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 *

262 related articles for article (PubMed ID: 7536035)

  • 1. Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.
    Zapun A; Missiakas D; Raina S; Creighton TE
    Biochemistry; 1995 Apr; 34(15):5075-89. PubMed ID: 7536035
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.
    Zapun A; Cooper L; Creighton TE
    Biochemistry; 1994 Feb; 33(7):1907-14. PubMed ID: 8110795
    [TBL] [Abstract][Full Text] [Related]  

  • 3. The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.
    Zapun A; Bardwell JC; Creighton TE
    Biochemistry; 1993 May; 32(19):5083-92. PubMed ID: 8494885
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways.
    Segatori L; Paukstelis PJ; Gilbert HF; Georgiou G
    Proc Natl Acad Sci U S A; 2004 Jul; 101(27):10018-23. PubMed ID: 15220477
    [TBL] [Abstract][Full Text] [Related]  

  • 5. The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.
    Missiakas D; Georgopoulos C; Raina S
    EMBO J; 1994 Apr; 13(8):2013-20. PubMed ID: 8168498
    [TBL] [Abstract][Full Text] [Related]  

  • 6. DsbA and DsbC-catalyzed oxidative folding of proteins with complex disulfide bridge patterns in vitro and in vivo.
    Maskos K; Huber-Wunderlich M; Glockshuber R
    J Mol Biol; 2003 Jan; 325(3):495-513. PubMed ID: 12498799
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Contributions of substrate binding to the catalytic activity of DsbC.
    Darby NJ; Raina S; Creighton TE
    Biochemistry; 1998 Jan; 37(3):783-91. PubMed ID: 9454567
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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; 26(1):121-32. PubMed ID: 9383195
    [TBL] [Abstract][Full Text] [Related]  

  • 9. In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.
    Joly JC; Swartz JR
    Biochemistry; 1997 Aug; 36(33):10067-72. PubMed ID: 9254601
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds.
    Sone M; Akiyama Y; Ito K
    J Biol Chem; 1997 Apr; 272(16):10349-52. PubMed ID: 9099671
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Building bridges: disulphide bond formation in the cell.
    Bardwell JC
    Mol Microbiol; 1994 Oct; 14(2):199-205. PubMed ID: 7830566
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC.
    Hiniker A; Collet JF; Bardwell JC
    J Biol Chem; 2005 Oct; 280(40):33785-91. PubMed ID: 16087673
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Why is DsbA such an oxidizing disulfide catalyst?
    Grauschopf U; Winther JR; Korber P; Zander T; Dallinger P; Bardwell JC
    Cell; 1995 Dec; 83(6):947-55. PubMed ID: 8521518
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.
    Bessette PH; Qiu J; Bardwell JC; Swartz JR; Georgiou G
    J Bacteriol; 2001 Feb; 183(3):980-8. PubMed ID: 11208797
    [TBL] [Abstract][Full Text] [Related]  

  • 15. De novo design and evolution of artificial disulfide isomerase enzymes analogous to the bacterial DsbC.
    Arredondo S; Segatori L; Gilbert HF; Georgiou G
    J Biol Chem; 2008 Nov; 283(46):31469-76. PubMed ID: 18782764
    [TBL] [Abstract][Full Text] [Related]  

  • 16. An in vivo pathway for disulfide bond isomerization in Escherichia coli.
    Rietsch A; Belin D; Martin N; Beckwith J
    Proc Natl Acad Sci U S A; 1996 Nov; 93(23):13048-53. PubMed ID: 8917542
    [TBL] [Abstract][Full Text] [Related]  

  • 17. In vivo substrate specificity of periplasmic disulfide oxidoreductases.
    Hiniker A; Bardwell JC
    J Biol Chem; 2004 Mar; 279(13):12967-73. PubMed ID: 14726535
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
    McCarthy AA; Haebel PW; Törrönen A; Rybin V; Baker EN; Metcalf P
    Nat Struct Biol; 2000 Mar; 7(3):196-9. PubMed ID: 10700276
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
    Rietsch A; Bessette P; Georgiou G; Beckwith J
    J Bacteriol; 1997 Nov; 179(21):6602-8. PubMed ID: 9352906
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Enzymatic catalysis of disulfide formation.
    Noiva R
    Protein Expr Purif; 1994 Feb; 5(1):1-13. PubMed ID: 7909462
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 14.