These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

182 related articles for article (PubMed ID: 3511052)

  • 1. Effect of amino acid substitutions at the signal peptide cleavage site of the Escherichia coli major outer membrane lipoprotein.
    Pollitt S; Inouye S; Inouye M
    J Biol Chem; 1986 Feb; 261(4):1835-7. PubMed ID: 3511052
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Post-translational modification and processing of outer membrane prolipoproteins in Escherichia coli.
    Mizushima S
    Mol Cell Biochem; 1984; 60(1):5-15. PubMed ID: 6369111
    [TBL] [Abstract][Full Text] [Related]  

  • 3. 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; 258(4):326-33. PubMed ID: 9648736
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Prolipoprotein signal peptidase of Escherichia coli requires a cysteine residue at the cleavage site.
    Inouye S; Franceschini T; Sato M; Itakura K; Inouye M
    EMBO J; 1983; 2(1):87-91. PubMed ID: 11894915
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Temperature-sensitive processing of outer membrane lipoprotein in an Escherichia coli mutant.
    Yamagata H; Ippolito C; Inukai M; Inouye M
    J Bacteriol; 1982 Dec; 152(3):1163-8. PubMed ID: 6754699
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Residues flanking the COOH-terminal C-region of a model eukaryotic signal peptide influence the site of its cleavage by signal peptidase and the extent of coupling of its co-translational translocation and proteolytic processing in vitro.
    Nothwehr SF; Hoeltzli SD; Allen KL; Lively MO; Gordon JI
    J Biol Chem; 1990 Dec; 265(35):21797-803. PubMed ID: 2123875
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Requirement for signal peptide cleavage of Escherichia coli prolipoprotein.
    Inouye S; Hsu CP; Itakura K; Inouye M
    Science; 1983 Jul; 221(4605):59-61. PubMed ID: 6344218
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo.
    Barkocy-Gallagher GA; Bassford PJ
    J Biol Chem; 1992 Jan; 267(2):1231-8. PubMed ID: 1730647
    [TBL] [Abstract][Full Text] [Related]  

  • 9. An alternate pathway for the processing of the prolipoprotein signal peptide in Escherichia coli.
    Ghrayeb J; Lunn CA; Inouye S; Inouye M
    J Biol Chem; 1985 Sep; 260(20):10961-5. PubMed ID: 2993296
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Maturation of Escherichia coli maltose-binding protein by signal peptidase I in vivo. Sequence requirements for efficient processing and demonstration of an alternate cleavage site.
    Fikes JD; Barkocy-Gallagher GA; Klapper DG; Bassford PJ
    J Biol Chem; 1990 Feb; 265(6):3417-23. PubMed ID: 2406254
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Temperature-sensitive prolipoprotein signal peptidase in an Escherichia coli mutant: use of the mutant for an efficient and convenient assay system.
    Yamagata H
    J Biochem; 1983 Jun; 93(6):1509-15. PubMed ID: 6350278
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Effects of mutations at glycine residues in the hydrophobic region of the Escherichia coli prolipoprotein signal peptide on the secretion across the membrane.
    Inouye S; Vlasuk GP; Hsiung H; Inouye M
    J Biol Chem; 1984 Mar; 259(6):3729-33. PubMed ID: 6368550
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Kinetics and sequence specificity of processing of prepilin by PilD, the type IV leader peptidase of Pseudomonas aeruginosa.
    Strom MS; Lory S
    J Bacteriol; 1992 Nov; 174(22):7345-51. PubMed ID: 1429457
    [TBL] [Abstract][Full Text] [Related]  

  • 14. A lipoprotein signal peptide plus a cysteine residue at the amino-terminal end of the periplasmic protein beta-lactamase is sufficient for its lipid modification, processing and membrane localization in Escherichia coli.
    Oudega B; Clark D; Stegehuis F; Majoor MJ; Luirink J
    FEMS Microbiol Lett; 1993 Apr; 108(3):353-9. PubMed ID: 8514122
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Modification of bacterial lipoproteins.
    Sankaran K; Gupta SD; Wu HC
    Methods Enzymol; 1995; 250():683-97. PubMed ID: 7651187
    [No Abstract]   [Full Text] [Related]  

  • 16. Prolipoprotein modification and processing in Escherichia coli. A unique secondary structure in prolipoprotein signal sequence for the recognition by glyceryl transferase.
    Giam CZ; Chai T; Hayashi S; Wu HC
    Eur J Biochem; 1984 Jun; 141(2):331-7. PubMed ID: 6428886
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Apolipoprotein, an intermediate in the processing of the major lipoprotein of the Escherichia coli outer membrane.
    Inukai M; Ghrayeb J; Nakamura K; Inouye M
    J Biol Chem; 1984 Jan; 259(2):757-60. PubMed ID: 6363408
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Structural requirement at the cleavage site for efficient processing of the lipoprotein secretory precursor of Escherichia coli.
    Inouye S; Duffaud G; Inouye M
    J Biol Chem; 1986 Aug; 261(24):10970-5. PubMed ID: 3525558
    [TBL] [Abstract][Full Text] [Related]  

  • 19. The major outer membrane lipoprotein and new lipoproteins share a common signal peptidase that exists in the cytoplasmic membrane of Escherichia coli.
    Yamada H; Yamagata H; Mizushima S
    FEBS Lett; 1984 Jan; 166(1):179-82. PubMed ID: 6363127
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Signal peptide cleavage regions. Functional limits on length and topological implications.
    Jain RG; Rusch SL; Kendall DA
    J Biol Chem; 1994 Jun; 269(23):16305-10. PubMed ID: 8206936
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 10.