BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

175 related articles for article (PubMed ID: 10393549)

  • 1. Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering.
    Wörn A; Plückthun A
    Biochemistry; 1999 Jul; 38(27):8739-50. PubMed ID: 10393549
    [TBL] [Abstract][Full Text] [Related]  

  • 2. Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability.
    Wörn A; Plückthun A
    Biochemistry; 1998 Sep; 37(38):13120-7. PubMed ID: 9748318
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Contributions of a highly conserved VH/VL hydrogen bonding interaction to scFv folding stability and refolding efficiency.
    Tan PH; Sandmaier BM; Stayton PS
    Biophys J; 1998 Sep; 75(3):1473-82. PubMed ID: 9726949
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability.
    Röthlisberger D; Honegger A; Plückthun A
    J Mol Biol; 2005 Apr; 347(4):773-89. PubMed ID: 15769469
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Removal of the conserved disulfide bridges from the scFv fragment of an antibody: effects on folding kinetics and aggregation.
    Ramm K; Gehrig P; Plückthun A
    J Mol Biol; 1999 Jul; 290(2):535-46. PubMed ID: 10390351
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Selection for improved protein stability by phage display.
    Jung S; Honegger A; Plückthun A
    J Mol Biol; 1999 Nov; 294(1):163-80. PubMed ID: 10556036
    [TBL] [Abstract][Full Text] [Related]  

  • 7. A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding.
    Proba K; Honegger A; Plückthun A
    J Mol Biol; 1997 Jan; 265(2):161-72. PubMed ID: 9020980
    [TBL] [Abstract][Full Text] [Related]  

  • 8. Antibody scFv fragments without disulfide bonds made by molecular evolution.
    Proba K; Wörn A; Honegger A; Plückthun A
    J Mol Biol; 1998 Jan; 275(2):245-53. PubMed ID: 9466907
    [TBL] [Abstract][Full Text] [Related]  

  • 9. The influence of the framework core residues on the biophysical properties of immunoglobulin heavy chain variable domains.
    Honegger A; Malebranche AD; Röthlisberger D; Plückthun A
    Protein Eng Des Sel; 2009 Mar; 22(3):121-34. PubMed ID: 19136675
    [TBL] [Abstract][Full Text] [Related]  

  • 10. Engineering antibodies for stability and efficient folding.
    Honegger A
    Handb Exp Pharmacol; 2008; (181):47-68. PubMed ID: 18071941
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Humanization of a highly stable single-chain antibody by structure-based antigen-binding site grafting.
    Villani ME; Morea V; Consalvi V; Chiaraluce R; Desiderio A; Benvenuto E; Donini M
    Mol Immunol; 2008 May; 45(9):2474-85. PubMed ID: 18313757
    [TBL] [Abstract][Full Text] [Related]  

  • 12. Production of functionalized single-chain Fv antibody fragments binding to the ED-B domain of the B-isoform of fibronectin in Pichia pastoris.
    Marty C; Scheidegger P; Ballmer-Hofer K; Klemenz R; Schwendener RA
    Protein Expr Purif; 2001 Feb; 21(1):156-64. PubMed ID: 11162401
    [TBL] [Abstract][Full Text] [Related]  

  • 13. In vitro folding and thermodynamic stability of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm.
    Martineau P; Betton JM
    J Mol Biol; 1999 Oct; 292(4):921-9. PubMed ID: 10525415
    [TBL] [Abstract][Full Text] [Related]  

  • 14. Gene cloning, bacterial expression, in vitro refolding, and characterization of a single-chain Fv antibody against PreS1(21-47) fragment of HBsAg.
    Yang X; Hu W; Li F; Xia H; Zhang Z
    Protein Expr Purif; 2005 Jun; 41(2):341-8. PubMed ID: 15866720
    [TBL] [Abstract][Full Text] [Related]  

  • 15. The importance of framework residues H6, H7 and H10 in antibody heavy chains: experimental evidence for a new structural subclassification of antibody V(H) domains.
    Jung S; Spinelli S; Schimmele B; Honegger A; Pugliese L; Cambillau C; Plückthun A
    J Mol Biol; 2001 Jun; 309(3):701-16. PubMed ID: 11397090
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Direct evidence by H/D exchange and ESI-MS for transient unproductive domain interaction in the refolding of an antibody scFv fragment.
    Jäger M; Plückthun A
    Protein Sci; 2000 Mar; 9(3):552-63. PubMed ID: 10752617
    [TBL] [Abstract][Full Text] [Related]  

  • 17. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly.
    Wörn A; Plückthun A
    FEBS Lett; 1998 May; 427(3):357-61. PubMed ID: 9637257
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Structure-based stability engineering of the mouse IgG1 Fab fragment by modifying constant domains.
    Teerinen T; Valjakka J; Rouvinen J; Takkinen K
    J Mol Biol; 2006 Aug; 361(4):687-97. PubMed ID: 16876195
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Improving the stability of an antibody variable fragment by a combination of knowledge-based approaches: validation and mechanisms.
    Monsellier E; Bedouelle H
    J Mol Biol; 2006 Sep; 362(3):580-93. PubMed ID: 16926023
    [TBL] [Abstract][Full Text] [Related]  

  • 20. A kinetic trap is an intrinsic feature in the folding pathway of single-chain Fv fragments.
    Hoyer W; Ramm K; Plückthun A
    Biophys Chem; 2002 May; 96(2-3):273-84. PubMed ID: 12034446
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 9.