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Journal Abstract Search

89 related items for PubMed ID: 2659076

  • 1. Tubulin dimer dissociation and proteolytic accessibility.
    Sackett DL, Zimmerman DA, Wolff J.
    Biochemistry; 1989 Mar 21; 28(6):2662-7. PubMed ID: 2659076
    [Abstract] [Full Text] [Related]

  • 2. Subtilisin cleavage of tubulin heterodimers and polymers.
    Lobert S, Correia JJ.
    Arch Biochem Biophys; 1992 Jul 21; 296(1):152-60. PubMed ID: 1605626
    [Abstract] [Full Text] [Related]

  • 3. Proteolysis of tubulin and the substructure of the tubulin dimer.
    Sackett DL, Wolff J.
    J Biol Chem; 1986 Jul 05; 261(19):9070-6. PubMed ID: 3522582
    [Abstract] [Full Text] [Related]

  • 4. Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction.
    Serrano L, Avila J, Maccioni RB.
    Biochemistry; 1984 Sep 25; 23(20):4675-81. PubMed ID: 6388633
    [Abstract] [Full Text] [Related]

  • 5. Calcium binding to tubulin.
    Fong KC, Babitch JA, Anthony FA.
    Biochim Biophys Acta; 1988 Jan 04; 952(1):13-9. PubMed ID: 3202916
    [Abstract] [Full Text] [Related]

  • 6. Involvement of the carboxyl-terminal domain of tubulin in the regulation of its assembly.
    Serrano L, de la Torre J, Maccioni RB, Avila J.
    Proc Natl Acad Sci U S A; 1984 Oct 04; 81(19):5989-93. PubMed ID: 6385005
    [Abstract] [Full Text] [Related]

  • 7. Effect of specific proteolytic cleavages on tubulin polymer formation.
    Serrano L, Wandosell F, de la Torre J, Avila J.
    Biochem J; 1988 Jun 15; 252(3):683-91. PubMed ID: 3048248
    [Abstract] [Full Text] [Related]

  • 8. Polymorphic assembly of subtilisin-cleaved tubulin.
    White EA, Burton PR, Himes RH.
    Cell Motil Cytoskeleton; 1987 Jun 15; 7(1):31-8. PubMed ID: 3545504
    [Abstract] [Full Text] [Related]

  • 9. The carboxy terminus of the alpha subunit of tubulin regulates its interaction with colchicine.
    Mukhopadhyay K, Parrack PK, Bhattacharyya B.
    Biochemistry; 1990 Jul 24; 29(29):6845-50. PubMed ID: 2204421
    [Abstract] [Full Text] [Related]

  • 10. Regulatory aspects of the colchicine interactions with tubulin.
    Avila J, Serrano L, Maccioni RB.
    Mol Cell Biochem; 1987 Jan 24; 73(1):29-36. PubMed ID: 3543651
    [Abstract] [Full Text] [Related]

  • 11. Dissociation of the tubulin dimer is extremely slow, thermodynamically very unfavorable, and reversible in the absence of an energy source.
    Caplow M, Fee L.
    Mol Biol Cell; 2002 Jun 24; 13(6):2120-31. PubMed ID: 12058074
    [Abstract] [Full Text] [Related]

  • 12. Tubulin, hybrid dimers, and tubulin S. Stepwise charge reduction and polymerization.
    Bhattacharyya B, Sackett DL, Wolff J.
    J Biol Chem; 1985 Aug 25; 260(18):10208-16. PubMed ID: 3894367
    [Abstract] [Full Text] [Related]

  • 13.
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  • 14. Limited proteolysis of pig heart citrate synthase by subtilisin, chymotrypsin, and trypsin.
    Bloxham DP, Ericsson LH, Titani K, Walsh KA, Neurath H.
    Biochemistry; 1980 Aug 19; 19(17):3979-85. PubMed ID: 6773558
    [Abstract] [Full Text] [Related]

  • 15. Thermodynamics of reversible monomer-dimer association of tubulin.
    Sackett DL, Lippoldt RE.
    Biochemistry; 1991 Apr 09; 30(14):3511-7. PubMed ID: 2012810
    [Abstract] [Full Text] [Related]

  • 16. Tubulin subunit carboxyl termini determine polymerization efficiency.
    Sackett DL, Bhattacharyya B, Wolff J.
    J Biol Chem; 1985 Jan 10; 260(1):43-5. PubMed ID: 3965457
    [Abstract] [Full Text] [Related]

  • 17. Tubulin dimer dissociation detected by fluorescence anisotropy.
    Mejillano MR, Himes RH.
    Biochemistry; 1989 Jul 25; 28(15):6518-24. PubMed ID: 2506927
    [Abstract] [Full Text] [Related]

  • 18. The interaction between subunits in the tubulin dimer.
    Serrano L, Avila J.
    Biochem J; 1985 Sep 01; 230(2):551-6. PubMed ID: 3902010
    [Abstract] [Full Text] [Related]

  • 19.
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  • 20. The C terminus of beta-tubulin regulates vinblastine-induced tubulin polymerization.
    Rai SS, Wolff J.
    Proc Natl Acad Sci U S A; 1998 Apr 14; 95(8):4253-7. PubMed ID: 9539723
    [Abstract] [Full Text] [Related]

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