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139 related items for PubMed ID: 3597376

  • 1. Cold-stable microtubules from Antarctic fishes contain unique alpha tubulins.
    Detrich HW, Prasad V, Ludueña RF.
    J Biol Chem; 1987 Jun 15; 262(17):8360-6. PubMed ID: 3597376
    [Abstract] [Full Text] [Related]

  • 2. Heterogeneity and structure of brain tubulins from cold-adapted Antarctic fishes. Comparison to brain tubulins from a temperate fish and a mammal.
    Detrich HW, Overton SA.
    J Biol Chem; 1986 Aug 15; 261(23):10922-30. PubMed ID: 3733739
    [Abstract] [Full Text] [Related]

  • 3. Antarctic fish tubulins: heterogeneity, structure, amino acid compositions and charge.
    Detrich HW, Overton SA.
    Comp Biochem Physiol B; 1988 Aug 15; 90(3):593-600. PubMed ID: 3180738
    [Abstract] [Full Text] [Related]

  • 4. Microtubule assembly in cold-adapted organisms: functional properties and structural adaptations of tubulins from antarctic fishes.
    Detrich HW.
    Comp Biochem Physiol A Physiol; 1997 Nov 15; 118(3):501-13. PubMed ID: 9406432
    [Abstract] [Full Text] [Related]

  • 5. Cold adaptation of microtubule assembly and dynamics. Structural interpretation of primary sequence changes present in the alpha- and beta-tubulins of Antarctic fishes.
    Detrich HW, Parker SK, Williams RC, Nogales E, Downing KH.
    J Biol Chem; 2000 Nov 24; 275(47):37038-47. PubMed ID: 10956651
    [Abstract] [Full Text] [Related]

  • 6. Brain and egg tubulins from antarctic fishes are functionally and structurally distinct.
    Detrich HW, Fitzgerald TJ, Dinsmore JH, Marchese-Ragona SP.
    J Biol Chem; 1992 Sep 15; 267(26):18766-75. PubMed ID: 1527007
    [Abstract] [Full Text] [Related]

  • 7. Polymerization of Antarctic fish tubulins at low temperatures: energetic aspects.
    Detrich HW, Johnson KA, Marchese-Ragona SP.
    Biochemistry; 1989 Dec 26; 28(26):10085-93. PubMed ID: 2620064
    [Abstract] [Full Text] [Related]

  • 8. Posttranslational modification of brain tubulins from the Antarctic fish Notothenia coriiceps: reduced C-terminal glutamylation correlates with efficient microtubule assembly at low temperature.
    Redeker V, Frankfurter A, Parker SK, Rossier J, Detrich HW.
    Biochemistry; 2004 Sep 28; 43(38):12265-74. PubMed ID: 15379565
    [Abstract] [Full Text] [Related]

  • 9. Colchicine-binding sites of brain tubulins from an antarctic fish and from a mammal are functionally similar, but not identical: implications for microtubule assembly at low temperature.
    Skoufias DA, Wilson L, Detrich HW.
    Cell Motil Cytoskeleton; 1992 Sep 28; 21(4):272-80. PubMed ID: 1628324
    [Abstract] [Full Text] [Related]

  • 10. Polymerization of Antarctic fish tubulins at low temperatures: role of carboxy-terminal domains.
    Singer WD, Parker SK, Himes RH, Detrich HW.
    Biochemistry; 1994 Dec 27; 33(51):15389-96. PubMed ID: 7803402
    [Abstract] [Full Text] [Related]

  • 11. Microtubule-associated proteins from Antarctic fishes.
    Detrich HW, Neighbors BW, Sloboda RD, Williams RC.
    Cell Motil Cytoskeleton; 1990 Dec 27; 17(3):174-86. PubMed ID: 1980093
    [Abstract] [Full Text] [Related]

  • 12. Dynamic instability of microtubules from cold-living fishes.
    Billger M, Wallin M, Williams RC, Detrich HW.
    Cell Motil Cytoskeleton; 1994 Dec 27; 28(4):327-32. PubMed ID: 7954859
    [Abstract] [Full Text] [Related]

  • 13. Divergent neural beta tubulin from the Antarctic fish Notothenia coriiceps neglecta: potential sequence contributions to cold adaptation of microtubule assembly.
    Detrich HW, Parker SK.
    Cell Motil Cytoskeleton; 1993 Dec 27; 24(3):156-66. PubMed ID: 8467523
    [Abstract] [Full Text] [Related]

  • 14. Identification of betaIII- and betaIV-tubulin isotypes in cold-adapted microtubules from Atlantic cod (Gadus morhua): antibody mapping and cDNA sequencing.
    Modig C, Olsson PE, Barasoain I, de Ines C, Andreu JM, Roach MC, Ludueña RF, Wallin M.
    Cell Motil Cytoskeleton; 1999 Dec 27; 42(4):315-30. PubMed ID: 10223637
    [Abstract] [Full Text] [Related]

  • 15. Evolution, organization, and expression of alpha-tubulin genes in the antarctic fish Notothenia coriiceps. Adaptive expansion of a gene family by recent gene duplication, inversion, and divergence.
    Parker SK, Detrich HW.
    J Biol Chem; 1998 Dec 18; 273(51):34358-69. PubMed ID: 9852102
    [Abstract] [Full Text] [Related]

  • 16. The amino acid sequence of the alpha- and beta-chains of the two hemoglobins of the Antarctic fish Notothenia coriiceps neglecta.
    D'Avino R, Caruso C, Schininà ME, Rutigliano B, Romano M, Camardella L, Bossa F, Barra D, di Prisco G.
    FEBS Lett; 1989 Jun 19; 250(1):53-6. PubMed ID: 2737301
    [Abstract] [Full Text] [Related]

  • 17. Formation of microtubules at low temperature by tubulin from antarctic fish.
    Williams RC, Correia JJ, DeVries AL.
    Biochemistry; 1985 May 21; 24(11):2790-8. PubMed ID: 4027227
    [Abstract] [Full Text] [Related]

  • 18. Hemoglobin from the antarctic fish Notothenia coriiceps neglecta. Amino acid sequence of the beta chain.
    D'Avino R, Caruso C, Schinina ME, Rutigliano B, Romano M, Camardella L, Bossa F, Barra D, di Prisco G.
    Comp Biochem Physiol B; 1990 May 21; 96(2):367-73. PubMed ID: 2361365
    [Abstract] [Full Text] [Related]

  • 19. Cold-adapted microtubules: characterization of tubulin posttranslational modifications in the Antarctic ciliate Euplotes focardii.
    Pucciarelli S, Ballarini P, Miceli C.
    Cell Motil Cytoskeleton; 1997 May 21; 38(4):329-40. PubMed ID: 9415375
    [Abstract] [Full Text] [Related]

  • 20. Partial purification and characterization of microtubular protein from Trypanosoma brucei.
    Stieger J, Wyler T, Seebeck T.
    J Biol Chem; 1984 Apr 10; 259(7):4596-602. PubMed ID: 6707021
    [Abstract] [Full Text] [Related]

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