BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

145 related articles for article (PubMed ID: 1588813)

  • 1. The autocatalytic processing of the subtilisin Carlsberg pro-region is independent of the primary structure of the cleavage site.
    Egnell P; Flock JI
    Mol Microbiol; 1992 May; 6(9):1115-9. PubMed ID: 1588813
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Functional analysis of the intramolecular chaperone. Mutational hot spots in the subtilisin pro-peptide and a second-site suppressor mutation within the subtilisin molecule.
    Kobayashi T; Inouye M
    J Mol Biol; 1992 Aug; 226(4):931-3. PubMed ID: 1355566
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process.
    Zhu XL; Ohta Y; Jordan F; Inouye M
    Nature; 1989 Jun; 339(6224):483-4. PubMed ID: 2657436
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Preprosubtilisin Carlsberg processing and secretion is blocked after deletion of amino acids 97-101 in the mature part of the enzyme.
    Schülein R; Kreft J; Gonski S; Goebel W
    Mol Gen Genet; 1991 May; 227(1):137-43. PubMed ID: 1904534
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Determination of the signal peptidase cleavage site in the preprosubtilisin of Bacillus subtilis.
    Wong SL; Doi RH
    J Biol Chem; 1986 Aug; 261(22):10176-81. PubMed ID: 3090033
    [TBL] [Abstract][Full Text] [Related]  

  • 6. The subtilisin Carlsberg pro-region is a membrane anchorage for two fusion proteins produced in Bacillus subtilis.
    Egnell P; Flock JI
    Gene; 1991 Jan; 97(1):49-54. PubMed ID: 1899845
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.
    Ikemura H; Takagi H; Inouye M
    J Biol Chem; 1987 Jun; 262(16):7859-64. PubMed ID: 3108260
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Pro-subtilisin E: purification and characterization of its autoprocessing to active subtilisin E in vitro.
    Ohta Y; Inouye M
    Mol Microbiol; 1990 Feb; 4(2):295-304. PubMed ID: 2110997
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Secretion of active subtilisin YaB by a simultaneous expression of separate pre-pro and pre-mature polypeptides in Bacillus subtilis.
    Chang YC; Kadokura H; Yoda K; Yamasaki M
    Biochem Biophys Res Commun; 1996 Feb; 219(2):463-8. PubMed ID: 8605010
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Folding of subtilisin BPN': role of the pro-sequence.
    Eder J; Rheinnecker M; Fersht AR
    J Mol Biol; 1993 Sep; 233(2):293-304. PubMed ID: 8377204
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Folding pathway mediated by an intramolecular chaperone: dissecting conformational changes coincident with autoprocessing and the role of Ca(2+) in subtilisin maturation.
    Yabuta Y; Subbian E; Takagi H; Shinde U; Inouye M
    J Biochem; 2002 Jan; 131(1):31-7. PubMed ID: 11754732
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis.
    Jang JS; Kang DO; Chun MJ; Byun SM
    Biochem Biophys Res Commun; 1992 Apr; 184(1):277-82. PubMed ID: 1567435
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Kinetic studies of the inhibitory effects of propeptides subtilisin BPN' and Carlsberg to bacterial serine proteases.
    Huang HW; Chen WC; Wu CY; Yu HC; Lin WY; Chen ST; Wang KT
    Protein Eng; 1997 Oct; 10(10):1227-33. PubMed ID: 9488148
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg.
    Eschenburg S; Genov N; Peters K; Fittkau S; Stoeva S; Wilson KS; Betzel C
    Eur J Biochem; 1998 Oct; 257(2):309-18. PubMed ID: 9826175
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.
    Strausberg S; Alexander P; Wang L; Schwarz F; Bryan P
    Biochemistry; 1993 Aug; 32(32):8112-9. PubMed ID: 8347611
    [TBL] [Abstract][Full Text] [Related]  

  • 16. HreP, an in vivo-expressed protease of Yersinia enterocolitica, is a new member of the family of subtilisin/kexin-like proteases.
    Heusipp G; Young GM; Miller VL
    J Bacteriol; 2001 Jun; 183(12):3556-63. PubMed ID: 11371518
    [TBL] [Abstract][Full Text] [Related]  

  • 17. A new approach for alteration of protease functions: pro-sequence engineering.
    Takagi H; Takahashi M
    Appl Microbiol Biotechnol; 2003 Nov; 63(1):1-9. PubMed ID: 12879301
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Intramolecular chaperone: the role of the pro-peptide in protein folding.
    Inouye M
    Enzyme; 1991; 45(5-6):314-21. PubMed ID: 1688202
    [TBL] [Abstract][Full Text] [Related]  

  • 19. In vitro processing of pro-subtilisin produced in Escherichia coli.
    Ikemura H; Inouye M
    J Biol Chem; 1988 Sep; 263(26):12959-63. PubMed ID: 3047114
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Improved autoprocessing efficiency of mutant subtilisins E with altered specificity by engineering of the pro-region.
    Takahashi M; Hasuura Y; Nakamori S; Takagi H
    J Biochem; 2001 Jul; 130(1):99-106. PubMed ID: 11432785
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 8.