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Journal Abstract Search

253 related items for PubMed ID: 19192627

  • 1. The voltage dependent anion selective channel family in Drosophila melanogaster.
    Guarino F, Messina A, Guarnera A, Puglia G, Bellia F, Reina S, De Pinto V, Specchia V, Bozzetti MP.
    Ital J Biochem; 2007 Dec; 56(4):279-84. PubMed ID: 19192627
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  • 2. Swapping of the N-terminus of VDAC1 with VDAC3 restores full activity of the channel and confers anti-aging features to the cell.
    Reina S, Palermo V, Guarnera A, Guarino F, Messina A, Mazzoni C, De Pinto V.
    FEBS Lett; 2010 Jul 02; 584(13):2837-44. PubMed ID: 20434446
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  • 3. VDAC1, having a shorter N-terminus than VDAC2 but showing the same migration in an SDS-polyacrylamide gel, is the predominant form expressed in mitochondria of various tissues.
    Yamamoto T, Yamada A, Watanabe M, Yoshimura Y, Yamazaki N, Yoshimura Y, Yamauchi T, Kataoka M, Nagata T, Terada H, Shinohara Y.
    J Proteome Res; 2006 Dec 02; 5(12):3336-44. PubMed ID: 17137335
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  • 4. Mitochondrial voltage-dependent anion channel gene family in Drosophila melanogaster: complex patterns of evolution, genomic organization, and developmental expression.
    Graham BH, Craigen WJ.
    Mol Genet Metab; 2005 Aug 02; 85(4):308-17. PubMed ID: 15886041
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  • 10. Effects of a mutation in the Drosophila porin gene encoding mitochondrial voltage-dependent anion channel protein on phototransduction.
    Lee S, Leung HT, Kim E, Jang J, Lee E, Baek K, Pak WL, Yoon J.
    Dev Neurobiol; 2007 Sep 15; 67(11):1533-45. PubMed ID: 17525991
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  • 13. Redox regulation of protein expression in Saccharomyces cerevisiae mitochondria: possible role of VDAC.
    Galganska H, Budzinska M, Wojtkowska M, Kmita H.
    Arch Biochem Biophys; 2008 Nov 01; 479(1):39-45. PubMed ID: 18768136
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  • 14. All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain.
    Cesar Mde C, Wilson JE.
    Arch Biochem Biophys; 2004 Feb 15; 422(2):191-6. PubMed ID: 14759607
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  • 15. Molecular and functional characterization of VDAC2 purified from mammal spermatozoa.
    Menzel VA, Cassará MC, Benz R, de Pinto V, Messina A, Cunsolo V, Saletti R, Hinsch KD, Hinsch E.
    Biosci Rep; 2009 Jul 22; 29(6):351-62. PubMed ID: 18976238
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  • 16. Protein-protein interaction networks as a new perspective to evaluate distinct functional roles of voltage-dependent anion channel isoforms.
    Caterino M, Ruoppolo M, Mandola A, Costanzo M, Orrù S, Imperlini E.
    Mol Biosyst; 2017 Nov 21; 13(12):2466-2476. PubMed ID: 29028058
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  • 17. Voltage-dependent anion-selective channels VDAC2 and VDAC3 are abundant proteins in bovine outer dense fibers, a cytoskeletal component of the sperm flagellum.
    Hinsch KD, De Pinto V, Aires VA, Schneider X, Messina A, Hinsch E.
    J Biol Chem; 2004 Apr 09; 279(15):15281-8. PubMed ID: 14739283
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