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Journal Abstract Search

131 related items for PubMed ID: 2663841

  • 1. Both a short hydrophobic domain and a carboxyl-terminal hydrophilic region are important for signal function in the Escherichia coli leader peptidase.
    Zhu HY, Dalbey RE.
    J Biol Chem; 1989 Jul 15; 264(20):11833-8. PubMed ID: 2663841
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  • 2. The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly.
    Dalbey RE, Kuhn A, Wickner W.
    J Biol Chem; 1987 Sep 25; 262(27):13241-5. PubMed ID: 3308874
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  • 3. Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.
    Laws JK, Dalbey RE.
    EMBO J; 1989 Jul 25; 8(7):2095-9. PubMed ID: 2676512
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  • 4. The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane.
    Dalbey RE, Wickner W.
    J Biol Chem; 1986 Oct 15; 261(29):13844-9. PubMed ID: 3531212
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  • 5. Characterization of the internal signal-anchor domain of Escherichia coli leader peptidase.
    Dalbey RE, Wickner W.
    J Biol Chem; 1988 Jan 05; 263(1):404-8. PubMed ID: 3275645
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  • 6. Leader peptidase.
    Dalbey RE.
    Mol Microbiol; 1991 Dec 05; 5(12):2855-60. PubMed ID: 1809829
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  • 7. Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly.
    Strom MS, Lory S.
    J Biol Chem; 1991 Jan 25; 266(3):1656-64. PubMed ID: 1671038
    [Abstract] [Full Text] [Related]

  • 8. The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence.
    von Heijne G, Wickner W, Dalbey RE.
    Proc Natl Acad Sci U S A; 1988 May 25; 85(10):3363-6. PubMed ID: 3285342
    [Abstract] [Full Text] [Related]

  • 9. Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly.
    Dalbey RE, Wickner W.
    Science; 1987 Feb 13; 235(4790):783-7. PubMed ID: 3544218
    [Abstract] [Full Text] [Related]

  • 10. Effect of signal peptide changes on the extracellular processing of streptokinase from Escherichia coli: requirement for secondary structure at the cleavage junction.
    Pratap J, Dikshit KL.
    Mol Gen Genet; 1998 May 13; 258(4):326-33. PubMed ID: 9648736
    [Abstract] [Full Text] [Related]

  • 11. The hydrophobic domains in the carboxyl-terminal signal for GPI modification and in the amino-terminal leader peptide have similar structural requirements.
    Yan W, Shen F, Dillon B, Ratnam M.
    J Mol Biol; 1998 Jan 09; 275(1):25-33. PubMed ID: 9451436
    [Abstract] [Full Text] [Related]

  • 12. Structural features in the NH2-terminal region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase.
    Nothwehr SF, Gordon JI.
    J Biol Chem; 1990 Oct 05; 265(28):17202-8. PubMed ID: 2120214
    [Abstract] [Full Text] [Related]

  • 13. Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis.
    van der Meer JR, Rollema HS, Siezen RJ, Beerthuyzen MM, Kuipers OP, de Vos WM.
    J Biol Chem; 1994 Feb 04; 269(5):3555-62. PubMed ID: 8106398
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  • 16. 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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  • 20. A comparative analysis of single- and multiple-residue substitutions in the alkaline phosphatase signal peptide.
    Kendall DA, Doud SK, Kaiser ET.
    Biopolymers; 1990 Jan 10; 29(1):139-47. PubMed ID: 2183883
    [Abstract] [Full Text] [Related]

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