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Journal Abstract Search

202 related items for PubMed ID: 7632690

  • 1. 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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  • 2. Titration of protein transport activity by incremental changes in signal peptide hydrophobicity.
    Doud SK, Chou MM, Kendall DA.
    Biochemistry; 1993 Feb 09; 32(5):1251-6. PubMed ID: 8448135
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  • 6. 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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  • 7. Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments.
    Rizo J, Blanco FJ, Kobe B, Bruch MD, Gierasch LM.
    Biochemistry; 1993 May 11; 32(18):4881-94. PubMed ID: 8387821
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  • 8. Comparison of helix stability in wild-type and mutant LamB signal sequences.
    Bruch MD, Gierasch LM.
    J Biol Chem; 1990 Mar 05; 265(7):3851-8. PubMed ID: 2406265
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  • 9. Structures of wild-type and mutant signal sequences of Escherichia coli ribose binding protein.
    Yi GS, Choi BS, Kim H.
    Biophys J; 1994 May 05; 66(5):1604-11. PubMed ID: 8061209
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  • 10. Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide.
    Kendall DA, Bock SC, Kaiser ET.
    Nature; 1994 May 05; 321(6071):706-8. PubMed ID: 3520341
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  • 11. Structures of revertant signal sequences of Escherichia coli ribose binding protein.
    Chi SW, Yi GS, Suh JY, Choi BS, Kim H.
    Biophys J; 1995 Dec 05; 69(6):2703-9. PubMed ID: 8599676
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  • 12. 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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  • 13. 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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  • 14. Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region.
    Karamyshev AL, Karamysheva ZN, Kajava AV, Ksenzenko VN, Nesmeyanova MA.
    J Mol Biol; 1998 Apr 10; 277(4):859-70. PubMed ID: 9545377
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  • 15. Signal sequences containing multiple aromatic residues.
    Rusch SL, Kendall DA.
    J Mol Biol; 1992 Mar 05; 224(1):77-85. PubMed ID: 1548710
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  • 16. Signal peptide hydrophobicity is finely tailored for function.
    Rusch SL, Chen H, Izard JW, Kendall DA.
    J Cell Biochem; 1994 Jun 05; 55(2):209-17. PubMed ID: 8089196
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  • 17. Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides.
    Rusch SL, Mascolo CL, Kebir MO, Kendall DA.
    Arch Microbiol; 2002 Oct 05; 178(4):306-10. PubMed ID: 12209265
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  • 20. Correlation of secondary structure with biological activity for a leader peptide: circular dichroism-derived structure and in vitro biological activities of preproparathyroid hormone peptide and its analogs.
    Caulfield MP, Park K, Rosenblatt M, Fasman GD.
    Arch Biochem Biophys; 1991 Sep 05; 289(2):208-13. PubMed ID: 1898067
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