| scholarly article | Q13442814 |
| P356 | DOI | 10.1074/JBC.271.17.10010 |
| P698 | PubMed publication ID | 8626554 |
| P2093 | author name string | Aqvist J | |
| Fothergill M | |||
| P2860 | cites work | Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway | Q27661173 |
| Structure of yeast triosephosphate isomerase at 1.9-A resolution | Q27675336 | ||
| Enzyme catalysis: not different, just better | Q28269755 | ||
| Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism | Q28281585 | ||
| Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. | Q30353521 | ||
| Design, creation, and characterization of a stable, monomeric triosephosphate isomerase | Q35055478 | ||
| Computer simulation of the initial proton transfer step in human carbonic anhydrase I | Q35225998 | ||
| Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase | Q38319872 | ||
| Free energy via molecular simulation: applications to chemical and biomolecular systems | Q38648060 | ||
| Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli | Q42206966 | ||
| The pKa and keto-enol equilibrium constant of acetone in aqueous solution | Q42343162 | ||
| Analysis of ground-state and transition-state effects in enzyme catalysis | Q44288349 | ||
| How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases | Q44701613 | ||
| Molecular dynamics simulations of "loop closing" in the enzyme triose phosphate isomerase | Q46645011 | ||
| An SCF Solvation Model for the Hydrophobic Effect and Absolute Free Energies of Aqueous Solvation | Q57250708 | ||
| P433 | issue | 17 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | computer simulation | Q925667 |
| P304 | page(s) | 10010-10016 | |
| P577 | publication date | 1996-04-01 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Computer simulation of the triosephosphate isomerase catalyzed reaction | |
| P478 | volume | 271 |
| Q39482505 | An analysis of reaction pathways for proton tunnelling in methylamine dehydrogenase |
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| Q35590769 | Catalysis and specificity in enzymes: a study of triosephosphate isomerase and comparison with methyl glyoxal synthase |
| Q73216607 | Competitive inhibitors of yeast phosphoglucose isomerase: synthesis and evaluation of new types of phosphorylated sugars from the synthon D-arabinolactone-5-phosphate |
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| Q28239049 | Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis |
| Q46023362 | Electrostatic basis for bioenergetics. |
| Q47959634 | Electrostatic effects in macromolecules: fundamental concepts and practical modeling |
| Q77993672 | Energetics of the proposed rate-determining step of the glyoxalase I reaction |
| Q41246660 | Enzyme Architecture: Modeling the Operation of a Hydrophobic Clamp in Catalysis by Triosephosphate Isomerase |
| Q37055269 | Free energies of chemical reactions in solution and in enzymes with ab initio quantum mechanics/molecular mechanics methods |
| Q36627431 | Modeling electrostatic effects in proteins |
| Q44387969 | On the generation of catalytic antibodies by transition state analogues. |
| Q27640262 | Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. |
| Q38658999 | Polarizable Force Fields: History, Test Cases, and Prospects |
| Q44148708 | Quantifying free energy profiles of proton transfer reactions in solution and proteins by using a diabatic FDFT mapping |
| Q52363202 | Role of Ligand-Driven Conformational Changes in Enzyme Catalysis: Modeling the Reactivity of the Catalytic Cage of Triosephosphate Isomerase. |
| Q27635230 | Structural determinants for ligand binding and catalysis of triosephosphate isomerase |
| Q27642369 | Structure of Plasmodium falciparum triose-phosphate isomerase-2-phosphoglycerate complex at 1.1-A resolution |
| Q35590761 | Structure/function correlations of proteins using MM, QM/MM, and related approaches: methods, concepts, pitfalls, and current progress |
| Q41904561 | The EVB as a quantitative tool for formulating simulations and analyzing biological and chemical reactions |
| Q40533640 | The control of the discrimination between dNTP and rNTP in DNA and RNA polymerase |
| Q27638924 | The crystal structure of rabbit phosphoglucose isomerase complexed with 5-phospho-D-arabinonohydroxamic acid. |
| Q28206747 | Triosephosphate isomerase: a theoretical comparison of alternative pathways |
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