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.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

377 related items for PubMed ID: 7568240

  • 1. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA.
    Guilhot C, Jander G, Martin NL, Beckwith J.
    Proc Natl Acad Sci U S A; 1995 Oct 10; 92(21):9895-9. PubMed ID: 7568240
    [Abstract] [Full Text] [Related]

  • 2. Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.
    Kishigami S, Ito K.
    Genes Cells; 1996 Feb 10; 1(2):201-8. PubMed ID: 9140064
    [Abstract] [Full Text] [Related]

  • 3. DsbB catalyzes disulfide bond formation de novo.
    Regeimbal J, Bardwell JC.
    J Biol Chem; 2002 Sep 06; 277(36):32706-13. PubMed ID: 12072444
    [Abstract] [Full Text] [Related]

  • 4. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells.
    Kobayashi T, Kishigami S, Sone M, Inokuchi H, Mogi T, Ito K.
    Proc Natl Acad Sci U S A; 1997 Oct 28; 94(22):11857-62. PubMed ID: 9342327
    [Abstract] [Full Text] [Related]

  • 5.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 6. The DsbA-DsbB system affects the formation of disulfide bonds in periplasmic but not in intramembraneous protein domains.
    Whitley P, von Heijne G.
    FEBS Lett; 1993 Oct 11; 332(1-2):49-51. PubMed ID: 8405447
    [Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8. Redox states of DsbA in the periplasm of Escherichia coli.
    Kishigami S, Akiyama Y, Ito K.
    FEBS Lett; 1995 May 01; 364(1):55-8. PubMed ID: 7750543
    [Abstract] [Full Text] [Related]

  • 9. Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.
    Kadokura H, Beckwith J.
    EMBO J; 2002 May 15; 21(10):2354-63. PubMed ID: 12006488
    [Abstract] [Full Text] [Related]

  • 10. Mechanism of the electron transfer catalyst DsbB from Escherichia coli.
    Grauschopf U, Fritz A, Glockshuber R.
    EMBO J; 2003 Jul 15; 22(14):3503-13. PubMed ID: 12853466
    [Abstract] [Full Text] [Related]

  • 11. Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.
    Pan JL, Sliskovic I, Bardwell JC.
    J Mol Biol; 2008 Apr 11; 377(5):1433-42. PubMed ID: 18325532
    [Abstract] [Full Text] [Related]

  • 12. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.
    Kobayashi T, Ito K.
    EMBO J; 1999 Mar 01; 18(5):1192-8. PubMed ID: 10064586
    [Abstract] [Full Text] [Related]

  • 13. NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.
    Zhou Y, Cierpicki T, Jimenez RH, Lukasik SM, Ellena JF, Cafiso DS, Kadokura H, Beckwith J, Bushweller JH.
    Mol Cell; 2008 Sep 26; 31(6):896-908. PubMed ID: 18922471
    [Abstract] [Full Text] [Related]

  • 14. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.
    Kishigami S, Kanaya E, Kikuchi M, Ito K.
    J Biol Chem; 1995 Jul 21; 270(29):17072-4. PubMed ID: 7615498
    [Abstract] [Full Text] [Related]

  • 15. Identification of the Thioredoxin Partner of Vitamin K Epoxide Reductase in Mycobacterial Disulfide Bond Formation.
    Ke N, Landeta C, Wang X, Boyd D, Eser M, Beckwith J.
    J Bacteriol; 2018 Aug 15; 200(16):. PubMed ID: 29784887
    [Abstract] [Full Text] [Related]

  • 16. The dsbA-dsbB disulfide bond formation system of Burkholderia cepacia is involved in the production of protease and alkaline phosphatase, motility, metal resistance, and multi-drug resistance.
    Hayashi S, Abe M, Kimoto M, Furukawa S, Nakazawa T.
    Microbiol Immunol; 2000 Aug 15; 44(1):41-50. PubMed ID: 10711598
    [Abstract] [Full Text] [Related]

  • 17. A new Escherichia coli gene, dsbG, encodes a periplasmic protein involved in disulphide bond formation, required for recycling DsbA/DsbB and DsbC redox proteins.
    Andersen CL, Matthey-Dupraz A, Missiakas D, Raina S.
    Mol Microbiol; 1997 Oct 15; 26(1):121-32. PubMed ID: 9383195
    [Abstract] [Full Text] [Related]

  • 18. Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation.
    Jander G, Martin NL, Beckwith J.
    EMBO J; 1994 Nov 01; 13(21):5121-7. PubMed ID: 7957076
    [Abstract] [Full Text] [Related]

  • 19. Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli.
    Dailey FE, Berg HC.
    Proc Natl Acad Sci U S A; 1993 Feb 01; 90(3):1043-7. PubMed ID: 8503954
    [Abstract] [Full Text] [Related]

  • 20. Development of a sensor for disulfide bond formation in diverse bacteria.
    Dyotima, Abulaila S, Mendoza J, Landeta C.
    J Bacteriol; 2024 Apr 18; 206(4):e0043323. PubMed ID: 38493438
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 19.