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Volumn 49, Issue 3, 2010, Pages 512-521

A comparative study on conformation and ligand binding of the neuronal uncoupling proteins

Author keywords

[No Author keywords available]

Indexed keywords

, INHIBITOR; CD AND FLUORESCENCE SPECTROSCOPY; CENTRAL NERVOUS SYSTEMS; COMPARATIVE STUDIES; FUNCTIONAL PROPERTIES; HELICAL CONFORMATION; LIGAND BINDING; MICROENVIRONMENTS; MOLAR RATIO; NERVOUS SYSTEM; NUCLEOTIDE BINDING; NUCLEOTIDE-BINDING SITES; PHOSPHOLIPID VESICLES; PRIMARY SEQUENCES; PROTEOLIPOSOMES; PROTON TRANSPORT; PURINE NUCLEOTIDES; SMALL UNILAMELLAR VESICLE; SPECTROSCOPIC STUDIES; STRUCTURAL INFORMATION; UNCOUPLING PROTEINS;

EID: 74949093836     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901742g     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 34948890043 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins - what is their physiological role?
    • Echtay, K. S. (2007) Mitochondrial uncoupling proteins - what is their physiological role? Free Radical Biol. Med. 43, 1351-1371.
    • (2007) Free Radical Biol. Med , vol.43 , pp. 1351-1371
    • Echtay, K.S.1
  • 2
  • 4
    • 0032998265 scopus 로고    scopus 로고
    • UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells
    • Mao, W., Yu, X. X., Zhong, A., Li, W., Brush, J., Sherwood, S. W., Adams, S. H., and Pan, G. (1999) UCP4, a novel brain-specific mitochondrial protein that reduces membrane potential in mammalian cells. FEBS Lett. 443, 326-330.
    • (1999) FEBS Lett , vol.443 , pp. 326-330
    • Mao, W.1    Yu, X.X.2    Zhong, A.3    Li, W.4    Brush, J.5    Sherwood, S.W.6    Adams, S.H.7    Pan, G.8
  • 6
    • 27644448810 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins in the CNS: In support of function and survival
    • Andrews, Z. B., Diano, S., and Horvath, T. L. (2005) Mitochondrial uncoupling proteins in the CNS: in support of function and survival. Nat. Rev. Neurosci. 6, 829-840.
    • (2005) Nat. Rev. Neurosci , vol.6 , pp. 829-840
    • Andrews, Z.B.1    Diano, S.2    Horvath, T.L.3
  • 7
    • 33845985635 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein-4 regulates calcium homeostasis and sensitivity to store depletion-induced apoptosis in neuronal cells
    • Chan, S. L., Liu, D., Kyriazis, G. A., Bagsiyao, P., Ouyang, X., and Mattson,M. P. (2006) Mitochondrial uncoupling protein-4 regulates calcium homeostasis and sensitivity to store depletion-induced apoptosis in neuronal cells. J. Biol. Chem. 281, 37391-37403.
    • (2006) J. Biol. Chem , vol.281 , pp. 37391-37403
    • Chan, S.L.1    Liu, D.2    Kyriazis, G.A.3    Bagsiyao, P.4    Ouyang, X.5    Mattson, M.P.6
  • 10
    • 0034724170 scopus 로고    scopus 로고
    • Site-directed mutagenesis identifies residues in uncoupling protein (UCP1) involved in three different functions
    • Echtay, K. S., Winkler, E., Bienengraeber, M., and Klingenberg, M. (2000) Site-directed mutagenesis identifies residues in uncoupling protein (UCP1) involved in three different functions. Biochemistry 39, 3311-3317.
    • (2000) Biochemistry , vol.39 , pp. 3311-3317
    • Echtay, K.S.1    Winkler, E.2    Bienengraeber, M.3    Klingenberg, M.4
  • 12
    • 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
  • 14
    • 0035957755 scopus 로고    scopus 로고
    • Mitochondrial uncoupling proteins and phylogenesis - UCP4 as the ancestral uncoupling protein
    • Hanák, P., and Ježek, P. (2001) Mitochondrial uncoupling proteins and phylogenesis - UCP4 as the ancestral uncoupling protein. FEBS Lett. 495, 137-141.
    • (2001) FEBS Lett , vol.495 , pp. 137-141
    • Hanák, P.1    Ježek, P.2
  • 16
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton, L. A., and Johnson, W. C. (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155, 155-167.
    • (1986) Anal. Biochem , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson, W.C.2
  • 17
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson, W. C. (1999) Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins: Struct., Funct., Genet. 35, 307-312.
    • (1999) Proteins: Struct., Funct., Genet , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 18
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB: An online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 19
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • Lees, J. G., Miles, A. J., Wien, F., and Wallace, B. A. (2006) A reference database for circular dichroism spectroscopy covering fold and secondary structure space. Bioinformatics 22, 1955-1962.
    • (2006) Bioinformatics , vol.22 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 20
    • 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
  • 21
    • 0025055014 scopus 로고
    • Infrared spectroscopic studies of detergent-solubilized uncoupling protein from brown-adipose-tissue mitochondria
    • Rial, E., Muga, A., Valpuesta, J. M., Arrondo, J.-L.R., and Goni, F. M. (1990) Infrared spectroscopic studies of detergent-solubilized uncoupling protein from brown-adipose-tissue mitochondria. Eur. J. Biochem. 188, 83-89.
    • (1990) Eur. J. Biochem , vol.188 , pp. 83-89
    • Rial, E.1    Muga, A.2    Valpuesta, J.M.3    Arrondo, J.-L.R.4    Goni, F.M.5
  • 23
    • 0033387853 scopus 로고    scopus 로고
    • Anion carriers in fatty acid-mediated physiological uncoupling
    • Skulachev, V. P. (1999) Anion carriers in fatty acid-mediated physiological uncoupling. J. Bioenerg. Biomembr. 31, 431-445.
    • (1999) J. Bioenerg. Biomembr , vol.31 , pp. 431-445
    • Skulachev, V.P.1
  • 24
    • 70449345550 scopus 로고    scopus 로고
    • 14th ed, Merck & Co, Whitehouse Station, NJ
    • O'Neil, M. J. (2006) The Merck Index, 14th ed., Merck & Co., Whitehouse Station, NJ.
    • (2006) The Merck Index
    • O'Neil, M.J.1
  • 25
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao, D., and Wallace, B. A. (1984) Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23, 2667-2673.
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 26
    • 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
  • 27
    • 0037379159 scopus 로고    scopus 로고
    • Analyses of circular dichroism spectra of membrane proteins
    • Wallace, B. A., Lees, J. G., Orry, A. J. W., Lobley, A., and Janes, R. W. (2003) Analyses of circular dichroism spectra of membrane proteins. Protein Sci. 12, 875-884.
    • (2003) Protein Sci , vol.12 , pp. 875-884
    • Wallace, B.A.1    Lees, J.G.2    Orry, A.J.W.3    Lobley, A.4    Janes, R.W.5
  • 28
    • 0027076316 scopus 로고
    • Differentiation between transmembrane helices and peripheral helices by the deconvolution of circular dichroism spectra of membrane proteins
    • Park, K., Perczel, A., and Fasman, G. D. (1992) Differentiation between transmembrane helices and peripheral helices by the deconvolution of circular dichroism spectra of membrane proteins. Protein Sci. 1, 1032-1049.
    • (1992) Protein Sci , vol.1 , pp. 1032-1049
    • Park, K.1    Perczel, A.2    Fasman, G.D.3
  • 31
    • 41149151240 scopus 로고    scopus 로고
    • Ion-channel formation assisted by electrostatic interhelical interactions in covalently dimerized amphiphilic helical peptides
    • Taira, J., Jelokhani-Niaraki, M., Osada, S., Kato, F., and Kodama, H. (2008) Ion-channel formation assisted by electrostatic interhelical interactions in covalently dimerized amphiphilic helical peptides. Biochemistry 47, 3705-3714.
    • (2008) Biochemistry , vol.47 , pp. 3705-3714
    • Taira, J.1    Jelokhani-Niaraki, M.2    Osada, S.3    Kato, F.4    Kodama, H.5
  • 33
    • 0030956737 scopus 로고    scopus 로고
    • Fluorescence methods for studying equilibrium macromolecule-ligand interactions
    • Eftink, M. R. (1997) Fluorescence methods for studying equilibrium macromolecule-ligand interactions. Methods Enzymol. 278, 221-257.
    • (1997) Methods Enzymol , vol.278 , pp. 221-257
    • Eftink, M.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.