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4. Design of a serine protease-like catalytic triad on an antibody light chain displayed on the yeast cell surface. Okochi N; Kato-Murai M; Kadonosono T; Ueda M Appl Microbiol Biotechnol; 2007 Dec; 77(3):597-603. PubMed ID: 17899065 [TBL] [Abstract][Full Text] [Related]
5. Positional ordering of reacting groups contributes significantly to the efficiency of proton transfer at an antibody active site. Seebeck FP; Hilvert D J Am Chem Soc; 2005 Feb; 127(4):1307-12. PubMed ID: 15669871 [TBL] [Abstract][Full Text] [Related]
6. Natural catalytic antibodies. Paul S Mol Biotechnol; 1996 Jun; 5(3):197-207. PubMed ID: 8837026 [TBL] [Abstract][Full Text] [Related]
7. From molecular diversity to catalysis: lessons from the immune system. Schultz PG; Lerner RA Science; 1995 Sep; 269(5232):1835-42. PubMed ID: 7569920 [TBL] [Abstract][Full Text] [Related]
8. Site-directed mutagenesis of proteolytic antibody light chain. Gao QS; Sun M; Rees AR; Paul S J Mol Biol; 1995 Nov; 253(5):658-64. PubMed ID: 7473741 [TBL] [Abstract][Full Text] [Related]
10. Crystal structure of a catalytic antibody with a serine protease active site. Zhou GW; Guo J; Huang W; Fletterick RJ; Scanlan TS Science; 1994 Aug; 265(5175):1059-64. PubMed ID: 8066444 [TBL] [Abstract][Full Text] [Related]
11. Analysis of hapten binding and catalytic determinants in a family of catalytic antibodies. Ulrich HD; Schultz PG J Mol Biol; 1998 Jan; 275(1):95-111. PubMed ID: 9451442 [TBL] [Abstract][Full Text] [Related]
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13. Systemic lupus erythematosus: molecular cloning and analysis of recombinant monoclonal kappa light chain NGTA2-Me-pro-ChTr possessing two different activities-trypsin-like and metalloprotease. Timofeeva AM; Ivanisenko NV; Buneva VN; Nevinsky GA Int Immunol; 2015 Dec; 27(12):633-45. PubMed ID: 26174315 [TBL] [Abstract][Full Text] [Related]
14. Probing the importance of second sphere residues in an esterolytic antibody by phage display. Arkin MR; Wells JA J Mol Biol; 1998 Dec; 284(4):1083-94. PubMed ID: 9837728 [TBL] [Abstract][Full Text] [Related]
15. In vitro abzyme evolution to optimize antibody recognition for catalysis. Takahashi N; Kakinuma H; Liu L; Nishi Y; Fujii I Nat Biotechnol; 2001 Jun; 19(6):563-7. PubMed ID: 11385462 [TBL] [Abstract][Full Text] [Related]
16. Completing the circle. Schultz PG; Lerner RA Nature; 2002 Aug; 418(6897):485. PubMed ID: 12152057 [No Abstract] [Full Text] [Related]
17. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Baca M; Scanlan TS; Stephenson RC; Wells JA Proc Natl Acad Sci U S A; 1997 Sep; 94(19):10063-8. PubMed ID: 9294163 [TBL] [Abstract][Full Text] [Related]
18. Transition state docking: a probe for noncovalent catalysis in biological systems. Application to antibody-catalyzed ester hydrolysis. Tantillo DJ; Houk KN J Comput Chem; 2002 Jan; 23(1):84-95. PubMed ID: 11913392 [TBL] [Abstract][Full Text] [Related]
20. Just a near attack conformer for catalysis (chorismate to prephenate rearrangements in water, antibody, enzymes, and their mutants). Hur S; Bruice TC J Am Chem Soc; 2003 Sep; 125(35):10540-2. PubMed ID: 12940735 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]