| Year |
Citation |
Score |
| 2020 |
Szeler K, Williams NH, Hengge AC, Kamerlin SCL. Modeling the Alkaline Hydrolysis of Diaryl Sulfate Diesters: A Mechanistic Study. The Journal of Organic Chemistry. PMID 32309943 DOI: 10.1021/Acs.Joc.0C00441 |
0.517 |
|
| 2019 |
van Loo B, Berry R, Boonyuen U, Mohamed MF, Golicnik M, Hengge AC, Hollfelder F. Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase. Biochemistry. PMID 30810299 DOI: 10.1021/Acs.Biochem.8B00996 |
0.548 |
|
| 2019 |
Bigley AN, Xiang DF, Narindoshvili T, Burgert CW, Hengge AC, Raushel FM. Transition State Analysis of the Reaction Catalyzed by the Phosphotriesterase from Sphingobium sp. TCM1. Biochemistry. PMID 30730705 DOI: 10.1021/Acs.Biochem.9B00041 |
0.71 |
|
| 2019 |
Costa DMA, Gómez SV, de Araújo SS, Pereira MS, Alves RB, Favaro DC, Hengge AC, Nagem RAP, Brandão TAS. Catalytic mechanism for the conversion of salicylate into catechol by the flavin-dependent monooxygenase salicylate hydroxylase. International Journal of Biological Macromolecules. PMID 30703421 DOI: 10.1016/J.Ijbiomac.2019.01.135 |
0.777 |
|
| 2018 |
Moise G, Morales Y, Beaumont V, Caradonna T, Loria JP, Johnson SJ, Hengge AC. A YopH PTP1B Chimera shows the importance of WPD-loop sequence to activity, structure, and dynamics in protein tyrosine phosphatases. Biochemistry. PMID 30110154 DOI: 10.1021/Acs.Biochem.8B00663 |
0.395 |
|
| 2017 |
Chu Y, Williams NH, Hengge AC. Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1. Biochemistry. PMID 28678475 DOI: 10.1021/Acs.Biochem.7B00441 |
0.686 |
|
| 2016 |
Coitinho JB, Pereira MS, Costa DM, Guimaraes SL, de Araujo SS, Hengge AC, Brandao TA, Nagem RA. Structural and kinetic properties of the aldehyde dehydrogenase NahF, a broad substrate specificity enzyme for aldehyde oxidation. Biochemistry. PMID 27580341 DOI: 10.1021/Acs.Biochem.6B00614 |
0.792 |
|
| 2016 |
Pereira MS, Murta B, Oliveira TC, Manfredi AM, Nome F, Hengge AC, Brandao TA. Mechanistic aspects of phosphate diester cleavage assisted by imidazole. A template reaction for obtaining aryl phosphoimidazoles. The Journal of Organic Chemistry. PMID 27392322 DOI: 10.1021/Acs.Joc.6B01358 |
0.841 |
|
| 2015 |
Moise G, Gallup NM, Alexandrova AN, Hengge AC, Johnson SJ. Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites. Biochemistry. 54: 6490-500. PMID 26445170 DOI: 10.1021/Acs.Biochem.5B00496 |
0.363 |
|
| 2015 |
Hengge AC. Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases. Biochimica Et Biophysica Acta. 1854: 1768-75. PMID 25840000 DOI: 10.1016/J.Bbapap.2015.03.010 |
0.472 |
|
| 2013 |
Kuznetsov VI, Hengge AC. New functional aspects of the atypical protein tyrosine phosphatase VHZ. Biochemistry. 52: 8012-25. PMID 24073992 DOI: 10.1021/Bi400776Z |
0.595 |
|
| 2013 |
Whittier SK, Hengge AC, Loria JP. Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases. Science (New York, N.Y.). 341: 899-903. PMID 23970698 DOI: 10.1126/Science.1241735 |
0.412 |
|
| 2013 |
Hengge AC. Chemistry and mechanism of phosphatases, diesterases and triesterases. Biochimica Et Biophysica Acta. 1834: 415-6. PMID 23267546 DOI: 10.1016/J.Bbapap.2012.09.013 |
0.476 |
|
| 2013 |
Whittier S, Hengge A, Loria JP. Coupling of Loop Closure and Chemistry in Protein Tyrosine Phosphatases Biophysical Journal. 104: 30a. DOI: 10.1016/J.Bpj.2012.11.204 |
0.415 |
|
| 2012 |
Kuznetsov VI, Hengge AC, Johnson SJ. New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening. Biochemistry. 51: 9869-79. PMID 23145819 DOI: 10.1021/Bi300908Y |
0.554 |
|
| 2012 |
Kuznetsov VI, Alexandrova AN, Hengge AC. Metavanadate at the active site of the phosphatase VHZ Journal of the American Chemical Society. 134: 14298-14301. PMID 22876963 DOI: 10.1021/Ja305579H |
0.582 |
|
| 2012 |
Brandão TA, Johnson SJ, Hengge AC. The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Archives of Biochemistry and Biophysics. 525: 53-9. PMID 22698963 DOI: 10.1016/J.Abb.2012.06.002 |
0.711 |
|
| 2011 |
Smith GK, Ke Z, Guo H, Hengge AC. Insights into the phosphoryl transfer mechanism of cyclin-dependent protein kinases from ab initio QM/MM free-energy studies. The Journal of Physical Chemistry. B. 115: 13713-22. PMID 21999515 DOI: 10.1021/Jp207532S |
0.45 |
|
| 2010 |
Mitić N, Hadler KS, Gahan LR, Hengge AC, Schenk G. The divalent metal ion in the active site of uteroferrin modulates substrate binding and catalysis. Journal of the American Chemical Society. 132: 7049-54. PMID 20433174 DOI: 10.1021/Ja910583Y |
0.338 |
|
| 2010 |
Brandão TA, Hengge AC, Johnson SJ. Insights into the reaction of protein-tyrosine phosphatase 1B: crystal structures for transition state analogs of both catalytic steps. The Journal of Biological Chemistry. 285: 15874-83. PMID 20236928 DOI: 10.1074/Jbc.M109.066951 |
0.78 |
|
| 2009 |
Smith GK, Ke Z, Hengge AC, Xu D, Xie D, Guo H. Active-site dynamics of SpvC virulence factor from Salmonella typhimurium and density functional theory study of phosphothreonine lyase catalysis. The Journal of Physical Chemistry. B. 113: 15327-33. PMID 19715325 DOI: 10.1021/Jp9052677 |
0.415 |
|
| 2009 |
Feng G, Tanifum EA, Adams H, Hengge AC, Williams NH. Mechanism and transition state structure of aryl methylphosphonate esters doubly coordinated to a dinuclear cobalt(III) center. Journal of the American Chemical Society. 131: 12771-9. PMID 19673521 DOI: 10.1021/Ja904134N |
0.502 |
|
| 2009 |
Brandão TA, Robinson H, Johnson SJ, Hengge AC. Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society. 131: 778-86. PMID 19140798 DOI: 10.1021/Ja807418B |
0.728 |
|
| 2008 |
Humphry T, Iyer S, Iranzo O, Morrow JR, Richard JP, Paneth P, Hengge AC. Altered transition state for the reaction of an RNA model catalyzed by a dinuclear zinc(II) catalyst. Journal of the American Chemical Society. 130: 17858-66. PMID 19053445 DOI: 10.1021/Ja8059864 |
0.831 |
|
| 2008 |
Hengge AC. NMR data do not implicate a phosphorane in the T4 DNA ligase reaction. Proceedings of the National Academy of Sciences of the United States of America. 105: E84; author reply E8. PMID 19004796 DOI: 10.1073/Pnas.0806371105 |
0.349 |
|
| 2008 |
Hadler KS, Tanifum EA, Yip SH, Mitić N, Guddat LW, Jackson CJ, Gahan LR, Nguyen K, Carr PD, Ollis DL, Hengge AC, Larrabee JA, Schenk G. Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes. Journal of the American Chemical Society. 130: 14129-38. PMID 18831553 DOI: 10.1021/Ja803346W |
0.45 |
|
| 2008 |
McWhirter C, Lund EA, Tanifum EA, Feng G, Sheikh QI, Hengge AC, Williams NH. Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzyme. Journal of the American Chemical Society. 130: 13673-82. PMID 18798625 DOI: 10.1021/Ja803612Z |
0.57 |
|
| 2008 |
Iyer S, Hengge AC. The effects of sulfur substitution for the nucleophile and bridging oxygen atoms in reactions of hydroxyalkyl phosphate esters. The Journal of Organic Chemistry. 73: 4819-29. PMID 18533704 DOI: 10.1021/Jo8002198 |
0.698 |
|
| 2007 |
Cox RS, Schenk G, Mitić N, Gahan LR, Hengge AC. Diesterase activity and substrate binding in purple acid phosphatases. Journal of the American Chemical Society. 129: 9550-1. PMID 17636903 DOI: 10.1021/Ja072647Q |
0.486 |
|
| 2007 |
Zalatan JG, Catrina I, Mitchell R, Grzyska PK, O'brien PJ, Herschlag D, Hengge AC. Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis. Journal of the American Chemical Society. 129: 9789-98. PMID 17630738 DOI: 10.1021/Ja072196+ |
0.822 |
|
| 2007 |
Catrina I, O'Brien PJ, Purcell J, Nikolic-Hughes I, Zalatan JG, Hengge AC, Herschlag D. Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction. Journal of the American Chemical Society. 129: 5760-5. PMID 17411045 DOI: 10.1021/Ja069111+ |
0.838 |
|
| 2007 |
Wong FM, Wang J, Hengge AC, Wu W. Mechanism of rhodium-catalyzed carbene formation from diazo compounds. Organic Letters. 9: 1663-5. PMID 17408276 DOI: 10.1021/Ol070345N |
0.469 |
|
| 2007 |
Grzyska PK, Czyryca PG, Purcell J, Hengge AC. Transition State Differences in Hydrolysis Reactions of Alkyl versus Aryl Phosphate Monoester Monoanions [J. Am. Chem. Soc.2003,125, 13106−13111]. Journal of the American Chemical Society. 129: 5298-5298. DOI: 10.1021/Ja071527F |
0.817 |
|
| 2007 |
Hoff RH, Hengge AC. The use of isotopes in the study of reactions of acyl, phosphoryl, and sulfuryl esters Journal of Labelled Compounds and Radiopharmaceuticals. 50: 1026-1038. DOI: 10.1002/Jlcr.1433 |
0.42 |
|
| 2006 |
Rawlings J, Cleland WW, Hengge AC. Metal-catalyzed phosphodiester cleavage: secondary 18O isotope effects as an indicator of mechanism. Journal of the American Chemical Society. 128: 17120-5. PMID 17177465 DOI: 10.1021/Ja065931A |
0.704 |
|
| 2006 |
Sorensen-Stowell K, Hengge AC. Thermodynamic origin of the increased rate of hydrolysis of phosphate and phosphorothioate esters in DMSO/water mixtures. The Journal of Organic Chemistry. 71: 7180-4. PMID 16958510 DOI: 10.1021/Jo060896B |
0.804 |
|
| 2006 |
Liu Y, Gregersen BA, Hengge A, York DM. Transesterification thio effects of phosphate diesters: free energy barriers and kinetic and equilibrium isotope effects from density-functional theory. Biochemistry. 45: 10043-53. PMID 16906762 DOI: 10.1021/Bi060869F |
0.431 |
|
| 2006 |
Hoff RH, Czyryca PG, Sun M, Leyh TS, Hengge AC. Transition state of the sulfuryl transfer reaction of estrogen sulfotransferase. The Journal of Biological Chemistry. 281: 30645-9. PMID 16899461 DOI: 10.1074/Jbc.M604205200 |
0.564 |
|
| 2006 |
Cleland WW, Hengge AC. Enzymatic mechanisms of phosphate and sulfate transfer. Chemical Reviews. 106: 3252-78. PMID 16895327 DOI: 10.1021/Cr050287O |
0.565 |
|
| 2005 |
Purcell J, Hengge AC. The thermodynamics of phosphate versus phosphorothioate ester hydrolysis. The Journal of Organic Chemistry. 70: 8437-42. PMID 16209589 DOI: 10.1021/Jo0511997 |
0.49 |
|
| 2005 |
Sorensen-Stowell K, Hengge AC. Probing potential medium effects on phosphate ester bonds using 18O isotope shifts on 31P NMR. The Journal of Organic Chemistry. 70: 8303-8. PMID 16209571 DOI: 10.1021/Jo051090Z |
0.791 |
|
| 2005 |
Sorensen-Stowell K, Hengge AC. Examination of P-OR bridging bond orders in phosphate monoesters using (18)O isotope shifts in 31P NMR. The Journal of Organic Chemistry. 70: 4805-9. PMID 15932321 DOI: 10.1021/Jo050359B |
0.794 |
|
| 2005 |
Onyido I, Swierczek K, Purcell J, Hengge AC. A concerted mechanism for the transfer of the thiophosphinoyl group from aryl dimethylphosphinothioate esters to oxyanionic nucleophiles in aqueous solution. Journal of the American Chemical Society. 127: 7703-11. PMID 15913360 DOI: 10.1021/Ja0501565 |
0.476 |
|
| 2005 |
Hengge AC, Onyido I. Physical organic perspectives on phospho group transfer from phosphates and phosphinates Current Organic Chemistry. 9: 61-74. DOI: 10.2174/1385272053369349 |
0.418 |
|
| 2005 |
Hengge AC. Mechanistic studies on enzyme-catalyzed phosphoryl transfer Advances in Physical Organic Chemistry. 40: 49-108. DOI: 10.1016/S0065-3160(05)40002-7 |
0.48 |
|
| 2004 |
Younker JM, Hengge AC. A mechanistic study of the alkaline hydrolysis of diaryl sulfate diesters. The Journal of Organic Chemistry. 69: 9043-8. PMID 15609936 DOI: 10.1021/Jo0488309 |
0.544 |
|
| 2004 |
Iyer S, Younker JM, Czyryca PG, Hengge AC. A nonhydrolyzable analogue of phosphotyrosine, and related aryloxymethano- and aryloxyethano-phosphonic acids as motifs for inhibition of phosphatases. Bioorganic & Medicinal Chemistry Letters. 14: 5931-5. PMID 15501071 DOI: 10.1016/J.Bmcl.2004.09.008 |
0.571 |
|
| 2004 |
Humphry T, Forconi M, Williams NH, Hengge AC. Altered mechanisms of reactions of phosphate esters bridging a dinuclear metal center. Journal of the American Chemical Society. 126: 11864-9. PMID 15382921 DOI: 10.1021/Ja047110G |
0.83 |
|
| 2004 |
Grzyska PK, Kim Y, Jackson MD, Hengge AC, Denu JM. Probing the transition-state structure of dual-specificity protein phosphatases using a physiological substrate mimic. Biochemistry. 43: 8807-14. PMID 15236589 DOI: 10.1021/Bi049473Z |
0.847 |
|
| 2004 |
McCain DF, Grzyska PK, Wu L, Hengge AC, Zhang ZY. Mechanistic studies of protein tyrosine phosphatases YopH and Cdc25A with m-nitrobenzyl phosphate. Biochemistry. 43: 8256-64. PMID 15209522 DOI: 10.1021/Bi0496182 |
0.86 |
|
| 2004 |
Hengge AC, Stein RL. Role of protein conformational mobility in enzyme catalysis: acylation of alpha-chymotrypsin by specific peptide substrates. Biochemistry. 43: 742-7. PMID 14730979 DOI: 10.1021/Bi030222K |
0.464 |
|
| 2004 |
Gibby SG, Younker JM, Hengge AC. Investigation of the sulfuryl transfer step from substrate to enzyme by arylsulfatases Journal of Physical Organic Chemistry. 17: 541-547. DOI: 10.1002/Poc.775 |
0.538 |
|
| 2003 |
Grzyska PK, Czyryca PG, Purcell J, Hengge AC. Transition state differences in hydrolysis reactions of alkyl versus aryl phosphate monoester monoanions. Journal of the American Chemical Society. 125: 13106-11. PMID 14570483 DOI: 10.1021/Ja036571J |
0.847 |
|
| 2003 |
Swierczek K, Pandey AS, Peters JW, Hengge AC. A comparison of phosphonothioic acids with phosphonic acids as phosphatase inhibitors. Journal of Medicinal Chemistry. 46: 3703-8. PMID 12904075 DOI: 10.1021/Jm030106F |
0.355 |
|
| 2003 |
Catrina IE, Hengge AC. Comparisons of phosphorothioate with phosphate transfer reactions for a monoester, diester, and triester: isotope effect studies. Journal of the American Chemical Society. 125: 7546-52. PMID 12812494 DOI: 10.1021/Ja0340026 |
0.84 |
|
| 2003 |
Rawlings J, Cleland WW, Hengge AC. Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate. Journal of Inorganic Biochemistry. 93: 61-5. PMID 12538053 DOI: 10.1016/S0162-0134(02)00435-X |
0.647 |
|
| 2002 |
Humphry T, Forconi M, Williams NH, Hengge AC. An altered mechanism of hydrolysis for a metal-complexed phosphate diester. Journal of the American Chemical Society. 124: 14860-1. PMID 12475323 DOI: 10.1021/Ja027671C |
0.843 |
|
| 2002 |
Hengge AC. Isotope effects in the study of phosphoryl and sulfuryl transfer reactions. Accounts of Chemical Research. 35: 105-12. PMID 11851388 DOI: 10.1021/Ar000143Q |
0.539 |
|
| 2002 |
Grzyska PK, Czyryca PG, Golightly J, Small K, Larsen P, Hoff RH, Hengge AC. Generality of solvation effects on the hydrolysis rates of phosphate monoesters and their possible relevance to enzymatic catalysis. The Journal of Organic Chemistry. 67: 1214-20. PMID 11846665 DOI: 10.1021/Jo016104P |
0.835 |
|
| 2002 |
McCain DF, Catrina IE, Hengge AC, Zhang ZY. The catalytic mechanism of Cdc25A phosphatase. The Journal of Biological Chemistry. 277: 11190-200. PMID 11805096 DOI: 10.1074/Jbc.M109636200 |
0.805 |
|
| 2002 |
Catrina IE, Czyryca PG, Hengge AC. Isotope effects on enzymatic and nonenzymatic reactions of phosphorothioates Nukleonika. 47. |
0.831 |
|
| 2001 |
Hoff RH, Larsen P, Hengge AC. Isotope effects and medium effects on sulfuryl transfer reactions Journal of the American Chemical Society. 123: 9338-9344. PMID 11562216 DOI: 10.1021/Ja0163974 |
0.59 |
|
| 2001 |
Hengge AC. Isotope effects in the study of enzymatic phosphoryl transfer reactions Febs Letters. 501: 99-102. PMID 11470264 DOI: 10.1016/S0014-5793(01)02638-2 |
0.476 |
|
| 2001 |
Czyryca PG, Hengge AC. The mechanism of the phosphoryl transfer catalyzed by Yersinia protein-tyrosine phosphatase: A computational and isotope effect study Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1547: 245-253. PMID 11410280 DOI: 10.1016/S0167-4838(01)00191-1 |
0.495 |
|
| 2001 |
Rigas JD, Hoff RH, Rice AE, Hengge AC, Denu JM. Transition state analysis and requirement of Asp-262 general acid/base catalyst for full activation of dual-specificity phosphatase MKP3 by extracellular regulated kinase. Biochemistry. 40: 4398-406. PMID 11284696 DOI: 10.1021/Bi002951V |
0.491 |
|
| 2000 |
Rishavy MA, Hengge AC, Cleland WW. Lanthanide Catalyzed Cyclization of Uridine 3'-p-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 283-292. PMID 11133147 DOI: 10.1006/Bioo.2000.1179 |
0.731 |
|
| 2000 |
Holtz KM, Catrina IE, Hengge AC, Kantrowitz ER. Mutation of Arg-166 of alkaline phosphatase alters the thio effect but not the transition state for phosphoryl transfer. Implications for the interpretation of thio effects in reactions of phosphatases. Biochemistry. 39: 9451-8. PMID 10924140 DOI: 10.1021/Bi000899X |
0.827 |
|
| 2000 |
Hengge AC, Bruzik KS, Tobin AE, Cleland WW, Tsai MD. Kinetic Isotope Effects and Stereochemical Studies on a Ribonuclease Model: Hydrolysis Reactions of Uridine 3'-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 119-133. PMID 10915550 DOI: 10.1006/Bioo.2000.1170 |
0.702 |
|
| 2000 |
Hoff RH, Hengge AC, Wu L, Keng YF, Zhang ZY. Effects on general acid catalysis from mutations of the invariant tryptophan and arginine residues in the protein tyrosine phosphatase from Yersinia Biochemistry. 39: 46-54. PMID 10625478 DOI: 10.1021/Bi991570I |
0.422 |
|
| 1999 |
Martin BL, Jurado LA, Hengge AC. Comparison of the reaction progress of calcineurin with Mn2+ and Mg2+ Biochemistry. 38: 3386-3392. PMID 10079083 DOI: 10.1021/Bi981748L |
0.392 |
|
| 1999 |
Hoff RH, Wu L, Zhou B, Zhang ZY, Hengge AC. Does positive charge at the active sites of phosphatases cause a change in mechanism? The effect of the conserved arginine on the transition state for phosphoryl transfer in the protein-tyrosine phosphatase from Yersinia Journal of the American Chemical Society. 121: 9514-9521. DOI: 10.1021/Ja992361O |
0.502 |
|
| 1999 |
Hoff RH, Mertz P, Rusnak F, Hengge AC. The transition state of the phosphoryl-transfer reaction catalyzed by the lambda Ser/Thr protein phosphatase Journal of the American Chemical Society. 121: 6382-6390. DOI: 10.1021/Ja990667P |
0.492 |
|
| 1999 |
Catrina IE, Hengge AC. Comparisons of phosphorothioate and phosphate monoester transfer reactions: Activation parameters, solvent effects, and the effect of metal ions Journal of the American Chemical Society. 121: 2156-2163. DOI: 10.1021/Ja983862X |
0.825 |
|
| 1998 |
Hoff RH, Hengge AC. Entropy and Enthalpy Contributions to Solvent Effects on Phosphate Monoester Solvolysis. The Importance of Entropy Effects in the Dissociative Transition State Journal of Organic Chemistry. 63: 6680-6688. DOI: 10.1021/Jo981160K |
0.454 |
|
| 1998 |
Hess RA, Hengge AC, Cleland WW. Isotope effects on enzyme-catalyzed acyl transfer from p-nitrophenyl acetate: Concerted mechanisms and increased hyperconjugation in the transition state Journal of the American Chemical Society. 120: 2703-2709. DOI: 10.1021/Ja973413H |
0.619 |
|
| 1998 |
Hoff RH, Hengge AC. Entropy effects in the catalytic efficiency of phosphatases Faseb Journal. 12. |
0.468 |
|
| 1998 |
Catrina IE, Hengge AC. Solution and enzymatic reactions of phosphorothioate monoesters: Thermodynamics and mechanisms Faseb Journal. 12. |
0.815 |
|
| 1997 |
Hengge AC, Martin BL. Isotope effect studies on the calcineurin phosphoryl-transfer reaction: Transition state structure and effect of calmodulin and Mn2+ Biochemistry. 36: 10185-10191. PMID 9254616 DOI: 10.1021/Bi9706374 |
0.48 |
|
| 1997 |
Hengge AC, Zhao Y, Wu L, Zhang ZY. Examination of the transition state of the low-molecular mass small tyrosine phosphatase 1. Comparisons with other protein phosphatases Biochemistry. 36: 7928-7935. PMID 9201938 DOI: 10.1021/Bi970364C |
0.521 |
|
| 1997 |
Hess RA, Hengge AC, Cleland WW. Kinetic isotope effects for acyl transfer from p-nitrophenyl acetate to hydroxylamine show a pH-dependent change in mechanism Journal of the American Chemical Society. 119: 6980-6983. DOI: 10.1021/Ja970648K |
0.6 |
|
| 1997 |
Sowa GA, Hengge AC, Cleland WW. 18O isotope effects support a concerted mechanism for ribonuclease A Journal of the American Chemical Society. 119: 2319-2320. DOI: 10.1021/ja963974t |
0.503 |
|
| 1997 |
Rawlings J, Hengge AC, Cleland WW. Heavy-atom isotope effects on reactions of Co(III)-bound p-nitrophenyl phosphate: Nucleophilic displacements of p-nitrophenol and dissociation of p-nitrophenyl phosphate Journal of the American Chemical Society. 119: 542-549. DOI: 10.1021/Ja962448Z |
0.613 |
|
| 1996 |
Hengge AC, Denu JM, Dixon JE. Transition-state structures for the native dual-specific phosphatase VHR and D92N and S131A mutants. Contributions to the driving force for catalysis. Biochemistry. 35: 7084-92. PMID 8679534 DOI: 10.1021/Bi960255I |
0.611 |
|
| 1996 |
Deal KA, Hengge AC, Burstyn JN. Characterization of transition states in dichloro(1,4,7-triazacyclononane)copper(II)-catalyzed activated phosphate diester hydrolysis Journal of the American Chemical Society. 118: 1713-1718. DOI: 10.1021/Ja952306P |
0.477 |
|
| 1996 |
Hengge AC. Isotope effect studies of the dual-specific phosphatases VHR and STP1 Faseb Journal. 10. |
0.477 |
|
| 1995 |
Cleland WW, Hengge AC. Mechanisms of phosphoryl and acyl transfer. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1585-94. PMID 8529838 DOI: 10.1096/Fasebj.9.15.8529838 |
0.72 |
|
| 1995 |
Hengge AC. Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction Biochemistry. 34: 13982-13987. PMID 7577995 DOI: 10.1021/Bi00043A003 |
0.452 |
|
| 1995 |
Hengge AC, Tobin AE, Cleland WW. Studies of Transition-State Structures in Phosphoryl Transfer Reactions of Phosphodiesters of p-Nitrophenol Journal of the American Chemical Society. 117: 5919-5926. DOI: 10.1021/Ja00127A003 |
0.673 |
|
| 1995 |
Hengge AC, Tobin AE, Cleland WW. Studies of transition-state structures in phosphoryl transfer reactions of phosphodiesters of p-nitrophenol Journal of the American Chemical Society. 117: 5919-5926. |
0.55 |
|
| 1994 |
Hengge AC, Hess RA. Concerted or stepwise mechanisms for acyl transfer reactions of p-nitrophenyl acetate? Transition state structures from isotope effects Journal of the American Chemical Society. 116: 11256-11263. DOI: 10.1021/Ja00104A007 |
0.597 |
|
| 1994 |
Hengge AC, Edens WA, Elsing H. Transition-state structures for phosphoryl-transfer reactions of p-nitrophenyl phosphate Journal of the American Chemical Society. 116: 5045-5049. DOI: 10.1021/Ja00091A003 |
0.489 |
|
| 1992 |
Hengge A. Can acyl transfer occur via a concerted mechanism? Direct evidence from heavy-atom isotope effects Journal of the American Chemical Society. 114: 6575-6576. DOI: 10.1021/Ja00042A057 |
0.354 |
|
| 1992 |
Hengge AC. Oxygen-18 exchange in nitrophenols: significance for labeling and isotope effect experiments Journal of the American Chemical Society. 114: 2747-2748. DOI: 10.1021/Ja00033A075 |
0.381 |
|
| 1991 |
Hengge AC, Cleland WW. Mechanism of phosphodiester cleavage with .beta.-cyclodextrin The Journal of Organic Chemistry. 56: 1972-1974. DOI: 10.1021/Jo00005A064 |
0.479 |
|
| 1991 |
Wilson RM, Hengge AC, Ataei A, Ho DM. Oxidative α coupling of carbonyl compounds via the condensation of acylated triazolinedione ylides with enolates: A facile synthesis of polyacylated olefins Journal of the American Chemical Society. 113: 7240-7249. DOI: 10.1021/Ja00019A023 |
0.312 |
|
| 1991 |
Hengge AC, Cleland WW. Phosphoryl-transfer reactions of phosphodiesters: characterization of transition states by heavy-atom isotope effects Journal of the American Chemical Society. 113: 5835-5841. DOI: 10.1021/Ja00015A043 |
0.716 |
|
| 1991 |
Hengge AC, Cleland WW. Phosphoryl-transfer reactions of phosphodiesters: Characterization of transition states by heavy-atom isotope effects Journal of the American Chemical Society. 113: 5835-5841. |
0.519 |
|
| 1990 |
Wilson RM, Hengge AC, Ataei A, Chantarasiri N. Addition of 4- Phenyltriazolinedione toCarbonyl Compounds: The Formation of alpha-Urazolylcarbonyl Compounds Journal of Organic Chemistry. 55: 193-197. DOI: 10.1021/Jo00288A032 |
0.376 |
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| 1990 |
Hengge AC, Cleland WW. Direct measurement of transition-state bond cleavage in hydrolysis of phosphate esters of p-nitrophenol Journal of the American Chemical Society. 112: 7421-7422. DOI: 10.1021/Ja00176A067 |
0.66 |
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| 1987 |
Wilson RM, Hengge A. Nucleophilic additions to triazolinedione ylides, extremely reactive carbonyl equivalents: a new class of condensation reactions The Journal of Organic Chemistry. 52: 2699-2707. DOI: 10.1021/Jo00389A013 |
0.394 |
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| Low-probability matches (unlikely to be authored by this person) |
| 2021 |
Shen R, Crean RM, Johnson SJ, Kamerlin SCL, Hengge AC. Single Residue on the WPD-Loop Affects the pH Dependency of Catalysis in Protein Tyrosine Phosphatases. Jacs Au. 1: 646-659. PMID 34308419 DOI: 10.1021/jacsau.1c00054 |
0.291 |
|
| 1985 |
Wilson R, Hengge A. The chemistry of an azomethine imine derived from 2,3-dimethylindole and -phenyl triazolinedione. A new and facile condensation method Tetrahedron Letters. 26: 3673-3676. DOI: 10.1016/S0040-4039(00)89220-5 |
0.286 |
|
| 2003 |
Swierczek K, Peters JW, Hengge AC. A convenient synthesis of phosphonothioic acids Tetrahedron. 59: 595-599. DOI: 10.1016/S0040-4020(02)01616-2 |
0.276 |
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| 2022 |
Pinkston J, Shen R, Simons CR, Hengge AC. Competitive measurement of β/α naphthyl phosphate catalytic efficiency by phosphatases utilizing quantitative NMR. Analytical Biochemistry. 651: 114727. PMID 35580735 DOI: 10.1016/j.ab.2022.114727 |
0.268 |
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| 2021 |
Crean RM, Biler M, van der Kamp MW, Hengge AC, Kamerlin SCL. Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases. Journal of the American Chemical Society. PMID 33661624 DOI: 10.1021/jacs.0c11806 |
0.264 |
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| 2022 |
Shen R, Crean RM, Olsen KJ, Corbella M, Calixto AR, Richan T, Brandão TAS, Berry RD, Tolman A, Loria JP, Johnson SJ, Kamerlin SCL, Hengge AC. Insights into the importance of WPD-loop sequence for activity and structure in protein tyrosine phosphatases. Chemical Science. 13: 13524-13540. PMID 36507179 DOI: 10.1039/d2sc04135a |
0.255 |
|
| 1990 |
Wilson RM, Hengge AC. Synthesis and chemistry of acyltriazolinedione ylides and related intermediates: New methods for the preparation of di- and tricarbonyl compounds Journal of Organic Chemistry. 55: 197-202. DOI: 10.1021/Jo00288A033 |
0.239 |
|
| 2021 |
Pinkston J, Jo J, Olsen KJ, Comer D, Glaittli CA, Loria JP, Johnson SJ, Hengge AC. Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality. Biochemistry. PMID 34496202 DOI: 10.1021/acs.biochem.1c00365 |
0.233 |
|
| 1998 |
Hoff RH, Hengge AC. A Facile High-Yield Synthesis and Purification of Tetrabutylammonium Tetrabutylborate. The Journal of Organic Chemistry. 63: 195. PMID 11674064 DOI: 10.1021/Jo971506B |
0.227 |
|
| 1990 |
Wilson RM, Hengge AC, Ataei A, Chantarasiri N. Addition of 4-phenyltriazolinedione to carbonyl compounds: The formation of α-urazolylcarbonyl compounds Journal of Organic Chemistry. 55: 193-197. |
0.198 |
|
| 2006 |
Hengge AC. Secondary Isotope Effects Cheminform. 37. DOI: 10.1002/chin.200644232 |
0.163 |
|
| 2022 |
Crean RM, Biler M, Corbella M, Calixto AR, van der Kamp MW, Hengge AC, Kamerlin SCL. Correction to "Loop Dynamics and Enzyme Catalysis in Protein Tyrosine Phosphatases". Journal of the American Chemical Society. 144: 10091-10093. PMID 35609280 DOI: 10.1021/jacs.2c04624 |
0.157 |
|
| 2010 |
Brandao TAS, Hengge AC. Phosphoryl and sulfuryl transfer Comprehensive Natural Products Ii: Chemistry and Biology. 8: 315-348. |
0.143 |
|
| 2021 |
Hengge AC. Plasmodium falciparum finds the winning combination. The Journal of Biological Chemistry. 296: 100526. PMID 34237898 DOI: 10.1016/j.jbc.2021.100526 |
0.092 |
|
| 1991 |
Hengge AC, Cleland WW. Mechanism of phosphodiester cleavage with β-cyclodextrin Journal of Organic Chemistry. 56: 1972-1974. |
0.08 |
|
| Hide low-probability matches. |