| Year |
Citation |
Score |
| 2020 |
Zhai X, Ward RA, Doig P, Argyrou A. Insight into the Therapeutic Selectivity of the Irreversible EGFR Tyrosine Kinase Inhibitor Osimertinib through Enzyme Kinetic Studies. Biochemistry. PMID 32207968 DOI: 10.1021/Acs.Biochem.0C00104 |
0.391 |
|
| 2018 |
Zhai X, Reinhardt CJ, Malabanan MM, Amyes TL, Richard JP. Enzyme Architecture: Amino Acid Side Chains Which Function to Optimize the Basicity of the Active Site Glutamate of Triosephosphate Isomerase. Journal of the American Chemical Society. PMID 29862813 DOI: 10.1021/Jacs.8B04367 |
0.759 |
|
| 2018 |
Zhai X, Meek TD. Catalytic Mechanism of Cruzain from Trypanosoma cruzi as Determined from Solvent Kinetic Isotope Effects of Steady-State and Pre-Steady-State Kinetics. Biochemistry. PMID 29336553 DOI: 10.1021/Acs.Biochem.7B01250 |
0.509 |
|
| 2016 |
Amyes TL, Malabanan MM, Zhai X, Reyes AC, Richard JP. Enzyme activation through the utilization of intrinsic dianion binding energy. Protein Engineering, Design & Selection : Peds. PMID 27903763 DOI: 10.1093/Protein/Gzw064 |
0.758 |
|
| 2016 |
Richard JP, Amyes TL, Malabanan MM, Zhai X, Kim KJ, Reinhardt CJ, Wierenga RK, Drake EJ, Gulick AM. Structure-Function Studies on Hydrophobic Residues that Clamp a Basic Glutamate Side-Chain During Catalysis by Triosephosphate Isomerase. Biochemistry. PMID 27149328 DOI: 10.1021/Acs.Biochem.6B00311 |
0.773 |
|
| 2015 |
Zhai X, Amyes TL, Richard JP. The Role of Loop-Clamping Side Chains in Catalysis by Triosephosphate Isomerase. Journal of the American Chemical Society. PMID 26570983 DOI: 10.1021/Jacs.5B09328 |
0.701 |
|
| 2015 |
Reyes AC, Zhai X, Morgan KT, Reinhardt CJ, Amyes TL, Richard JP. The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: specificity and enzyme architecture. Journal of the American Chemical Society. 137: 1372-82. PMID 25555107 DOI: 10.1021/Ja5123842 |
0.82 |
|
| 2015 |
Reyes AC, Zhai X, Morgan KT, Reinhardt CJ, Amyes TL, Richard JP. The activating oxydianion binding domain for enzyme-catalyzed proton transfer, hydride transfer, and decarboxylation: Specificity and enzyme architecture Journal of the American Chemical Society. 137: 1372-1382. DOI: 10.1021/ja5123842 |
0.767 |
|
| 2014 |
Richard JP, Zhai X, Malabanan MM. Reflections on the catalytic power of a TIM-barrel. Bioorganic Chemistry. 57: 206-12. PMID 25092608 DOI: 10.1016/J.Bioorg.2014.07.001 |
0.792 |
|
| 2014 |
Zhai X, Go MK, O'Donoghue AC, Amyes TL, Pegan SD, Wang Y, Loria JP, Mesecar AD, Richard JP. Enzyme architecture: the effect of replacement and deletion mutations of loop 6 on catalysis by triosephosphate isomerase. Biochemistry. 53: 3486-501. PMID 24825099 DOI: 10.1021/Bi500458T |
0.79 |
|
| 2014 |
Zhai X, Malabanan MM, Amyes TL, Richard JP. Mechanistic Imperatives for Deprotonation of Carbon Catalyzed by Triosephosphate Isomerase: Enzyme-Activation by Phosphite Dianion. Journal of Physical Organic Chemistry. 27: 269-276. PMID 24729658 DOI: 10.1002/Poc.3195 |
0.8 |
|
| 2014 |
Richard JP, Amyes TL, Goryanova B, Zhai X. Enzyme architecture: on the importance of being in a protein cage. Current Opinion in Chemical Biology. 21: 1-10. PMID 24699188 DOI: 10.1016/J.Cbpa.2014.03.001 |
0.772 |
|
| 2014 |
Zhai X, Amyes TL, Richard JP. Enzyme architecture: remarkably similar transition states for triosephosphate isomerase-catalyzed reactions of the whole substrate and the substrate in pieces. Journal of the American Chemical Society. 136: 4145-8. PMID 24588650 DOI: 10.1021/Ja501103B |
0.705 |
|
| 2013 |
Zhai X, Amyes TL, Wierenga RK, Loria JP, Richard JP. Structural mutations that probe the interactions between the catalytic and dianion activation sites of triosephosphate isomerase. Biochemistry. 52: 5928-40. PMID 23909928 DOI: 10.1021/Bi401019H |
0.693 |
|
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