowell, B.B.3
  • 50
    • 0346340042 scopus 로고    scopus 로고
    • Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction
    • Krauss, S. et al. Superoxide-mediated activation of uncoupling protein 2 causes pancreatic β cell dysfunction. J. Clin. Invest. 112, 1831-1842 (2003). Highlights the significance of superoxide-medlated activation of UCP2 in β-cell pathophysiology and type-2 diabetes. Shows that increased UCP2 activity causes hyperglycaemia-induced loss of glucose sensing in β-cells.
    • (2003) J. Clin. Invest. , vol.112 , pp. 1831-1842
    • Krauss, S.1
  • 51
    • 0034717074 scopus 로고    scopus 로고
    • Lack of obesity and normal response to fasting and thyroid hormone in mice lacking uncoupling protein-3
    • Gong, D. W. et al. Lack of obesity and normal response to fasting and thyroid hormone in mice lacking uncoupling protein-3. J. Biol. Chem. 275, 16251-16257 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 16251-16257
    • Gong, D.W.1
  • 52
    • 0034717015 scopus 로고    scopus 로고
    • Energy metabolism in uncoupling protein 3 gene knockout mice
    • Vidal-Puig, A. J. et al. Energy metabolism in uncoupling protein 3 gene knockout mice. J. Biol. Cnem. 275, 16258-16266 (2000). Shows that endogenous UCP3 has a role in limiting superoxide production.
    • (2000) J. Biol. Cnem. , vol.275 , pp. 16258-16266
    • Vidal-Puig, A.J.1
  • 53
    • 0035875087 scopus 로고    scopus 로고
    • Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β cell dysfunction, and type 2 diabetes
    • Zhang, C. Y. et al. Uncoupling protein-2 negatively regulates insulin secretion and is a major link between obesity, β cell dysfunction, and type 2 diabetes. Cell 105, 745-755 (2001). Shows the critical role of UCP2 in vivo in the pathophysiology of β-cell dysfunction and type-2 diabetes.
    • (2001) Cell , vol.105 , pp. 745-755
    • Zhang, C.Y.1
  • 54
    • 0035827595 scopus 로고    scopus 로고
    • In vivo effects of uncoupling protein-3 gene disruption on mitochondrial energy metabolism
    • Cline, G. W. et al. In vivo effects of uncoupling protein-3 gene disruption on mitochondrial energy metabolism. J. Biol. Chem. 276, 20240-20244 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20240-20244
    • Cline, G.W.1
  • 55
    • 0346814090 scopus 로고    scopus 로고
    • Superoxide activates uncoupling proteins by generating carbon-centered radicals and Initiating lipid peroxidation: Studies using a mitochondria- targeted spin trap derived from α-phenyl-N-tert-butylnitrone
    • Murphy, M. P. et al. Superoxide activates uncoupling proteins by generating carbon-centered radicals and Initiating lipid peroxidation: studies using a mitochondria-targeted spin trap derived from α-phenyl-N-tert- butylnitrone. J. Biol. Chem. 278, 48534-48545 (2003). Outlines a basic model of the pathway by which superoxide might activate UCP1 and its homologues..
    • (2003) J. Biol. Chem. , vol.278 , pp. 48534-48545
    • Murphy, M.P.1
  • 56
    • 0037033039 scopus 로고    scopus 로고
    • Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants
    • Echtay, K. S., Murphy, M. P., Smith, R. A., Talbot, D. A. & Brand, M. D. Superoxide activates mitochondrial uncoupling protein 2 from the matrix side. Studies using targeted antioxidants. J. Biol. Chem. 277, 47129-47135 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47129-47135
    • Echtay, K.S.1    Murphy, M.P.2    Smith, R.A.3    Talbot, D.A.4    Brand, M.D.5
  • 57
    • 0038266426 scopus 로고    scopus 로고
    • Superoxide stimulates a proton leak in potato mitochondria that is related to the activity of uncoupling protein
    • Considine, M. J. et al. Superoxide stimulates a proton leak in potato mitochondria that is related to the activity of uncoupling protein. J. Biol. Chem. 278, 22298-22302 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 22298-22302
    • Considine, M.J.1
  • 58
    • 0041465009 scopus 로고    scopus 로고
    • A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling
    • Echtay, K. S. et al. A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling. EMBO J. 22, 4103-4110 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4103-4110
    • Echtay, K.S.1
  • 59
    • 0038419546 scopus 로고    scopus 로고
    • Activating ω-6 polyunsaturated fatty acids and inhibitory purine nucleotides are high affinity ligands for novel mitochondrial uncoupling proteins UCP2 and UCP3
    • Zackova, M., Skobisova, E., Urbankova, E. & Jezek, P. Activating ω-6 polyunsaturated fatty acids and inhibitory purine nucleotides are high affinity ligands for novel mitochondrial uncoupling proteins UCP2 and UCP3. J. Biol. Chem. 278, 20761-20769 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 20761-20769
    • Zackova, M.1    Skobisova, E.2    Urbankova, E.3    Jezek, P.4
  • 60
    • 0037773721 scopus 로고    scopus 로고
    • Transport function and regulation of mitochondrial uncoupling proteins 2 and 3
    • Jaburek, M. et al. Transport function and regulation of mitochondrial uncoupling proteins 2 and 3. J. Biol. Chem. 274, 26003-26007 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26003-26007
    • Jaburek, M.1
  • 61
    • 1842409029 scopus 로고    scopus 로고
    • Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese
    • Enerback, S. et al. Mice lacking mitochondrial uncoupling protein are cold-sensitive but not obese. Nature 387, 90-94 (1997). Shows that UCP1 is responsible for cold-exposure-induced, non-shivering thermogenesis.
    • (1997) Nature , vol.387 , pp. 90-94
    • Enerback, S.1
  • 62
    • 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. et al. Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production. Nature Genet. 26, 435-439 (2000). First report of a UCP2-knockout-mouse model; shows that endogenous UCP2 protein has a role in limiting ROS production.
    • (2000) Nature Genet. , vol.26 , pp. 435-439
    • Arsenijevic, D.1
  • 64
    • 3543099847 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 1 expressed in the heart of transgenic mice protects against ischemic-reperfusion damage
    • Hoerter, J. et al. Mitochondrial uncoupling protein 1 expressed in the heart of transgenic mice protects against ischemic-reperfusion damage. Circulation 110, 528-533 (2004).
    • (2004) Circulation , vol.110 , pp. 528-533
    • Hoerter, J.1
  • 65
    • 0344982956 scopus 로고    scopus 로고
    • Pharmacology: Uncoupling the agony from ecstasy
    • Mills, E. M., Banks, M. L., Sprague, J. E. & Finkel, T. Pharmacology: uncoupling the agony from ecstasy. Nature 426, 403-404 (2003).
    • (2003) Nature , vol.426 , pp. 403-404
    • Mills, E.M.1    Banks, M.L.2    Sprague, J.E.3    Finkel, T.4
  • 66
    • 0642272500 scopus 로고    scopus 로고
    • Uncoupling protein 3 as a mitochondrial fatty acid anion exporter
    • Schrauwen, P. et al. Uncoupling protein 3 as a mitochondrial fatty acid anion exporter. FASEB J. 17, 2272-2274 (2003).
    • (2003) FASEB J. , vol.17 , pp. 2272-2274
    • Schrauwen, P.1
  • 67
    • 0035133171 scopus 로고    scopus 로고
    • Physiological role of UCP3 may be export of fatty acids from mitochondria when fatty acid oxidation predominates: An hypothesis
    • Himms-Hagen, J. & Harper, M. E. Physiological role of UCP3 may be export of fatty acids from mitochondria when fatty acid oxidation predominates: an hypothesis. Exp. Biol. Med. (Maywood) 226, 78-84 (2001).
    • (2001) Exp. Biol. Med. (Maywood) , vol.226 , pp. 78-84
    • Himms-Hagen, J.1    Harper, M.E.2
  • 68
    • 0023790275 scopus 로고
    • A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria
    • Alexson, S. E. & Nedergaard, J. A novel type of short- and medium-chain acyl-CoA hydrolases in brown adipose tissue mitochondria. J. Biol. Chem. 263, 13564-13571 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 13564-13571
    • Alexson, S.E.1    Nedergaard, J.2
  • 69
    • 0033969421 scopus 로고    scopus 로고
    • Uncoupling proteins 2 and 3: Potential regulators of mitochondrial energy metabolism
    • Boss, O., Hagen, T. & Lowell, B. B. Uncoupling proteins 2 and 3: potential regulators of mitochondrial energy metabolism. Diabetes 49, 143-156 (2000).
    • (2000) Diabetes , vol.49 , pp. 143-156
    • Boss, O.1    Hagen, T.2    Lowell, B.B.3
  • 70
    • 0033525848 scopus 로고    scopus 로고
    • Genomic organization and regulation by dietary fat of the uncoupling protein 3 and 2 genes
    • Gong, D. W., He, Y. & Reitman, M. L. Genomic organization and regulation by dietary fat of the uncoupling protein 3 and 2 genes. Biochem. Biophys. Res. Commun. 256, 27-32 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 27-32
    • Gong, D.W.1    He, Y.2    Reitman, M.L.3
  • 71
    • 0032189845 scopus 로고    scopus 로고
    • Effects of mutations in the human uncoupling protein 3 gene on the respiratory quotient and fat oxidation in severe obesity and type 2 diabetes
    • Argyropoulos, G. et al. Effects of mutations in the human uncoupling protein 3 gene on the respiratory quotient and fat oxidation in severe obesity and type 2 diabetes. J. Clin. Invest. 102, 1345-1351 (1998).
    • (1998) J. Clin. Invest. , vol.102 , pp. 1345-1351
    • Argyropoulos, G.1
  • 72
    • 0032884928 scopus 로고    scopus 로고
    • Genetic and physiologic analysis of the role of uncoupling protein 3 in human energy homeostasis
    • Chung, W. K. et al. Genetic and physiologic analysis of the role of uncoupling protein 3 in human energy homeostasis. Diabetes 48, 1890-1895 (1999).
    • (1999) Diabetes , vol.48 , pp. 1890-1895
    • Chung, W.K.1
  • 73
    • 0033002467 scopus 로고    scopus 로고
    • The long isoform uncoupling protein-3 (UCP3L) in human energy homeostasis
    • Chung, W. K. et al. The long isoform uncoupling protein-3 (UCP3L) in human energy homeostasis. Int. J. Obes. Relat. Metab. Disord. 23 (Suppl. 6), S49-S50 (1999).
    • (1999) Int. J. Obes. Relat. Metab. Disord. , vol.23 , Issue.SUPPL. 6
    • Chung, W.K.1
  • 74
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S. S., Skulachev, V. P. & Starkov, A. A. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18 (1997).
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 75
    • 0038061012 scopus 로고    scopus 로고
    • A role for uncoupling protein-2 as a regulator of mitochondrial hydrogen peroxide generation
    • Negre-Salvayre, A. et al. A role for uncoupling protein-2 as a regulator of mitochondrial hydrogen peroxide generation. FASEB J. 11, 809-815 (1997). First formulation of the hypothesis that UCP homologues regulate superoxide production.
    • (1997) FASEB J. , vol.11 , pp. 809-815
    • Negre-Salvayre, A.1
  • 76
    • 0036965865 scopus 로고    scopus 로고
    • Increased reactive oxygen species production with antisense oligonucleotides directed against uncoupling protein 2 in murine endothelial cells
    • Duval, C. et al. Increased reactive oxygen species production with antisense oligonucleotides directed against uncoupling protein 2 in murine endothelial cells. Biochem. Cell Biol. 80, 757-764 (2002).
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 757-764
    • Duval, C.1
  • 77
    • 4043147798 scopus 로고    scopus 로고
    • Mitochondrial superoxide: Production, biological effects, and activation of uncoupling proteins
    • Brand, M. D. et al. Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins. Free Radic. Biol. Med. 37, 755-767 (2004).
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 755-767
    • Brand, M.D.1
  • 78
    • 0346094388 scopus 로고    scopus 로고
    • Production of endogenous matrix superoxide from mitochondrial complex I leads to activation of uncoupling protein 3
    • Talbot, D. A., Lambert, A. J. & Brand, M. D. Production of endogenous matrix superoxide from mitochondrial complex I leads to activation of uncoupling protein 3. FEBS Lett. 556, 111-115 (2004).
    • (2004) FEBS Lett. , vol.556 , pp. 111-115
    • Talbot, D.A.1    Lambert, A.J.2    Brand, M.D.3
  • 79
    • 2242425423 scopus 로고    scopus 로고
    • Oxidative damage and phospholipid fatty acyl composition in skeletal muscle mitochondria from mice underexpressing or overexpressing uncoupling protein 3
    • Brand, M. D. et al. Oxidative damage and phospholipid fatty acyl composition in skeletal muscle mitochondria from mice underexpressing or overexpressing uncoupling protein 3. Biochem. J. 368, 597-603 (2002).
    • (2002) Biochem. J. , vol.368 , pp. 597-603
    • Brand, M.D.1
  • 80
    • 0042526012 scopus 로고    scopus 로고
    • Uncoupling protein-2 overexpression inhibits mitochondrial death pathway in cardiomyocytes
    • Teshima, Y., Akao, M., Jones, S. P. & Marban, E. Uncoupling protein-2 overexpression inhibits mitochondrial death pathway in cardiomyocytes. Circ. Res. 93, 192-200 (2003).
    • (2003) Circ. Res. , vol.93 , pp. 192-200
    • Teshima, Y.1    Akao, M.2    Jones, S.P.3    Marban, E.4
  • 81
    • 0041464712 scopus 로고    scopus 로고
    • Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma
    • Mattiasson, G. et al. Uncoupling protein-2 prevents neuronal death and diminishes brain dysfunction after stroke and brain trauma. Nature Med. 9, 1062-1068 (2003).
    • (2003) Nature Med. , vol.9 , pp. 1062-1068
    • Mattiasson, G.1
  • 82
    • 0242468451 scopus 로고    scopus 로고
    • Uncoupling protein 2 prevents neuronal death including that occurring during seizures: A mechanism for preconditioning
    • Diano, S. et al. Uncoupling protein 2 prevents neuronal death including that occurring during seizures: a mechanism for preconditioning. Endocrinology 144, 5014-5021 (2003).
    • (2003) Endocrinology , vol.144 , pp. 5014-5021
    • Diano, S.1
  • 83
    • 2642573308 scopus 로고    scopus 로고
    • Resistance to cerebral ischemic injury in UCP2 knockout mice: Evidence for a role of UCP 2 as a regulator of mitochondrial glutathione levels
    • de Bilbao, F. et al. Resistance to cerebral ischemic injury in UCP2 knockout mice: evidence for a role of UCP2 as a regulator of mitochondrial glutathione levels. J. Neurochem. 89, 1283-1292 (2004).
    • (2004) J. Neurochem. , vol.89 , pp. 1283-1292
    • De Bilbao, F.1
  • 84
    • 0032787462 scopus 로고    scopus 로고
    • + channels and insulin secretion: Their role in health and disease
    • + channels and insulin secretion: their role in health and disease. Diabetologia 42, 903-919 (1999).
    • (1999) Diabetologia , vol.42 , pp. 903-919
    • Ashcroft, F.M.1    Gribble, F.M.2
  • 85
    • 0031892853 scopus 로고    scopus 로고
    • Pancreatic β-cell glucokinase: Dosing the gap between theoretical concepts and experimental realities
    • Matschinsky, F. M., Glaser, B. & Magnuson, M. A. Pancreatic β-cell glucokinase: dosing the gap between theoretical concepts and experimental realities. Diabetes 47, 307-315 (1998).
    • (1998) Diabetes , vol.47 , pp. 307-315
    • Matschinsky, F.M.1    Glaser, B.2    Magnuson, M.A.3
  • 87
    • 0033582196 scopus 로고    scopus 로고
    • 2+ dependent exocytosis in pancreatic β cells
    • 2+ dependent exocytosis in pancreatic β cells. Proc. Natl Acad. Sci. USA 96, 760-765 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 760-765
    • Takahashi, N.1
  • 88
    • 0034990987 scopus 로고    scopus 로고
    • Increased uncoupling protein-2 levels in β-cells are associated with impaired glucose-stimulated insulin secretion: Mechanism of action
    • Chan, C. B. et al. Increased uncoupling protein-2 levels in β-cells are associated with impaired glucose-stimulated insulin secretion: mechanism of action. Diabetes 50, 1302-1310 (2001).
    • (2001) Diabetes , vol.50 , pp. 1302-1310
    • Chan, C.B.1
  • 89
    • 0032991716 scopus 로고    scopus 로고
    • Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets
    • Chan, C. B. et al. Overexpression of uncoupling protein 2 inhibits glucose-stimulated insulin secretion from rat islets. Diabetes 48, 1482-1486 (1999). Shows that the forced overexpression of UCP2 in pancreatic β-cells causes loss of glucose sensing.
    • (1999) Diabetes , vol.48 , pp. 1482-1486
    • Chan, C.B.1
  • 90
    • 0036829870 scopus 로고    scopus 로고
    • Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet
    • Joseph, J. W. et al. Uncoupling protein 2 knockout mice have enhanced insulin secretory capacity after a high-fat diet. Diabetes 51, 3211-3219 (2002). Shows that the absence of UCP2 protects against high-fat-diet-induced β-cell dysfunction.
    • (2002) Diabetes , vol.51 , pp. 3211-3219
    • Joseph, J.W.1
  • 91
    • 0043268763 scopus 로고    scopus 로고
    • Pancreatic β-cell lipotoxicity induced by Overexpression of hormone-sensitive lipase
    • Winzell, M. S. et al. Pancreatic β-cell lipotoxicity induced by Overexpression of hormone-sensitive lipase. Diabetes 52, 2057-2065 (2003).
    • (2003) Diabetes , vol.52 , pp. 2057-2065
    • Winzell, M.S.1
  • 92
    • 0037192853 scopus 로고    scopus 로고
    • Genetic regulation of metabolic pathways in β-cells disrupted by hyperglycemia
    • Laybutt, D. R. et al. Genetic regulation of metabolic pathways in β-cells disrupted by hyperglycemia. J. Biol. Chem. 277, 10912-10921 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 10912-10921
    • Laybutt, D.R.1
  • 93
    • 0034577567 scopus 로고    scopus 로고
    • Correlation between pancreatic islet uncoupling protein-2 (UCP2) mRNA concentration and insulin status in rats
    • Kassis, N. et al. Correlation between pancreatic islet uncoupling protein-2 (UCP2) mRNA concentration and insulin status in rats. Int. J. Exp. Diabetes Res. 1, 185-193 (2000).
    • (2000) Int. J. Exp. Diabetes Res. , vol.1 , pp. 185-193
    • Kassis, N.1
  • 94
    • 0037984371 scopus 로고    scopus 로고
    • Visualizing superoxide production in normal and diabetic rat islets of langerhans
    • Bindokas, V. P. et al. Visualizing superoxide production in normal and diabetic rat islets of langerhans. J. Biol. Chem. 278, 9796-9801 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 9796-9801
    • Bindokas, V.P.1
  • 95
    • 0035078830 scopus 로고    scopus 로고
    • Uncoupling protein 2: A possible link between fatty acid excess and impaired glucose-induced insulin secretion?
    • Lameloise, N., Muzzin, P., Prentki, M. & Assimacopoulos-Jeannet, F. Uncoupling protein 2: a possible link between fatty acid excess and impaired glucose-induced insulin secretion? Diabetes 50, 803-809 (2001).
    • (2001) Diabetes , vol.50 , pp. 803-809
    • Lameloise, N.1    Muzzin, P.2    Prentki, M.3    Assimacopoulos-Jeannet, F.4
  • 96
    • 1642546212 scopus 로고    scopus 로고
    • Over-expression of sterol regulatory element binding protein-1c in rat pancreatic islets induces iipogenesis and decreases glucose-stimulated insulin release: Modulation by 5-aminoimidazole-4-carboxamide ribonucleoside
    • Diraison, F. et al. Over-expression of sterol regulatory element binding protein-1c in rat pancreatic islets induces iipogenesis and decreases glucose-stimulated insulin release: modulation by 5-aminoimidazole-4-carboxamide ribonucleoside. Biochem. J. 378, 769-778 (2003).
    • (2003) Biochem. J. , vol.378 , pp. 769-778
    • Diraison, F.1
  • 97
    • 3843145012 scopus 로고    scopus 로고
    • Role of UCP-2 up-regulation and TG accumulation in impaired glucose-stimulated insulin secretion in a β-cell lipotoxicity model overexpressing SREBP-1c
    • Yamashita, T. et al. Role of UCP-2 up-regulation and TG accumulation in impaired glucose-stimulated insulin secretion in a β-cell lipotoxicity model overexpressing SREBP-1c. Endocrinology 145, 3566-3577 (2004).
    • (2004) Endocrinology , vol.145 , pp. 3566-3577
    • Yamashita, T.1
  • 98
    • 0038165514 scopus 로고    scopus 로고
    • Mitochondrial functional state in clonal pancreatic β-cells exposed to free fatty acids
    • Koshkin, V., Wang, X., Scherer, P. E., Chan, C. B. & Wheeler, M. B. Mitochondrial functional state in clonal pancreatic β-cells exposed to free fatty acids. J. Biol. Chem. 278, 19709-19715 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 19709-19715
    • Koshkin, V.1    Wang, X.2    Scherer, P.E.3    Chan, C.B.4    Wheeler, M.B.5
  • 99
    • 10944265062 scopus 로고    scopus 로고
    • Free fatty acid induced β-cell defects are dependent on uncoupling protein 2 expression
    • Joseph, J. W. et al. Free fatty acid induced β-cell defects are dependent on uncoupling protein 2 expression. J. Biol. Chem. 279, 51049-51056 (2004). Shows that the absence of UCP2 protects against fatty-acid-induced β-cell dysfunction.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51049-51056
    • Joseph, J.W.1
  • 100
    • 0034464215 scopus 로고    scopus 로고
    • Inhibition of glucose-induced insulin secretion by 4-hydroxy-2-nonenal and other lipid peroxidation products
    • Miwa, I., Ichimura, N., Sugiura, M., Hamada, Y. & Taniguchi, S. Inhibition of glucose-induced insulin secretion by 4-hydroxy-2-nonenal and other lipid peroxidation products. Endocrinology 141, 2767-2772 (2000).
    • (2000) Endocrinology , vol.141 , pp. 2767-2772
    • Miwa, I.1    Ichimura, N.2    Sugiura, M.3    Hamada, Y.4    Taniguchi, S.5
  • 101
    • 0036153256 scopus 로고    scopus 로고
    • Minireview: Secondary β-cell failure in type 2 diabetes - A convergence of glucotoxicity and lipotoxidty
    • Poitout, V. & Robertson, H. P. Minireview: Secondary β-cell failure in type 2 diabetes - a convergence of glucotoxicity and lipotoxidty. Endocrinology 143, 339-342 (2002).
    • (2002) Endocrinology , vol.143 , pp. 339-342
    • Poitout, V.1    Robertson, H.P.2
  • 102
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • Pebay-Peyroula, E. et al. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 426, 39-44 (2003).
    • (2003) Nature , vol.426 , pp. 39-44
    • Pebay-Peyroula, E.1
  • 103
    • 0027222094 scopus 로고
    • The topology of the brown adipose tissue mitochondrial uncoupling protein determined with antibodies against its antigenic sites revealed by a library of fusion proteins
    • Miroux, B., Frossard, V., Raimbault, S., Ricquier, D. & Bouillaud, P. The topology of the brown adipose tissue mitochondrial uncoupling protein determined with antibodies against its antigenic sites revealed by a library of fusion proteins. EMBO J. 12, 3739-3745 (1993).
    • (1993) EMBO J. , vol.12 , pp. 3739-3745
    • Miroux, B.1    Frossard, V.2    Raimbault, S.3    Ricquier, D.4    Bouillaud, P.5
  • 104
    • 0036139671 scopus 로고    scopus 로고
    • The mitochondrial uncoupling protein UCP1: A gated pore
    • Arechaga, I., Ledesma, A. & Rial, E. The mitochondrial uncoupling protein UCP1: a gated pore. IUBMB Life 52, 165-173 (2001).
    • (2001) IUBMB Life , vol.52 , pp. 165-173
    • Arechaga, I.1    Ledesma, A.2    Rial, E.3
  • 105
    • 0032995203 scopus 로고    scopus 로고
    • Structure-function relationship in UCP1
    • Mingenberg, M., Echtay, K. S., Bienengraeber, M., Winkler, E. & Huang, S. G. Structure-function relationship in UCP1. Int. J. Obes. Relat. Metab. Disord. 23(Suppl. 6), S24-S29 (1999). Comprehensive review of UCP1-mediated proton transport, summarizing the work that led to the formulation of the proton-buffering model.
    • (1999) Int. J. Obes. Relat. Metab. Disord. , vol.23 , Issue.SUPPL. 6
    • Mingenberg, M.1    Echtay, K.S.2    Bienengraeber, M.3    Winkler, E.4    Huang, S.G.5
  • 106
    • 0030881775 scopus 로고    scopus 로고
    • Identification by site-directed mutagenesis of three arginines in uncoupling protein that are essential for nucleotide binding and inhibition
    • Modriansky, M., Murdza-Inglis, D. L., Patel, H. V., Freeman, K. B. & Garlid, K. D. Identification by site-directed mutagenesis of three arginines in uncoupling protein that are essential for nucleotide binding and inhibition. J. Biol. Chem. 272, 24759-24762 (1997). Important paper showing the critical role of arginine residues in mediating inhibition of UCP1 by purine nucleotides.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24759-24762
    • Modriansky, M.1    Murdza-Inglis, D.L.2    Patel, H.V.3    Freeman, K.B.4    Garlid, K.D.5
  • 107
    • 0034972150 scopus 로고    scopus 로고
    • A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans
    • Esterbauer, H. et al. A common polymorphism in the promoter of UCP2 is associated with decreased risk of obesity in middle-aged humans. Nature Genet. 28, 178-183 (2001).
    • (2001) Nature Genet. , vol.28 , pp. 178-183
    • Esterbauer, H.1
  • 108
    • 0036830548 scopus 로고    scopus 로고
    • A functional polymorphism in the promoter of UCP2 enhances obesity risk but reduces type 2 diabetes risk in obese middle-aged humans
    • Krempler, F. et al. A functional polymorphism in the promoter of UCP2 enhances obesity risk but reduces type 2 diabetes risk in obese middle-aged humans. Diabetes 51, 3331-3335 (2002).
    • (2002) Diabetes , vol.51 , pp. 3331-3335
    • Krempler, F.1
  • 109
    • 12444292715 scopus 로고    scopus 로고
    • A common polymorphism in the promoter of UCP2 contributes to the variation in insulin secretion in glucose-tolerant subjects
    • Sesti, G. et al. A common polymorphism in the promoter of UCP2 contributes to the variation in insulin secretion in glucose-tolerant subjects. Diabetes 52, 1280-1283 (2003).
    • (2003) Diabetes , vol.52 , pp. 1280-1283
    • Sesti, G.1
  • 110
    • 10744222893 scopus 로고    scopus 로고
    • Uncoupling protein 2 promoter polymorphism -866G/A affects its expression in β-cells and modulates clinical profiles of Japanese type 2 diabetic patients
    • Sasahara, M. et al. Uncoupling protein 2 promoter polymorphism -866G/A affects its expression in β-cells and modulates clinical profiles of Japanese type 2 diabetic patients. Diabetes 53, 482-485 (2004).
    • (2004) Diabetes , vol.53 , pp. 482-485
    • Sasahara, M.1
  • 111
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820 (2001).
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 112
    • 0035856942 scopus 로고    scopus 로고
    • Mitochondrial function in normal and diabetic β-cells
    • Maechler, P. & Wollheim, C. B. Mitochondrial function in normal and diabetic β-cells. Nature 414, 807-812 (2001).
    • (2001) Nature , vol.414 , pp. 807-812
    • Maechler, P.1    Wollheim, C.B.2
  • 113
    • 0033856196 scopus 로고    scopus 로고
    • Oxygen consumption oscillates in single donal pancreatic β-cells (HIT)
    • Porterfield, D. M. et al. Oxygen consumption oscillates in single donal pancreatic β-cells (HIT). Diabetes 49, 1511-1516 (2000).
    • (2000) Diabetes , vol.49 , pp. 1511-1516
    • Porterfield, D.M.1
  • 114
    • 44949272730 scopus 로고
    • A time-efficient, linear-space local similarity algorithm
    • Huang, X. & Miller, W. E. A time-efficient, linear-space local similarity algorithm. Adv. Appl. Math. 12, 337-357 (1991).
    • (1991) Adv. Appl. Math. , vol.12 , pp. 337-357
    • Huang, X.1    Miller, W.E.2


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