| Year |
Citation |
Score |
| 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 |
0.691 |
|
| 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 |
0.724 |
|
| 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 |
0.702 |
|
| 2016 |
Malabanan MM, Blind RD. Inositol polyphosphate multikinase (IPMK) in transcriptional regulation and nuclear inositide metabolism. Biochemical Society Transactions. 44: 279-85. PMID 26862216 DOI: 10.1042/Bst20150225 |
0.664 |
|
| 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 |
0.722 |
|
| 2014 |
Mashiyama ST, Malabanan MM, Akiva E, Bhosle R, Branch MC, Hillerich B, Jagessar K, Kim J, Patskovsky Y, Seidel RD, Stead M, Toro R, Vetting MW, Almo SC, Armstrong RN, et al. Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere. Plos Biology. 12: e1001843. PMID 24756107 DOI: 10.1371/Journal.Pbio.1001843 |
0.671 |
|
| 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 |
0.734 |
|
| 2013 |
Malabanan MM, Nitsch-Velasquez L, Amyes TL, Richard JP. Magnitude and origin of the enhanced basicity of the catalytic glutamate of triosephosphate isomerase. Journal of the American Chemical Society. 135: 5978-81. PMID 23560625 DOI: 10.1021/Ja401504W |
0.588 |
|
| 2012 |
Malabanan MM, Koudelka AP, Amyes TL, Richard JP. Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a hydrophobic clamp. Journal of the American Chemical Society. 134: 10286-98. PMID 22583393 DOI: 10.1021/Ja303695U |
0.631 |
|
| 2011 |
Malabanan MM, Amyes TL, Richard JP. Mechanism for activation of triosephosphate isomerase by phosphite dianion: the role of a ligand-driven conformational change. Journal of the American Chemical Society. 133: 16428-31. PMID 21939233 DOI: 10.1021/Ja208019P |
0.648 |
|
| 2011 |
Malabanan MM, Go MK, Amyes TL, Richard JP. Wildtype and engineered monomeric triosephosphate isomerase from Trypanosoma brucei: partitioning of reaction intermediates in D2O and activation by phosphite dianion. Biochemistry. 50: 5767-79. PMID 21553855 DOI: 10.1021/Bi2005416 |
0.726 |
|
| 2010 |
Malabanan MM, Amyes TL, Richard JP. A role for flexible loops in enzyme catalysis. Current Opinion in Structural Biology. 20: 702-10. PMID 20951028 DOI: 10.1016/J.Sbi.2010.09.005 |
0.615 |
|
| 2010 |
Go MK, Malabanan MM, Amyes TL, Richard JP. Bovine serum albumin-catalyzed deprotonation of [1-(13)C]glycolaldehyde: protein reactivity toward deprotonation of the alpha-hydroxy alpha-carbonyl carbon. Biochemistry. 49: 7704-8. PMID 20687575 DOI: 10.1021/Bi101118G |
0.694 |
|
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