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Journal Abstract Search

417 related items for PubMed ID: 8914985

  • 1. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore.
    Beutner G, Ruck A, Riede B, Welte W, Brdiczka D.
    FEBS Lett; 1996 Nov 04; 396(2-3):189-95. PubMed ID: 8914985
    [Abstract] [Full Text] [Related]

  • 2. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases.
    Beutner G, Rück A, Riede B, Brdiczka D.
    Biochim Biophys Acta; 1998 Jan 05; 1368(1):7-18. PubMed ID: 9459579
    [Abstract] [Full Text] [Related]

  • 3. Complexes between hexokinase, mitochondrial porin and adenylate translocator in brain: regulation of hexokinase, oxidative phosphorylation and permeability transition pore.
    Beutner G, Rück A, Riede B, Brdiczka D.
    Biochem Soc Trans; 1997 Feb 05; 25(1):151-7. PubMed ID: 9056862
    [No Abstract] [Full Text] [Related]

  • 4. The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition.
    Brdiczka D, Beutner G, Rück A, Dolder M, Wallimann T.
    Biofactors; 1998 Feb 05; 8(3-4):235-42. PubMed ID: 9914825
    [Abstract] [Full Text] [Related]

  • 5. The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin.
    Benz R, Kottke M, Brdiczka D.
    Biochim Biophys Acta; 1990 Mar 05; 1022(3):311-8. PubMed ID: 1690571
    [Abstract] [Full Text] [Related]

  • 6. Porin proteins in mitochondria from rat pancreatic islet cells and white adipocytes: identification and regulation of hexokinase binding by the sulfonylurea glimepiride.
    Müller G, Korndörfer A, Kornak U, Malaisse WJ.
    Arch Biochem Biophys; 1994 Jan 05; 308(1):8-23. PubMed ID: 8311478
    [Abstract] [Full Text] [Related]

  • 7. The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis.
    Vyssokikh MY, Brdiczka D.
    Acta Biochim Pol; 2003 Jan 05; 50(2):389-404. PubMed ID: 12833165
    [Abstract] [Full Text] [Related]

  • 8. The intra-mitochondrial cytochrome c distribution varies correlated to the formation of a complex between VDAC and the adenine nucleotide translocase: this affects Bax-dependent cytochrome c release.
    Vyssokikh M, Zorova L, Zorov D, Heimlich G, Jürgensmeier J, Schreiner D, Brdiczka D.
    Biochim Biophys Acta; 2004 Feb 02; 1644(1):27-36. PubMed ID: 14741742
    [Abstract] [Full Text] [Related]

  • 9. Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translocator. Hexokinase activity suppresses this effect.
    Vyssokikh MY, Zorova L, Zorov D, Heimlich G, Jürgensmeier JJ, Brdiczka D.
    Mol Biol Rep; 2002 Feb 02; 29(1-2):93-6. PubMed ID: 12243190
    [Abstract] [Full Text] [Related]

  • 10. Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore.
    Crompton M, Virji S, Ward JM.
    Eur J Biochem; 1998 Dec 01; 258(2):729-35. PubMed ID: 9874241
    [Abstract] [Full Text] [Related]

  • 11. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin.
    Brdiczka D, Kaldis P, Wallimann T.
    J Biol Chem; 1994 Nov 04; 269(44):27640-4. PubMed ID: 7525559
    [Abstract] [Full Text] [Related]

  • 12. Adenine nucleotide translocator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D.
    Vyssokikh MY, Katz A, Rueck A, Wuensch C, Dörner A, Zorov DB, Brdiczka D.
    Biochem J; 2001 Sep 01; 358(Pt 2):349-58. PubMed ID: 11513733
    [Abstract] [Full Text] [Related]

  • 13. Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria.
    Fiek C, Benz R, Roos N, Brdiczka D.
    Biochim Biophys Acta; 1982 Jun 14; 688(2):429-40. PubMed ID: 6285967
    [Abstract] [Full Text] [Related]

  • 14. Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria.
    Baines CP, Song CX, Zheng YT, Wang GW, Zhang J, Wang OL, Guo Y, Bolli R, Cardwell EM, Ping P.
    Circ Res; 2003 May 02; 92(8):873-80. PubMed ID: 12663490
    [Abstract] [Full Text] [Related]

  • 15. The role of creatine kinase in inhibition of mitochondrial permeability transition.
    O'Gorman E, Beutner G, Dolder M, Koretsky AP, Brdiczka D, Wallimann T.
    FEBS Lett; 1997 Sep 08; 414(2):253-7. PubMed ID: 9315696
    [Abstract] [Full Text] [Related]

  • 16. VDAC and peripheral channelling complexes in health and disease.
    Vyssokikh M, Brdiczka D.
    Mol Cell Biochem; 2004 Sep 08; 256-257(1-2):117-26. PubMed ID: 14977175
    [Abstract] [Full Text] [Related]

  • 17. Factors determining the relative contribution of the adenine-nucleotide translocator and the ADP-regenerating system to the control of oxidative phosphorylation in isolated rat-liver mitochondria.
    Wanders RJ, Groen AK, Van Roermund CW, Tager JM.
    Eur J Biochem; 1984 Jul 16; 142(2):417-24. PubMed ID: 6086353
    [Abstract] [Full Text] [Related]

  • 18. Pore formation by the mitochondrial porin of rat brain in lipid bilayer membranes.
    Ludwig O, De Pinto V, Palmieri F, Benz R.
    Biochim Biophys Acta; 1986 Aug 21; 860(2):268-76. PubMed ID: 2427116
    [Abstract] [Full Text] [Related]

  • 19. Mitochondrial creatine kinase in contact sites: interaction with porin and adenine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage.
    Dolder M, Wendt S, Wallimann T.
    Biol Signals Recept; 2001 Aug 21; 10(1-2):93-111. PubMed ID: 11223643
    [Abstract] [Full Text] [Related]

  • 20. VDAC electronics: 2. A new, anaerobic mechanism of generation of the membrane potentials in mitochondria.
    Lemeshko VV.
    Biochim Biophys Acta; 2014 Jul 21; 1838(7):1801-8. PubMed ID: 24565793
    [Abstract] [Full Text] [Related]

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