메뉴 건너뛰기




Volumn 18, Issue 1, 2010, Pages 39-46

Probing the Interactions of Carboxy-atractyloside and Atractyloside with the Yeast Mitochondrial ADP/ATP Carrier

Author keywords

PROTEINS

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; ATRACTYLOSIDE; CARBOXYATRACTYLOSIDE;

EID: 73449133713     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.11.009     Document Type: Article
Times cited : (39)

References (33)
  • 2
    • 67650632375 scopus 로고    scopus 로고
    • Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter
    • Bippes C.A., Zeltina A., Casagrande F., Ratera M., Palacin M., Muller D.J., and Fotiadis D. Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter. J. Biol. Chem. 284 (2009) 18651-18663
    • (2009) J. Biol. Chem. , vol.284 , pp. 18651-18663
    • Bippes, C.A.1    Zeltina, A.2    Casagrande, F.3    Ratera, M.4    Palacin, M.5    Muller, D.J.6    Fotiadis, D.7
  • 3
    • 0242606610 scopus 로고
    • Inhibition by atractyloside of the binding of adenine-nucleotides to rat-liver mitochondria
    • Bruni A., Luciani S., and Contessa A.R. Inhibition by atractyloside of the binding of adenine-nucleotides to rat-liver mitochondria. Nature 201 (1964) 1219-1220
    • (1964) Nature , vol.201 , pp. 1219-1220
    • Bruni, A.1    Luciani, S.2    Contessa, A.R.3
  • 4
    • 34347209835 scopus 로고
    • Calculation of thermal noise in atomic-force microscopy
    • Butt H., and Jaschke M. Calculation of thermal noise in atomic-force microscopy. Nanotechnology 6 (1995) 1-7
    • (1995) Nanotechnology , vol.6 , pp. 1-7
    • Butt, H.1    Jaschke, M.2
  • 8
    • 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. Binding of ADP in the mitochondrial ADP/ATP carrier is driven by an electrostatic funnel. J. Am. Chem. Soc. 130 (2008) 12725-12733
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12725-12733
    • Dehez, F.1    Pebay-Peyroula, E.2    Chipot, C.3
  • 9
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans E., and Ritchie K. Dynamic strength of molecular adhesion bonds. Biophys. J. 72 (1997) 1541-1555
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 10
    • 0001066319 scopus 로고    scopus 로고
    • Dynamic strengths of molecular anchoring and material cohesion in fluid biomembranes
    • Evans E., and Ludwig F. Dynamic strengths of molecular anchoring and material cohesion in fluid biomembranes. J. Phys. Condens. Matter 12 (2000) A315-A320
    • (2000) J. Phys. Condens. Matter , vol.12
    • Evans, E.1    Ludwig, F.2
  • 13
    • 43649083578 scopus 로고    scopus 로고
    • From valleys to ridges: exploring the dynamic energy landscape of single membrane proteins
    • Janovjak H., Sapra K.T., Kedrov A., and Muller D.J. From valleys to ridges: exploring the dynamic energy landscape of single membrane proteins. ChemPhysChem 9 (2008) 954-966
    • (2008) ChemPhysChem , vol.9 , pp. 954-966
    • Janovjak, H.1    Sapra, K.T.2    Kedrov, A.3    Muller, D.J.4
  • 14
    • 56849094008 scopus 로고    scopus 로고
    • Conformational dynamics of the mitochondrial ADP/ATP carrier: a simulation study
    • Johnston J.M., Khalid S., and Sansom M.S. Conformational dynamics of the mitochondrial ADP/ATP carrier: a simulation study. Mol. Membr. Biol. 25 (2008) 506-517
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 506-517
    • Johnston, J.M.1    Khalid, S.2    Sansom, M.S.3
  • 15
    • 3242796697 scopus 로고    scopus 로고
    • Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy
    • Kedrov A., Ziegler C., Janovjak H., Kuhlbrandt W., and Muller D.J. Controlled unfolding and refolding of a single sodium-proton antiporter using atomic force microscopy. J. Mol. Biol. 340 (2004) 1143-1152
    • (2004) J. Mol. Biol. , vol.340 , pp. 1143-1152
    • Kedrov, A.1    Ziegler, C.2    Janovjak, H.3    Kuhlbrandt, W.4    Muller, D.J.5
  • 16
    • 33748467970 scopus 로고    scopus 로고
    • Differentiating ligand and inhibitor interactions of a single antiporter
    • Kedrov A., Ziegler C., and Muller D.J. Differentiating ligand and inhibitor interactions of a single antiporter. J. Mol. Biol. 362 (2006) 925-932
    • (2006) J. Mol. Biol. , vol.362 , pp. 925-932
    • Kedrov, A.1    Ziegler, C.2    Muller, D.J.3
  • 17
    • 34347259478 scopus 로고    scopus 로고
    • Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy
    • Kedrov A., Janovjak H., Sapra K.T., and Muller D.J. Deciphering molecular interactions of native membrane proteins by single-molecule force spectroscopy. Annu. Rev. Biophys. Biomol. Struct. 36 (2007) 233-260
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 233-260
    • Kedrov, A.1    Janovjak, H.2    Sapra, K.T.3    Muller, D.J.4
  • 18
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • Klingenberg M. Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270 (1989) 1-14
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 19
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg M. The ADP and ATP transport in mitochondria and its carrier. Biochim. Biophys. Acta 1778 (2008) 1978-2021
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 20
    • 0141484658 scopus 로고    scopus 로고
    • Projection structure of the atractyloside-inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae
    • Kunji E.R.S., and Harding M. Projection structure of the atractyloside-inhibited mitochondrial ADP/ATP carrier of Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 36985-36988
    • (2003) J. Biol. Chem. , vol.278 , pp. 36985-36988
    • Kunji, E.R.S.1    Harding, M.2
  • 21
    • 33748964653 scopus 로고    scopus 로고
    • The conserved substrate binding site of mitochondrial carriers
    • Kunji E.R.S., and Robinson A.J. The conserved substrate binding site of mitochondrial carriers. Biochim. Biophys. Acta 1757 (2006) 1237-1248
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1237-1248
    • Kunji, E.R.S.1    Robinson, A.J.2
  • 22
    • 0015215457 scopus 로고
    • Effects of carboxyatractyloside a structural analogue of atractyloside on mitochondrial oxidative phosphorylation
    • Luciani S., Martini N., and Santi R. Effects of carboxyatractyloside a structural analogue of atractyloside on mitochondrial oxidative phosphorylation. Life Sci. II. 10 (1971) 961-968
    • (1971) Life Sci. II. , vol.10 , pp. 961-968
    • Luciani, S.1    Martini, N.2    Santi, R.3
  • 23
    • 84970579743 scopus 로고
    • Bifloratoxin, a toxic aminoglycoside of carboxyatractyligenin, from Melanthera biflora
    • MacLeod J.K., Gaul K.L., and Oelrichs P.B. Bifloratoxin, a toxic aminoglycoside of carboxyatractyligenin, from Melanthera biflora. Aust. J. Chem. 43 (1990) 1533-1539
    • (1990) Aust. J. Chem. , vol.43 , pp. 1533-1539
    • MacLeod, J.K.1    Gaul, K.L.2    Oelrichs, P.B.3
  • 24
    • 48649106769 scopus 로고    scopus 로고
    • AFM: a nanotool in membrane biology
    • Muller D.J. AFM: a nanotool in membrane biology. Biochemistry 47 (2008) 7986-7998
    • (2008) Biochemistry , vol.47 , pp. 7986-7998
    • Muller, D.J.1
  • 27
    • 0013847968 scopus 로고
    • Unspecific permeation and specific exchange of adenine nucleotides in liver mitochondria
    • Pfaff E., Klingenberg M., and Heldt H.W. Unspecific permeation and specific exchange of adenine nucleotides in liver mitochondria. Biochim. Biophys. Acta 104 (1965) 312-315
    • (1965) Biochim. Biophys. Acta , vol.104 , pp. 312-315
    • Pfaff, E.1    Klingenberg, M.2    Heldt, H.W.3
  • 29
    • 33644555509 scopus 로고    scopus 로고
    • Mitochondrial carriers in the cytoplasmic state have a common substrate binding site
    • Robinson A.J., and Kunji E.R.S. Mitochondrial carriers in the cytoplasmic state have a common substrate binding site. Proc. Natl. Acad. Sci. USA 103 (2006) 2617-2622
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2617-2622
    • Robinson, A.J.1    Kunji, E.R.S.2
  • 30
    • 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.S. The mechanism of transport by mitochondrial carriers based on analysis of symmetry. Proc. Natl. Acad. Sci. USA 105 (2008) 17766-17771
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17766-17771
    • Robinson, A.J.1    Overy, C.2    Kunji, E.R.S.3
  • 31
    • 0020473533 scopus 로고
    • Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase
    • Saraste M., and Walker J.E. Internal sequence repeats and the path of polypeptide in mitochondrial ADP/ATP translocase. FEBS Lett. 144 (1982) 250-254
    • (1982) FEBS Lett. , vol.144 , pp. 250-254
    • Saraste, M.1    Walker, J.E.2
  • 32
    • 0010595341 scopus 로고
    • Gummiferin, an inhibitor of the adenine-nucleotide translocation. Study of its binding properties to mitochondria
    • Vignais P.V., Vignais P.M., and Defaye G. Gummiferin, an inhibitor of the adenine-nucleotide translocation. Study of its binding properties to mitochondria. FEBS Lett. 17 (1971) 281-288
    • (1971) FEBS Lett. , vol.17 , pp. 281-288
    • Vignais, P.V.1    Vignais, P.M.2    Defaye, G.3
  • 33
    • 47749085530 scopus 로고    scopus 로고
    • Electrostatic funneling of substrate in mitochondrial inner membrane carriers
    • Wang Y., and Tajkhorshid E. Electrostatic funneling of substrate in mitochondrial inner membrane carriers. Proc. Natl. Acad. Sci. USA 105 (2008) 9598-9603
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9598-9603
    • Wang, Y.1    Tajkhorshid, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.