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PUBMED FOR HANDHELDS

Journal Abstract Search


140 related items for PubMed ID: 2668291

  • 1. Signal peptide subsegments are not always functionally interchangeable. M13 procoat hydrophobic core fails to transport alkaline phosphatase in Escherichia coli.
    Laforet GA, Kaiser ET, Kendall DA.
    J Biol Chem; 1989 Aug 25; 264(24):14478-85. PubMed ID: 2668291
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  • 2. Escherichia coli signal peptides direct inefficient secretion of an outer membrane protein (OmpA) and periplasmic proteins (maltose-binding protein, ribose-binding protein, and alkaline phosphatase) in Bacillus subtilis.
    Collier DN.
    J Bacteriol; 1994 May 25; 176(10):3013-20. PubMed ID: 8188602
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  • 4. Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.
    Puziss JW, Strobel SM, Bassford PJ.
    J Bacteriol; 1992 Jan 25; 174(1):92-101. PubMed ID: 1729228
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  • 7. Transport of an export-defective protein by a highly hydrophobic signal peptide.
    Rusch SL, Kendall DA.
    J Biol Chem; 1994 Jan 14; 269(2):1243-8. PubMed ID: 8288586
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  • 9. Bacteriophage M13 procoat protein inserts into the plasma membrane as a loop structure.
    Kuhn A.
    Science; 1987 Dec 04; 238(4832):1413-5. PubMed ID: 3317833
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  • 10. Thermodynamics of the membrane insertion process of the M13 procoat protein, a lipid bilayer traversing protein containing a leader sequence.
    Soekarjo M, Eisenhawer M, Kuhn A, Vogel H.
    Biochemistry; 1996 Jan 30; 35(4):1232-41. PubMed ID: 8573578
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  • 12. Physical and conformational properties of synthetic idealized signal sequences parallel their biological function.
    Izard JW, Doughty MB, Kendall DA.
    Biochemistry; 1995 Aug 08; 34(31):9904-12. PubMed ID: 7632690
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  • 14. Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells.
    Fikes JD, Bassford PJ.
    J Bacteriol; 1987 Jun 08; 169(6):2352-9. PubMed ID: 3294787
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  • 16. Mutational alterations affecting the export competence of a truncated but fully functional maltose-binding protein signal peptide.
    Fikes JD, Bankaitis VA, Ryan JP, Bassford PJ.
    J Bacteriol; 1987 Jun 08; 169(6):2345-51. PubMed ID: 3294786
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  • 19. Yersinia spp. HMWP2, a cytosolic protein with a cryptic internal signal sequence which can promote alkaline phosphatase export.
    Guilvout I, Carniel E, Pugsley AP.
    J Bacteriol; 1995 Apr 08; 177(7):1780-7. PubMed ID: 7896701
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  • 20. Polymeric sequences reveal a functional interrelationship between hydrophobicity and length of signal peptides.
    Chou MM, Kendall DA.
    J Biol Chem; 1990 Feb 15; 265(5):2873-80. PubMed ID: 2154463
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