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1. Evolution of nanobodies specific for BCL11A

2. Structural insights into bacterial sterol transport

3. Nuclear Resonance Vibrational Spectroscopic Definition of the Facial Triad FeIV═O Intermediate in Taurine Dioxygenase: Evaluation of Structural Contributions to Hydrogen Atom Abstraction

4. MbnH is a diheme MauG-like protein associated with microbial copper homeostasis

5. The enzymology of oxazolone and thioamide synthesis in methanobactin

6. The enzymology of oxazolone and thioamide synthesis in methanobactin

7. Nuclear Resonance Vibrational Spectroscopic Definition of the Facial Triad Fe

8. O–H Activation by an Unexpected Ferryl Intermediate during Catalysis by 2-Hydroxyethylphosphonate Dioxygenase

9. Transport and synthesis of a bacterial natural product

10. Methanobactins: from genome to function

11. Methanobactin transport machinery

12. Rational targeting of a NuRD subcomplex guided by comprehensive in situ mutagenesis

13. Rational Targeting of a NuRD Sub-Complex for Fetal Hemoglobin Induction Following Comprehensive in Situ Mutagenesis

14. Novel approaches for the accumulation of oxygenated intermediates to multi-millimolar concentrations

15. Evidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1

16. Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis

17. Geometric and Electronic Structure of the Mn(IV)Fe(III) Cofactor in Class Ic Ribonucleotide Reductase: Correlation to the Class Ia Binuclear Non-Heme Iron Enzyme

18. A 2.8 Å Fe-Fe separation in the Fe2(III/IV) intermediate, X, from Escherichia coli ribonucleotide reductase

19. Structural basis for assembly of the Mn(IV)/Fe(III) cofactor in the class Ic ribonucleotide reductase from Chlamydia trachomatis

20. Radical-translocation Intermediates and Hurdling of Pathway Defects in 'Super-oxidized' (MnIV/FeIV) Chlamydia trachomatis Ribonucleotide Reductase

21. O2-evolving Chlorite Dismutase as a Tool to Study O2-Utilizing Enzymes†

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