Year |
Citation |
Score |
2014 |
Cheriyan M, Chan SH, Perler F. Traceless splicing enabled by substrate-induced activation of the Nostoc punctiforme Npu DnaE intein after mutation of a catalytic cysteine to serine. Journal of Molecular Biology. 426: 4018-29. PMID 25451033 DOI: 10.1016/J.Jmb.2014.10.025 |
0.496 |
|
2013 |
Cheriyan M, Pedamallu CS, Tori K, Perler F. Faster protein splicing with the Nostoc punctiforme DnaE intein using non-native extein residues. The Journal of Biological Chemistry. 288: 6202-11. PMID 23306197 DOI: 10.1074/Jbc.M112.433094 |
0.465 |
|
2012 |
Tori K, Cheriyan M, Pedamallu CS, Contreras MA, Perler FB. The Thermococcus kodakaraensis Tko CDC21-1 intein activates its N-terminal splice junction in the absence of a conserved histidine by a compensatory mechanism. Biochemistry. 51: 2496-505. PMID 22380677 DOI: 10.1021/Bi201840K |
0.528 |
|
2012 |
Cheriyan M, Toone EJ, Fierke CA. Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates. Biochemistry. 51: 1658-68. PMID 22316217 DOI: 10.1021/Bi201899B |
0.66 |
|
2011 |
Cheriyan M, Walters MJ, Kang BD, Anzaldi LL, Toone EJ, Fierke CA. Directed evolution of a pyruvate aldolase to recognize a long chain acyl substrate. Bioorganic & Medicinal Chemistry. 19: 6447-53. PMID 21944547 DOI: 10.1016/J.Bmc.2011.08.056 |
0.599 |
|
2007 |
Cheriyan M, Toone EJ, Fierke CA. Mutagenesis of the phosphate-binding pocket of KDPG aldolase enhances selectivity for hydrophobic substrates. Protein Science : a Publication of the Protein Society. 16: 2368-77. PMID 17962400 DOI: 10.1110/Ps.073042907 |
0.64 |
|
2006 |
Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH. Mechanism of the Class I KDPG aldolase. Bioorganic & Medicinal Chemistry. 14: 3002-10. PMID 16403639 DOI: 10.1016/J.Bmc.2005.12.022 |
0.577 |
|
2004 |
Griffiths JS, Cheriyan M, Corbell JB, Pocivavsek L, Fierke CA, Toone EJ. A bacterial selection for the directed evolution of pyruvate aldolases. Bioorganic & Medicinal Chemistry. 12: 4067-74. PMID 15246084 DOI: 10.1016/J.Bmc.2004.05.034 |
0.588 |
|
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