Year |
Citation |
Score |
2014 |
Bansal S, Goel G, Ojha S. Applications of industrially important enzymes Industrial Enzymes: Trends, Scope and Relevance. 50-71. |
0.307 |
|
2013 |
Dai X, Mashiguchi K, Chen Q, Kasahara H, Kamiya Y, Ojha S, DuBois J, Ballou D, Zhao Y. The biochemical mechanism of auxin biosynthesis by an arabidopsis YUCCA flavin-containing monooxygenase. The Journal of Biological Chemistry. 288: 1448-57. PMID 23188833 DOI: 10.1074/Jbc.M112.424077 |
0.332 |
|
2006 |
Pegg SC, Brown SD, Ojha S, Seffernick J, Meng EC, Morris JH, Chang PJ, Huang CC, Ferrin TE, Babbitt PC. Leveraging enzyme structure-function relationships for functional inference and experimental design: the structure-function linkage database. Biochemistry. 45: 2545-55. PMID 16489747 DOI: 10.1021/Bi052101L |
0.349 |
|
2004 |
Evande R, Ojha S, Banerjee R. Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base. Archives of Biochemistry and Biophysics. 427: 188-96. PMID 15196993 DOI: 10.1016/J.Abb.2004.04.027 |
0.661 |
|
2003 |
Banerjee R, Evande R, Kabil O, Ojha S, Taoka S. Reaction mechanism and regulation of cystathionine beta-synthase. Biochimica Et Biophysica Acta. 1647: 30-5. PMID 12686104 DOI: 10.1016/S1570-9639(03)00044-X |
0.657 |
|
2002 |
Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R. Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 41: 10454-61. PMID 12173932 DOI: 10.1021/Bi026052D |
0.652 |
|
2002 |
Ojha S, Wu J, LoBrutto R, Banerjee R. Effects of heme ligand mutations including a pathogenic variant, H65R, on the properties of human cystathionine beta-synthase. Biochemistry. 41: 4649-54. PMID 11926827 DOI: 10.1021/Bi011827O |
0.618 |
|
2000 |
Ojha S, Hwang J, Kabil O, Penner-Hahn JE, Banerjee R. Characterization of the heme in human cystathionine beta-synthase by X-ray absorption and electron paramagnetic resonance spectroscopies. Biochemistry. 39: 10542-7. PMID 10956045 DOI: 10.1021/Bi000831H |
0.652 |
|
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