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 *

106 related articles for article (PubMed ID: 15618616)

  • 1. Role of the carbohydrate chain and two phosphate moieties in the heat-induced aggregation of hen ovalbumin.
    Tani F; Shirai N; Nakanishi Y; Yasumoto K; Kitabatake N
    Biosci Biotechnol Biochem; 2004 Dec; 68(12):2466-76. PubMed ID: 15618616
    [TBL] [Abstract][Full Text] [Related]  

  • 2. 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]  

  • 3. 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]  

  • 4. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
    Patra AK; Udgaonkar JB
    Biochemistry; 2007 Oct; 46(42):11727-43. PubMed ID: 17902706
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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]  

  • 6. The folding of ovalbumin. Renaturation in vitro versus biosynthesis in vitro.
    Klausner RD; Kempf C; Weinstein JN; Blumenthal R; Van Renswoude J
    Biochem J; 1983 Jun; 212(3):801-10. PubMed ID: 6882395
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Renaturation of lysozyme--temperature dependence of renaturation rate, renaturation yield, and aggregation: identification of hydrophobic folding intermediates.
    Fischer B; Sumner I; Goodenough P
    Arch Biochem Biophys; 1993 Oct; 306(1):183-7. PubMed ID: 8215401
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme.
    Matagne A; Jamin M; Chung EW; Robinson CV; Radford SE; Dobson CM
    J Mol Biol; 2000 Mar; 297(1):193-210. PubMed ID: 10704316
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Deglycosylation of ovalbumin prohibits formation of a heat-stable conformer.
    de Groot J; Kosters HA; de Jongh HH
    Biotechnol Bioeng; 2007 Jul; 97(4):735-41. PubMed ID: 17154314
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Refolding of urea denatured ovalbumin with three phase partitioning generates many conformational variants.
    Rather GM; Gupta MN
    Int J Biol Macromol; 2013 Sep; 60():301-8. PubMed ID: 23777710
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Conformational changes involved in the switch from ovalbumin to S-ovalbumin.
    Castellano AC; Barteri M; Bianconi A; Bruni F; Della Longa S; Paolinelli C
    Z Naturforsch C J Biosci; 1996; 51(5-6):379-85. PubMed ID: 8663899
    [TBL] [Abstract][Full Text] [Related]  

  • 12. 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]  

  • 13. Effect of protein charge on the generation of aggregation-prone conformers.
    Broersen K; Weijers M; de Groot J; Hamer RJ; de Jongh HH
    Biomacromolecules; 2007 May; 8(5):1648-56. PubMed ID: 17465525
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Analysis of molecular interactions in heat-induced aggregation of a non-inhibitory serpin ovalbumin using a molecular chaperone.
    Tani F; Shirai N; Nakanishi Y; Kitabatake N
    Biosci Biotechnol Biochem; 2003 May; 67(5):1030-8. PubMed ID: 12834280
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Linear polymerization caused by the defective folding of a non-inhibitory serpin ovalbumin.
    Shirai N; Tani F; Higasa T; Yasumoto K
    J Biochem; 1997 Apr; 121(4):787-97. PubMed ID: 9163532
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Dielectric study of heat-denatured ovalbumin in aqueous solution by time domain reflectometry method.
    Sun Y; Ishida T; Hayakawa S
    J Agric Food Chem; 2004 Apr; 52(8):2351-7. PubMed ID: 15080645
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Structural characteristics of hen egg ovalbumin expressed in yeast Pichia pastoris.
    Ito K; Matsudomi N
    Biosci Biotechnol Biochem; 2005 Apr; 69(4):755-61. PubMed ID: 15849414
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Influence of sodium chloride and glucose on the aggregation behavior of heat-denatured ovalbumin investigated with a multiangle laser light scattering technique.
    Choi SJ; Moon TW
    J Food Sci; 2008 Mar; 73(2):C41-9. PubMed ID: 18298715
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Appraisal of casein's inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis.
    Khodarahmi R; Beyrami M; Soori H
    Arch Biochem Biophys; 2008 Sep; 477(1):67-76. PubMed ID: 18485276
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Heat-induced denaturation and aggregation of ovalbumin at neutral pH described by irreversible first-order kinetics.
    Weijers M; Barneveld PA; Cohen Stuart MA; Visschers RW
    Protein Sci; 2003 Dec; 12(12):2693-703. PubMed ID: 14627731
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 6.