BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

120 related articles for article (PubMed ID: 12711610)

  • 1. Refolding mechanism of ovalbumin: investigation by using a starting urea-denatured disulfide isomer with mispaired CYS367-CYS382.
    Onda M; Hirose M
    J Biol Chem; 2003 Jun; 278(26):23600-9. PubMed ID: 12711610
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Refolding of urea-denatured ovalbumin that comprises non-native disulfide isomers.
    Onda M; Tatsumi E; Takahashi N; Hirose M
    J Biochem; 1997 Jul; 122(1):83-9. PubMed ID: 9276674
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Refolding process of ovalbumin from urea-denatured state. Evidence for the involvement of nonproductive side chain interactions in an early intermediate.
    Onda M; Tatsumi E; Takahashi N; Hirose M
    J Biol Chem; 1997 Feb; 272(7):3973-9. PubMed ID: 9020102
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Conformational state of ovalbumin at acidic pH as evaluated by a novel approach utilizing intrachain sulfhydryl-mixed disulfide exchange reactions.
    Tatsumi E; Yoshimatsu D; Hirose M
    Biochemistry; 1998 Sep; 37(35):12351-9. PubMed ID: 9724549
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Highly ordered molten globule-like state of ovalbumin at acidic pH: native-like fragmentation by protease and selective modification of Cys367 with dithiodipyridine.
    Tatsumi E; Hirose M
    J Biochem; 1997 Aug; 122(2):300-8. PubMed ID: 9378706
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Temperature control for kinetic refolding of heat-denatured ovalbumin.
    Tani F; Shirai N; Onishi T; Venelle F; Yasumoto K; Doi E
    Protein Sci; 1997 Jul; 6(7):1491-502. PubMed ID: 9232650
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Denatured state of ovalbumin in high concentrations of urea as evaluated by disulfide rearrangement analysis.
    Tatsumi E; Takahashi N; Hirose M
    J Biol Chem; 1994 Nov; 269(45):28062-7. PubMed ID: 7961742
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Participation of cysteine 30 residue in the folding process of ovalbumin evaluated in a refolding experiment using cysteine mutants.
    Ishimaru T; Ito K; Tanaka M; Matsudomi N
    Biochem Biophys Res Commun; 2018 Jan; 495(1):1061-1066. PubMed ID: 29175210
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Sequential comparison of peptides containing half-cystine residues from ovalbumins of six avian species.
    Sun Y; Hayakawa S
    Biosci Biotechnol Biochem; 2001 Dec; 65(12):2589-96. PubMed ID: 11826952
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link.
    Takahashi N; Hirose M
    J Biol Chem; 1992 Jun; 267(16):11565-72. PubMed ID: 1597484
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Thermostability of refolded ovalbumin and S-ovalbumin.
    Takahashi N; Onda M; Hayashi K; Yamasaki M; Mita T; Hirose M
    Biosci Biotechnol Biochem; 2005 May; 69(5):922-31. PubMed ID: 15914911
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Size-exclusion high performance liquid chromatography of native trypsinogen, the denatured protein, and partially refolded molecules. Further evidence that non-native disulfide bonds are dominant in refolding the completely reduced protein.
    al-Obeidi AM; Light A
    J Biol Chem; 1988 Jun; 263(18):8642-5. PubMed ID: 3379038
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin.
    Cavagnero S; Dyson HJ; Wright PE
    J Mol Biol; 1999 Jan; 285(1):269-82. PubMed ID: 9878405
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Role of an intrachain disulfide bond in the conformation and stability of ovalbumin.
    Takahashi N; Koseki T; Doi E; Hirose M
    J Biochem; 1991 Jun; 109(6):846-51. PubMed ID: 1939004
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Refolding of denatured and denatured/reduced lysozyme at high concentrations.
    Raman B; Ramakrishna T; Rao CM
    J Biol Chem; 1996 Jul; 271(29):17067-72. PubMed ID: 8663382
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Fluorescence energy transfer indicates similar transient and equilibrium intermediates in staphylococcal nuclease folding.
    Nishimura C; Riley R; Eastman P; Fink AL
    J Mol Biol; 2000 Jun; 299(4):1133-46. PubMed ID: 10843864
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy.
    Reinstädler D; Fabian H; Backmann J; Naumann D
    Biochemistry; 1996 Dec; 35(49):15822-30. PubMed ID: 8961946
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Conformational state of disulfide-reduced ovalbumin at acidic pH.
    Tatsumi E; Yoshimatsu D; Hirose M
    Biosci Biotechnol Biochem; 1999 Jul; 63(7):1285-90. PubMed ID: 10478455
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Structural properties of recombinant ovalbumin and its transformation into a thermostabilized form by alkaline treatment.
    Arii Y; Takahashi N; Tatsumi E; Hirose M
    Biosci Biotechnol Biochem; 1999 Aug; 63(8):1392-9. PubMed ID: 10501000
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Cleaved serpin refolds into the relaxed state via a stressed conformer.
    Onda M; Nakatani K; Takehara S; Nishiyama M; Takahashi N; Hirose M
    J Biol Chem; 2008 Jun; 283(25):17568-78. PubMed ID: 18390904
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.