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PUBMED FOR HANDHELDS

Journal Abstract Search


319 related items for PubMed ID: 8431430

  • 1. Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form.
    Alexander RS, Kiefer LL, Fierke CA, Christianson DW.
    Biochemistry; 1993 Feb 16; 32(6):1510-8. PubMed ID: 8431430
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  • 3. Structure of His94-->Asp carbonic anhydrase II in a new crystalline form reveals a partially occupied zinc binding site.
    Ippolito JA, Nair SK, Alexander RS, Kiefer LL, Fierke CA, Christianson DW.
    Protein Eng; 1995 Oct 16; 8(10):975-80. PubMed ID: 8771178
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  • 4. Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II.
    Ippolito JA, Christianson DW.
    Biochemistry; 1993 Sep 28; 32(38):9901-5. PubMed ID: 8399159
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  • 5. Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity.
    Ippolito JA, Baird TT, McGee SA, Christianson DW, Fierke CA.
    Proc Natl Acad Sci U S A; 1995 May 23; 92(11):5017-21. PubMed ID: 7761440
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  • 10. Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II.
    Huang CC, Lesburg CA, Kiefer LL, Fierke CA, Christianson DW.
    Biochemistry; 1996 Mar 19; 35(11):3439-46. PubMed ID: 8639494
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  • 11. Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II.
    Cox JD, Hunt JA, Compher KM, Fierke CA, Christianson DW.
    Biochemistry; 2000 Nov 14; 39(45):13687-94. PubMed ID: 11076507
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  • 12. Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II.
    Fierke CA, Calderone TL, Krebs JF.
    Biochemistry; 1991 Nov 19; 30(46):11054-63. PubMed ID: 1657158
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  • 18. Structure-based design of an intramolecular proton transfer site in murine carbonic anhydrase V.
    Heck RW, Boriack-Sjodin PA, Qian M, Tu C, Christianson DW, Laipis PJ, Silverman DN.
    Biochemistry; 1996 Sep 10; 35(36):11605-11. PubMed ID: 8794740
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