BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

169 related articles for article (PubMed ID: 20630532)

  • 1. Changes in solvent exposure reveal the kinetics and equilibria of adsorbed protein unfolding in hydrophobic interaction chromatography.
    Deitcher RW; O'Connell JP; Fernandez EJ
    J Chromatogr A; 2010 Aug; 1217(35):5571-83. PubMed ID: 20630532
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Protein stability and structure in HIC: hydrogen exchange experiments and COREX calculations.
    Gospodarek AM; Smatlak ME; O'Connell JP; Fernandez EJ
    Langmuir; 2011 Jan; 27(1):286-95. PubMed ID: 21117672
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Protein instability during HIC: evidence of unfolding reversibility, and apparent adsorption strength of disulfide bond-reduced alpha-lactalbumin variants.
    Deitcher RW; Xiao Y; O'Connell JP; Fernandez EJ
    Biotechnol Bioeng; 2009 Apr; 102(5):1416-27. PubMed ID: 19152385
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Structures of multidomain proteins adsorbed on hydrophobic interaction chromatography surfaces.
    Gospodarek AM; Sun W; O'Connell JP; Fernandez EJ
    J Chromatogr A; 2014 Dec; 1371():204-19. PubMed ID: 25456599
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Hydrophobic interaction chromatography selectivity changes among three stable proteins: conformation does not play a major role.
    Jones TT; Fernandez EJ
    Biotechnol Bioeng; 2004 Aug; 87(3):388-99. PubMed ID: 15281113
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Hydrophobic interaction chromatography of proteins: Studies of unfolding upon adsorption by isothermal titration calorimetry.
    Rodler A; Beyer B; Ueberbacher R; Hahn R; Jungbauer A
    J Sep Sci; 2018 Aug; 41(15):3069-3080. PubMed ID: 29877629
    [TBL] [Abstract][Full Text] [Related]  

  • 7. The adsorption and unfolding kinetics determines the folding state of proteins at the air-water interface and thereby the equation of state.
    Wierenga PA; Egmond MR; Voragen AG; de Jongh HH
    J Colloid Interface Sci; 2006 Jul; 299(2):850-7. PubMed ID: 16600281
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Hydrophobic interaction chromatography of proteins V. Quantitative assessment of conformational changes.
    Ueberbacher R; Haimer E; Hahn R; Jungbauer A
    J Chromatogr A; 2008 Jul; 1198-1199():154-63. PubMed ID: 18541249
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Unfolding and refolding of bovine beta-lactoglobulin monitored by hydrogen exchange measurements.
    Ragona L; Fogolari F; Romagnoli S; Zetta L; Maubois JL; Molinari H
    J Mol Biol; 1999 Nov; 293(4):953-69. PubMed ID: 10543977
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Effect of mass overloading on binding and elution of unstable proteins in hydrophobic interaction chromatography.
    Muca R; Marek W; Żurawski M; Piątkowski W; Antos D
    J Chromatogr A; 2017 Apr; 1492():79-88. PubMed ID: 28284765
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Unfolding of a model protein on ion exchange and mixed mode chromatography surfaces.
    Gospodarek AM; Hiser DE; O'Connell JP; Fernandez EJ
    J Chromatogr A; 2014 Aug; 1355():238-52. PubMed ID: 24997510
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Conformation and orientation of a protein folding intermediate trapped by adsorption.
    Engel MF; Visser AJ; van Mierlo CP
    Proc Natl Acad Sci U S A; 2004 Aug; 101(31):11316-21. PubMed ID: 15263072
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Protein instability during HIC: describing the effects of mobile phase conditions on instability and chromatographic retention.
    Xiao Y; Freed AS; Jones TT; Makrodimitris K; O'Connell JP; Fernandez EJ
    Biotechnol Bioeng; 2006 Apr; 93(6):1177-89. PubMed ID: 16444741
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Characterization of secondary and tertiary conformational changes of beta-lactoglobulin adsorbed on silica nanoparticle surfaces.
    Wu X; Narsimhan G
    Langmuir; 2008 May; 24(9):4989-98. PubMed ID: 18366223
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Hydrophobic interaction chromatography of proteins. III. Unfolding of proteins upon adsorption.
    Jungbauer A; Machold C; Hahn R
    J Chromatogr A; 2005 Jun; 1079(1-2):221-8. PubMed ID: 16038308
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Limited conformational change of beta-lactoglobulin when adsorbed at the air-water interface.
    Meinders MB; De Jongh HH
    Biopolymers; 2002; 67(4-5):319-22. PubMed ID: 12012457
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Charge state distribution and hydrogen/deuterium exchange of alpha-lactalbumin and beta-lactoglobulin preparations by electrospray ionization mass spectrometry.
    Alomirah H; Alli I; Konishi Y
    J Agric Food Chem; 2003 Mar; 51(7):2049-57. PubMed ID: 12643672
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Hydrophobic interaction chromatography of proteins: thermodynamic analysis of conformational changes.
    Ueberbacher R; Rodler A; Hahn R; Jungbauer A
    J Chromatogr A; 2010 Jan; 1217(2):184-90. PubMed ID: 19501365
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Effects of water activity and aqueous solvent ordering on thermal stability of lysozyme, alpha-chymotrypsinogen A, and alcohol dehydrogenase.
    Matsue S; Fujii T; Miyawaki O
    Int J Biol Macromol; 2001 Jun; 28(5):343-9. PubMed ID: 11325420
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Intrinsic fluorescence studies of the kinetic mechanism of unfolding of alpha-lactalbumin on weakly hydrophobic chromatographic surfaces.
    Oroszlan P; Blanco R; Lu XM; Yarmush D; Karger BL
    J Chromatogr; 1990 Feb; 500():481-502. PubMed ID: 2329148
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.