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Journal Abstract Search

102 related items for PubMed ID: 4133311

  • 1. Isolation and characterization of an antibody to a highly purified preparation of the hemin-controlled translational repressor from rabbit reticulocytes.
    Gross M.
    Biochem Biophys Res Commun; 1974 Apr 08; 57(3):611-9. PubMed ID: 4133311
    [No Abstract] [Full Text] [Related]

  • 2. Inhibition of an initiation codon function by hemin deficiency and the hemin-controlled translational repressor in the reticulocyte cell-free system.
    Balkow K, Mizuno S, Rabinovitz M.
    Biochem Biophys Res Commun; 1973 Sep 05; 54(1):315-23. PubMed ID: 4795367
    [No Abstract] [Full Text] [Related]

  • 3. Control of globin synthesis by hemin: factors influencing formation of an inhibitor of globin chain initiation in reticulocyte lysates.
    Gross M, Rabinovitz M.
    Biochim Biophys Acta; 1972 Dec 06; 287(2):340-52. PubMed ID: 4680051
    [No Abstract] [Full Text] [Related]

  • 4. The high-temperature inactivation of rabbit reticulocyte lysates by a haemin-independent mechanism.
    Bonanou-Tzedaki SA, Smith KE, Sheeran BA, Arnstein HR.
    Eur J Biochem; 1978 Mar 15; 84(2):591-600. PubMed ID: 639804
    [No Abstract] [Full Text] [Related]

  • 5. Met-tRNAfMet binding to 40S ribosomal subunits: a site for the regulation of initiation of protein synthesis by hemin.
    Clemens MJ, Henshaw EC, Rahamimoff H, London IM.
    Proc Natl Acad Sci U S A; 1974 Aug 15; 71(8):2946-50. PubMed ID: 4528641
    [Abstract] [Full Text] [Related]

  • 6. Control of globin synthesis in cell-free preparations of reticulocytes by formation of a translational repressor that is inactivated by hemin.
    Gross M, Rabinovitz M.
    Proc Natl Acad Sci U S A; 1972 Jun 15; 69(6):1565-8. PubMed ID: 4504369
    [Abstract] [Full Text] [Related]

  • 7. Control of globin synthesis by hemin. Regulation by hemin of the formation and inactivation of a translational repressor of globin synthesis in rabbit reticulocyte lysates.
    Gross M.
    Biochim Biophys Acta; 1974 Apr 10; 340(4):484-97. PubMed ID: 4831913
    [No Abstract] [Full Text] [Related]

  • 8. Hemin control of globin synthesis: action of an inhibitor formed in the absence of hemin on the reticulocyte cell-free system and its reversal by a ribosomal factor.
    Mizuno S, Fisher JM, Rabinovitz M.
    Biochim Biophys Acta; 1972 Jul 31; 272(4):638-50. PubMed ID: 5050923
    [No Abstract] [Full Text] [Related]

  • 9. Translational repression in the control of globin chain initiation by hemin.
    Rabinovitz M.
    Ann N Y Acad Sci; 1974 Nov 29; 241(0):322-33. PubMed ID: 4530662
    [No Abstract] [Full Text] [Related]

  • 10. The effect of cyclic AMP and related compounds on the control of protein synthesis in reticulocyte lysates.
    Legon S, Brayley A, Hunt T, Jackson RJ.
    Biochem Biophys Res Commun; 1974 Feb 04; 56(3):745-52. PubMed ID: 4363751
    [No Abstract] [Full Text] [Related]

  • 11. Regulatory role of heme.
    Kaplan BH, Tricoche M, Vanderhoff G.
    Ann N Y Acad Sci; 1974 Nov 29; 241(0):334-46. PubMed ID: 4530663
    [No Abstract] [Full Text] [Related]

  • 12. Involvement of hemin, a stimulatory fraction from ribosomes and a protein synthesis inhibitor in the regulation of hemoglobin synthesis.
    Adamson SD, Yau PM, Herbert E, Zucker WV.
    J Mol Biol; 1972 Jan 28; 63(2):247-64. PubMed ID: 4634507
    [No Abstract] [Full Text] [Related]

  • 13. Partial purification of a translational repressor mediating hemin control of globin synthesis and implication of results on the site of inhibition.
    Gross M, Rabinovitz M.
    Biochem Biophys Res Commun; 1973 Feb 05; 50(3):832-8. PubMed ID: 4689080
    [No Abstract] [Full Text] [Related]

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  • 15. Translational control at the level of initiation of protein synthesis. The effect of 3-methylcholanthrene administration on the activity of rat liver IF-M2A, IF-M2B and IF-M3.
    Hopkinson J, Prichard PM, Bresnick E.
    Biochim Biophys Acta; 1974 Dec 20; 374(3):375-83. PubMed ID: 4433602
    [No Abstract] [Full Text] [Related]

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  • 19. Control of globin synthesis by hemin. An intermediate form of the translational repressor in rabbit reticulocyte lysates.
    Gross M.
    Biochim Biophys Acta; 1974 Oct 28; 366(3):319-32. PubMed ID: 4425656
    [No Abstract] [Full Text] [Related]

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