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Volumn 290, Issue 13, 2015, Pages 8206-8217

Trends in thermostability provide information on the nature of substrate, inhibitor, and lipid interactions with mitochondrial carriers

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; STABILITY;

EID: 84925798847     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.616607     Document Type: Article
Times cited : (68)

References (59)
  • 1
    • 84875218644 scopus 로고    scopus 로고
    • The mitochondrial transporter family SLC25: Identification, properties and physiopathology
    • Palmieri, F. (2013) The mitochondrial transporter family SLC25: identification, properties and physiopathology. Mol. Aspects Med. 34, 465-484
    • (2013) Mol. Aspects Med. , vol.34 , pp. 465-484
    • Palmieri, F.1
  • 2
    • 46349088952 scopus 로고    scopus 로고
    • Diseases caused by defects of mitochondrial carriers: A review
    • Palmieri, F. (2008) Diseases caused by defects of mitochondrial carriers: a review. Biochim. Biophys. Acta 1777, 564-578
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 564-578
    • Palmieri, F.1
  • 5
    • 0020473533 scopus 로고
    • Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase
    • Saraste, M., and Walker, J. E. (1982) Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase. FEBS Lett. 144, 250-254
    • (1982) FEBS Lett. , vol.144 , pp. 250-254
    • Saraste, M.1    Walker, J.E.2
  • 6
    • 0023118165 scopus 로고
    • Solute carriers involved in energy transfer of mitochondria form a homologous protein family
    • Aquila, H., Link, T. A., and Klingenberg, M. (1987) Solute carriers involved in energy transfer of mitochondria form a homologous protein family. FEBS Lett. 212, 1-9
    • (1987) FEBS Lett. , vol.212 , pp. 1-9
    • Aquila, H.1    Link, T.A.2    Klingenberg, M.3
  • 8
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg, M. (2008) The ADP and ATP transport in mitochondria and its carrier. Biochim. Biophys. Acta. 1778, 1978-2021
    • (2008) Biochim. Biophys. Acta. , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 9
    • 0015919573 scopus 로고
    • Adenosine diphosphate translocation in mitochondria: Nature of the receptor site for carboxyatractyloside (gummiferin)
    • Vignais, P. V., Vignais, P. M., and Defaye, G. (1973) Adenosine diphosphate translocation in mitochondria: nature of the receptor site for carboxyatractyloside (gummiferin). Biochemistry 12, 1508-1519
    • (1973) Biochemistry , vol.12 , pp. 1508-1519
    • Vignais, P.V.1    Vignais, P.M.2    Defaye, G.3
  • 10
    • 0014961595 scopus 로고
    • Bongkrekic acid. An inhibitor of the adenine nucleotide translocase of mitochondria
    • Henderson, P. J., and Lardy, H. A. (1970) Bongkrekic acid. An inhibitor of the adenine nucleotide translocase of mitochondria. J. Biol. Chem. 245, 1319-1326
    • (1970) J. Biol. Chem. , vol.245 , pp. 1319-1326
    • Henderson, P.J.1    Lardy, H.A.2
  • 11
    • 0141484658 scopus 로고    scopus 로고
    • Projection structure of the atractyloside- inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae
    • Kunji, E. R., and Harding, M. (2003) Projection structure of the atractyloside- inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae. J. Biol. Chem. 278, 36985-36988
    • (2003) J. Biol. Chem. , vol.278 , pp. 36985-36988
    • Kunji, E.R.1    Harding, M.2
  • 12
  • 13
    • 84893401009 scopus 로고    scopus 로고
    • Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism
    • Ruprecht, J. J., Hellawell, A. M., Harding, M., Crichton, P. G., McCoy, A. J., and Kunji, E. R. (2014) Structures of yeast mitochondrial ADP/ATP carriers support a domain-based alternating-access transport mechanism. Proc. Natl. Acad. Sci. U.S.A. 111, E426-E434
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E426-E434
    • Ruprecht, J.J.1    Hellawell, A.M.2    Harding, M.3    Crichton, P.G.4    McCoy, A.J.5    Kunji, E.R.6
  • 14
    • 0032571303 scopus 로고    scopus 로고
    • Highly conserved charge-pair networks in the mitochondrial carrier family
    • Nelson, D. R., Felix, C. M., and Swanson, J. M. (1998) Highly conserved charge-pair networks in the mitochondrial carrier family. J. Mol. Biol. 277, 285-308
    • (1998) J. Mol. Biol. , vol.277 , pp. 285-308
    • Nelson, D.R.1    Felix, C.M.2    Swanson, J.M.3
  • 15
    • 77953807486 scopus 로고    scopus 로고
    • Mitochondrial carriers function as monomers
    • Kunji, E. R., and Crichton, P. G. (2010) Mitochondrial carriers function as monomers. Biochim. Biophys. Acta. 1797, 817-831
    • (2010) Biochim. Biophys. Acta. , vol.1797 , pp. 817-831
    • Kunji, E.R.1    Crichton, P.G.2
  • 16
    • 33644555509 scopus 로고    scopus 로고
    • Mitochondrial carriers in the cytoplasmic state have a common substrate binding site
    • Robinson, A. J., and Kunji, E. R. (2006) Mitochondrial carriers in the cytoplasmic state have a common substrate binding site. Proc. Natl. Acad. Sci. U.S.A. 103, 2617-2622
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2617-2622
    • Robinson, A.J.1    Kunji, E.R.2
  • 17
    • 56649103828 scopus 로고    scopus 로고
    • The mechanism of transport by mitochondrial carriers based on analysis of symmetry
    • Robinson, A. J., Overy, C., and Kunji, E. R. (2008) The mechanism of transport by mitochondrial carriers based on analysis of symmetry. Proc. Natl. Acad. Sci. U.S.A. 105, 17766-17771
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 17766-17771
    • Robinson, A.J.1    Overy, C.2    Kunji, E.R.3
  • 18
    • 52449099841 scopus 로고    scopus 로고
    • Binding of ADP in the mitochondrial ADP/ATP carrier is driven by an electrostatic funnel
    • Dehez, F., Pebay-Peyroula, E., and Chipot, C. (2008) Binding of ADP in the mitochondrial ADP/ATP carrier is driven by an electrostatic funnel. J. Am. Chem. Soc. 130, 12725-12733
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12725-12733
    • Dehez, F.1    Pebay-Peyroula, E.2    Chipot, C.3
  • 19
    • 47749085530 scopus 로고    scopus 로고
    • Electrostatic funneling of substrate in mitochondrial inner membrane carriers
    • Wang, Y., and Tajkhorshid, E. (2008) Electrostatic funneling of substrate in mitochondrial inner membrane carriers. Proc. Natl. Acad. Sci. U.S.A. 105, 9598-9603
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9598-9603
    • Wang, Y.1    Tajkhorshid, E.2
  • 20
    • 84858031501 scopus 로고    scopus 로고
    • Substrate specificity of the two mitochondrial ornithine carriers can be swapped by single mutation in substrate binding site
    • Monné, M., Miniero, D. V., Daddabbo, L., Robinson, A. J., Kunji, E. R., and Palmieri, F. (2012) Substrate specificity of the two mitochondrial ornithine carriers can be swapped by single mutation in substrate binding site. J. Biol. Chem. 287, 7925-7934
    • (2012) J. Biol. Chem. , vol.287 , pp. 7925-7934
    • Monné, M.1    Miniero, D.V.2    Daddabbo, L.3    Robinson, A.J.4    Kunji, E.R.5    Palmieri, F.6
  • 21
    • 80054051101 scopus 로고    scopus 로고
    • The regulation and physiology of mitochondrial proton leak
    • Divakaruni, A. S., and Brand, M. D. (2011) The regulation and physiology of mitochondrial proton leak. Physiology 26, 192-205
    • (2011) Physiology , vol.26 , pp. 192-205
    • Divakaruni, A.S.1    Brand, M.D.2
  • 22
    • 0016734199 scopus 로고
    • Purification of the carboxy- atractylate binding protein from mitochondria
    • Riccio, P., Aquila, H., and Klingenberg, M. (1975) Purification of the carboxy- atractylate binding protein from mitochondria. FEBS Lett. 56, 133-138
    • (1975) FEBS Lett. , vol.56 , pp. 133-138
    • Riccio, P.1    Aquila, H.2    Klingenberg, M.3
  • 23
    • 0016537503 scopus 로고
    • Solubilization of the carboxy-atractylate binding protein from mitochondria
    • Riccio, P., Aquila, H., and Klingenberg, M. (1975) Solubilization of the carboxy-atractylate binding protein from mitochondria. FEBS Lett. 56, 192-232
    • (1975) FEBS Lett. , vol.56 , pp. 192-232
    • Riccio, P.1    Aquila, H.2    Klingenberg, M.3
  • 24
  • 25
    • 55649115081 scopus 로고    scopus 로고
    • Determination of the molecular mass and dimensions of membrane proteins by size exclusion chromatography
    • Kunji, E. R., Harding, M., Butler, P. J., and Akamine, P. (2008) Determination of the molecular mass and dimensions of membrane proteins by size exclusion chromatography. Methods 46, 62-72
    • (2008) Methods , vol.46 , pp. 62-72
    • Kunji, E.R.1    Harding, M.2    Butler, P.J.3    Akamine, P.4
  • 26
    • 0024558293 scopus 로고
    • Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria
    • Krämer, R., and Palmieri, F. (1989) Molecular aspects of isolated and reconstituted carrier proteins from animal mitochondria. Biochim. Biophys. Acta. 974, 1-23
    • (1989) Biochim. Biophys. Acta. , vol.974 , pp. 1-23
    • Krämer, R.1    Palmieri, F.2
  • 27
    • 70349518563 scopus 로고    scopus 로고
    • Cardiolipin and mitochondrial carriers
    • Klingenberg, M. (2009) Cardiolipin and mitochondrial carriers. Biochim. Biophys. Acta. 1788, 2048-2058
    • (2009) Biochim. Biophys. Acta. , vol.1788 , pp. 2048-2058
    • Klingenberg, M.1
  • 28
    • 0020477476 scopus 로고
    • Characteristics of the isolated purine nucleotide binding protein from brown fat mitochondria
    • Lin, C. S., and Klingenberg, M. (1982) Characteristics of the isolated purine nucleotide binding protein from brown fat mitochondria. Biochemistry 21, 2950-2956
    • (1982) Biochemistry , vol.21 , pp. 2950-2956
    • Lin, C.S.1    Klingenberg, M.2
  • 29
    • 84885601713 scopus 로고    scopus 로고
    • Dangerous liaisons between detergents and membrane proteins: The case of mitochondrial uncoupling protein 2
    • Zoonens, M., Comer, J., Masscheleyn, S., Pebay-Peyroula, E., Chipot, C., Miroux, B., and Dehez, F. (2013) Dangerous liaisons between detergents and membrane proteins: the case of mitochondrial uncoupling protein 2. J. Am. Chem. Soc. 135, 15174-15182
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 15174-15182
    • Zoonens, M.1    Comer, J.2    Masscheleyn, S.3    Pebay-Peyroula, E.4    Chipot, C.5    Miroux, B.6    Dehez, F.7
  • 30
    • 84890928961 scopus 로고    scopus 로고
    • Expression, folding, and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: Evidence for associated functional forms
    • Hoang, T., Smith, M. D., and Jelokhani-Niaraki, M. (2013) Expression, folding, and proton transport activity of human uncoupling protein-1 (UCP1) in lipid membranes: evidence for associated functional forms. J. Biol. Chem. 288, 36244-36258
    • (2013) J. Biol. Chem. , vol.288 , pp. 36244-36258
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3
  • 31
    • 79961168437 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching
    • Berardi, M. J., Shih, W. M., Harrison, S. C., and Chou, J. J. (2011) Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching. Nature 476, 109-113
    • (2011) Nature , vol.476 , pp. 109-113
    • Berardi, M.J.1    Shih, W.M.2    Harrison, S.C.3    Chou, J.J.4
  • 32
    • 40049099087 scopus 로고    scopus 로고
    • Microscale fluorescent thermal stability assay for membrane proteins
    • Alexandrov, A. I., Mileni, M., Chien, E. Y., Hanson, M. A., and Stevens, R. C. (2008) Microscale fluorescent thermal stability assay for membrane proteins. Structure 16, 351-359
    • (2008) Structure , vol.16 , pp. 351-359
    • Alexandrov, A.I.1    Mileni, M.2    Chien, E.Y.3    Hanson, M.A.4    Stevens, R.C.5
  • 33
    • 0032923151 scopus 로고    scopus 로고
    • Expression of the bovine heart mitochondrial ADP/ ATP carrier in yeast mitochondria: Significantly enhanced expression by replacement of the N-terminal region of the bovine carrier by the corresponding regions of the yeast carriers
    • Hashimoto, M., Shinohara, Y., Majima, E., Hatanaka, T., Yamazaki, N., and Terada, H. (1999) Expression of the bovine heart mitochondrial ADP/ ATP carrier in yeast mitochondria: significantly enhanced expression by replacement of the N-terminal region of the bovine carrier by the corresponding regions of the yeast carriers. Biochim. Biophys. Acta 1409, 113-124
    • (1999) Biochim. Biophys. Acta , vol.1409 , pp. 113-124
    • Hashimoto, M.1    Shinohara, Y.2    Majima, E.3    Hatanaka, T.4    Yamazaki, N.5    Terada, H.6
  • 34
    • 84923239495 scopus 로고    scopus 로고
    • Calciuminduced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers
    • Thangaratnarajah, C., Ruprecht, J. J., and Kunji, E. R. (2014) Calciuminduced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers. Nat. Commun. 5, 5491
    • (2014) Nat. Commun. , vol.5 , pp. 5491
    • Thangaratnarajah, C.1    Ruprecht, J.J.2    Kunji, E.R.3
  • 35
    • 0018337321 scopus 로고
    • Mitochondria from brown adipose tissue: Isolation and properties
    • Cannon, B., and Lindberg, O. (1979) Mitochondria from brown adipose tissue: isolation and properties. Methods Enzymol. 55, 65-78
    • (1979) Methods Enzymol. , vol.55 , pp. 65-78
    • Cannon, B.1    Lindberg, O.2
  • 36
    • 84881237077 scopus 로고    scopus 로고
    • Lipid, detergent, and Coomassie Blue G-250 affect the migration of small membrane proteins in blue native gels: Mitochondrial carriers migrate as monomers not dimers
    • Crichton, P. G., Harding, M., Ruprecht, J. J., Lee, Y., and Kunji, E. R. (2013) Lipid, detergent, and Coomassie Blue G-250 affect the migration of small membrane proteins in blue native gels: mitochondrial carriers migrate as monomers not dimers. J. Biol. Chem. 288, 22163-22173
    • (2013) J. Biol. Chem. , vol.288 , pp. 22163-22173
    • Crichton, P.G.1    Harding, M.2    Ruprecht, J.J.3    Lee, Y.4    Kunji, E.R.5
  • 37
    • 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., and Brand, M. D. (2001) A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast. Biochem. J. 356, 779-789
    • (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
  • 39
    • 0030836775 scopus 로고    scopus 로고
    • Mutagenesis of the uncoupling protein of brown adipose tissue. Neutralization of E190 largely abolishes pH control of nucleotide binding
    • Echtay, K. S., Bienengraeber, M., and Klingenberg, M. (1997) Mutagenesis of the uncoupling protein of brown adipose tissue. Neutralization Of E190 largely abolishes pH control of nucleotide binding. Biochemistry 36, 8253-8260
    • (1997) Biochemistry , vol.36 , pp. 8253-8260
    • Echtay, K.S.1    Bienengraeber, M.2    Klingenberg, M.3
  • 40
    • 16344382388 scopus 로고    scopus 로고
    • Thermodynamic stability of carbonic anhydrase: Measurements of binding affinity and stoichiometry using Thermo Fluor
    • Matulis, D., Kranz, J. K., Salemme, F. R., and Todd, M. J. (2005) Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using Thermo Fluor. Biochemistry 44, 5258-5266
    • (2005) Biochemistry , vol.44 , pp. 5258-5266
    • Matulis, D.1    Kranz, J.K.2    Salemme, F.R.3    Todd, M.J.4
  • 41
    • 19044379861 scopus 로고    scopus 로고
    • Comparative genomics of two closely related unicellular thermo-acidophilic red algae, Galdieria sulphuraria and Cyanidioschyzon merolae, reveals the molecular basis of the metabolic flexibility of Galdieria sulphuraria and significant differences in carbohydrate metabolism of both algae
    • Barbier, G., Oesterhelt, C., Larson, M. D., Halgren, R. G., Wilkerson, C., Garavito, R. M., Benning, C., and Weber, A. P. (2005) Comparative genomics of two closely related unicellular thermo-acidophilic red algae, Galdieria sulphuraria and Cyanidioschyzon merolae, reveals the molecular basis of the metabolic flexibility of Galdieria sulphuraria and significant differences in carbohydrate metabolism of both algae. Plant Physiol. 137, 460-474
    • (2005) Plant Physiol. , vol.137 , pp. 460-474
    • Barbier, G.1    Oesterhelt, C.2    Larson, M.D.3    Halgren, R.G.4    Wilkerson, C.5    Garavito, R.M.6    Benning, C.7    Weber, A.P.8
  • 44
    • 0024539333 scopus 로고
    • The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups
    • Klingenberg, M., and Appel, M. (1989) The uncoupling protein dimer can form a disulfide cross-link between the mobile C-terminal SH groups. Eur. J. Biochem. 180, 123-131
    • (1989) Eur. J. Biochem. , vol.180 , pp. 123-131
    • Klingenberg, M.1    Appel, M.2
  • 45
    • 0024297516 scopus 로고
    • Nucleotide binding to uncoupling protein: Mechanism of control by protonation
    • Klingenberg, M. (1988) Nucleotide binding to uncoupling protein: mechanism of control by protonation. Biochemistry 27, 781-791
    • (1988) Biochemistry , vol.27 , pp. 781-791
    • Klingenberg, M.1
  • 46
    • 84867564026 scopus 로고    scopus 로고
    • Mechanism of fattyacid- dependent UCP1 uncoupling in brown fat mitochondria
    • Fedorenko, A., Lishko, P. V., and Kirichok, Y. (2012) Mechanism of fattyacid- dependent UCP1 uncoupling in brown fat mitochondria. Cell 151, 400-413
    • (2012) Cell , vol.151 , pp. 400-413
    • Fedorenko, A.1    Lishko, P.V.2    Kirichok, Y.3
  • 47
    • 0032901360 scopus 로고    scopus 로고
    • Structure and function of the uncoupling protein from brown adipose tissue
    • Klingenberg, M., and Huang, S. G. (1999) Structure and function of the uncoupling protein from brown adipose tissue. Biochim. Biophys. Acta 1415, 271-296
    • (1999) Biochim. Biophys. Acta , vol.1415 , pp. 271-296
    • Klingenberg, M.1    Huang, S.G.2
  • 48
    • 0032582799 scopus 로고    scopus 로고
    • The mechanism of proton transport mediated by mitochondrial uncoupling proteins
    • Garlid, K. D., Jaburek, M., and Jezek, P. (1998) The mechanism of proton transport mediated by mitochondrial uncoupling proteins. FEBS Lett. 438, 10-14
    • (1998) FEBS Lett. , vol.438 , pp. 10-14
    • Garlid, K.D.1    Jaburek, M.2    Jezek, P.3
  • 49
    • 4644295401 scopus 로고    scopus 로고
    • Native UCP1 displays simple competitive kinetics between the regulators purine nucleotides and fatty acids
    • Shabalina, I. G., Jacobsson, A., Cannon, B., and Nedergaard, J. (2004) Native UCP1 displays simple competitive kinetics between the regulators purine nucleotides and fatty acids. J. Biol. Chem. 279, 38236-38248
    • (2004) J. Biol. Chem. , vol.279 , pp. 38236-38248
    • Shabalina, I.G.1    Jacobsson, A.2    Cannon, B.3    Nedergaard, J.4
  • 52
    • 0022427458 scopus 로고
    • ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance
    • Beyer, K., and Klingenberg, M. (1985) ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance. Biochemistry 24, 3821-3826
    • (1985) Biochemistry , vol.24 , pp. 3821-3826
    • Beyer, K.1    Klingenberg, M.2
  • 53
    • 84868256765 scopus 로고    scopus 로고
    • Fatty acids change the conformation of uncoupling protein 1 (UCP1)
    • Divakaruni, A. S., Humphrey, D. M., and Brand, M. D. (2012) Fatty acids change the conformation of uncoupling protein 1 (UCP1) J. Biol. Chem. 287, 36845-36853
    • (2012) J. Biol. Chem. , vol.287 , pp. 36845-36853
    • Divakaruni, A.S.1    Humphrey, D.M.2    Brand, M.D.3
  • 54
    • 0023662148 scopus 로고
    • In the uncoupling protein from brown adipose tissue the C-terminus protrudes to the c-side of the membrane as shown by tryptic cleavage
    • Eckerskorn, C., and Klingenberg, M. (1987) In the uncoupling protein from brown adipose tissue the C-terminus protrudes to the c-side of the membrane as shown by tryptic cleavage. FEBS Lett. 226, 166-170
    • (1987) FEBS Lett. , vol.226 , pp. 166-170
    • Eckerskorn, C.1    Klingenberg, M.2
  • 55
    • 2642574988 scopus 로고    scopus 로고
    • Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast
    • Douette, P., Navet, R., Bouillenne, F., Brans, A., Sluse-Goffart, C., Matagne, A., and Sluse, F. E. (2004) Secondary-structure characterization by far-UV CD of highly purified uncoupling protein 1 expressed in yeast. Biochem. J. 380, 139-145
    • (2004) Biochem. J. , vol.380 , pp. 139-145
    • Douette, P.1    Navet, R.2    Bouillenne, F.3    Brans, A.4    Sluse-Goffart, C.5    Matagne, A.6    Sluse, F.E.7
  • 56
    • 74949093836 scopus 로고    scopus 로고
    • A comparative study on conformation and ligand binding of the neuronal uncoupling proteins
    • Ivanova, M. V., Hoang, T., McSorley, F. R., Krnac, G., Smith, M. D., and Jelokhani-Niaraki, M. (2010) A comparative study on conformation and ligand binding of the neuronal uncoupling proteins. Biochemistry 49, 512-521
    • (2010) Biochemistry , vol.49 , pp. 512-521
    • Ivanova, M.V.1    Hoang, T.2    McSorley, F.R.3    Krnac, G.4    Smith, M.D.5    Jelokhani-Niaraki, M.6
  • 58
    • 84855784885 scopus 로고    scopus 로고
    • Production of UCP1 a membrane protein from the inner mitochondrial membrane using the cell free expression system in the presence of a fluorinated surfactant
    • Blesneac, I., Ravaud, S., Juillan-Binard, C., Barret, L. A., Zoonens, M., Polidori, A., Miroux, B., Pucci, B., and Pebay-Peyroula, E. (2012) Production of UCP1 a membrane protein from the inner mitochondrial membrane using the cell free expression system in the presence of a fluorinated surfactant. Biochim. Biophys. Acta. 1818, 798-805
    • (2012) Biochim. Biophys. Acta. , vol.1818 , pp. 798-805
    • Blesneac, I.1    Ravaud, S.2    Juillan-Binard, C.3    Barret, L.A.4    Zoonens, M.5    Polidori, A.6    Miroux, B.7    Pucci, B.8    Pebay-Peyroula, E.9
  • 59
    • 84861134135 scopus 로고    scopus 로고
    • Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5
    • Hoang, T., Smith, M. D., and Jelokhani-Niaraki, M. (2012) Toward understanding the mechanism of ion transport activity of neuronal uncoupling proteins UCP2, UCP4, and UCP5. Biochemistry 51, 4004-4014
    • (2012) Biochemistry , vol.51 , pp. 4004-4014
    • Hoang, T.1    Smith, M.D.2    Jelokhani-Niaraki, M.3


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