Edward N. Baker

Affiliations: 
Department of Chemistry and Biochemistry Massey University (New Zealand) 
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"Edward Baker"
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Clyde A Smith grad student 1988-1993 (Crystallography Tree)
Richard L. Kingston grad student 1992-1996 Massey University (New Zealand)
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Publications

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Huang A, Burke J, Bunker RD, et al. (2019) Regulation of human 4-hydroxy-2-oxoglutarate aldolase by pyruvate and α-ketoglutarate. Implications for Primary Hyperoxaluria Type-3. The Biochemical Journal
Bashiri G, Grove TL, Hegde SS, et al. (2019) The active site of the branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase contains a 2Fe-2S cluster. The Journal of Biological Chemistry
Almo SC, Grove TL, Bashiri G, et al. (2019) Dihydroxyacid dehydratase (IlvD) from Mycobacterium tuberculosis is an essential biosynthetic enzyme with an Fe2-S2 cluster at its active site Journal of Biological Chemistry
Kwon H, Young PG, Squire CJ, et al. (2017) Engineering a Lys-Asn isopeptide bond into an immunoglobulin-like protein domain enhances its stability. Scientific Reports. 7: 42753
Young PG, Yosaatmadja Y, Harris PW, et al. (2017) Harnessing ester bond chemistry for protein ligation. Chemical Communications (Cambridge, England)
Raynes JM, Frost HR, Williamson DA, et al. (2016) Serological Evidence of Immune Priming by Group A Streptococci in Patients with Acute Rheumatic Fever. Frontiers in Microbiology. 7: 1119
Yeung H, Squire CJ, Yosaatmadja Y, et al. (2016) Radiation Damage and Racemic Protein Crystallography Reveal the Unique Structure of the GASA/Snakin Protein Superfamily. Angewandte Chemie (International Ed. in English)
Son SJ, Harris PW, Squire CJ, et al. (2016) Synthesis and structural insight into ESX-1 substrate protein C (EspC), an immunodominant Mycobacterium tuberculosis-secreted antigen. Biopolymers
Ting YT, Harris PW, Batot G, et al. (2016) Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization. Iucrj. 3: 10-9
Bashiri G, Rehan AM, Sreebhavan S, et al. (2016) Elongation of the poly-γ-glutamate tail of F420 requires both domains of the F420:γ-glutamyl ligase (FbiB) of Mycobacterium tuberculosis. The Journal of Biological Chemistry
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