| Year |
Citation |
Score |
| 2009 |
Fan C, Fromm HJ, Bobik TA. Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica. The Journal of Biological Chemistry. 284: 20240-8. PMID 19509296 DOI: 10.1074/Jbc.M109.027425 |
0.493 |
|
| 2007 |
Hines JK, Chen X, Nix JC, Fromm HJ, Honzatko RB. Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition. The Journal of Biological Chemistry. 282: 36121-31. PMID 17933867 DOI: 10.1074/Jbc.M707302200 |
0.38 |
|
| 2007 |
Hines JK, Kruesel CE, Fromm HJ, Honzatko RB. Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch. The Journal of Biological Chemistry. 282: 24697-706. PMID 17567577 DOI: 10.1074/Jbc.M703580200 |
0.429 |
|
| 2007 |
Hines JK, Fromm HJ, Honzatko RB. Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state. The Journal of Biological Chemistry. 282: 11696-704. PMID 17314096 DOI: 10.1074/Jbc.M611104200 |
0.465 |
|
| 2006 |
Iancu CV, Zhou Y, Borza T, Fromm HJ, Honzatko RB. Cavitation as a mechanism of substrate discrimination by adenylosuccinate synthetases. Biochemistry. 45: 11703-11. PMID 16981730 DOI: 10.1021/Bi0607498 |
0.389 |
|
| 2006 |
Ginder ND, Binkowski DJ, Fromm HJ, Honzatko RB. Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase. The Journal of Biological Chemistry. 281: 20680-8. PMID 16687397 DOI: 10.1074/Jbc.M602109200 |
0.465 |
|
| 2006 |
Hines JK, Fromm HJ, Honzatko RB. Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 281: 18386-93. PMID 16670087 DOI: 10.1074/Jbc.M602553200 |
0.511 |
|
| 2005 |
Skaff DA, Kim CS, Tsai HJ, Honzatko RB, Fromm HJ. Glucose 6-phosphate release of wild-type and mutant human brain hexokinases from mitochondria. The Journal of Biological Chemistry. 280: 38403-9. PMID 16166083 DOI: 10.1074/Jbc.M506943200 |
0.382 |
|
| 2005 |
Iancu CV, Mukund S, Fromm HJ, Honzatko RB. R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 280: 19737-45. PMID 15767255 DOI: 10.1074/Jbc.M501011200 |
0.456 |
|
| 2005 |
Nelson SW, Binkowski DJ, Honzatko RB, Fromm HJ. Mechanism of action of Escherichia coli phosphoribosylaminoimidazolesuccinocarboxamide synthetase. Biochemistry. 44: 766-74. PMID 15641804 DOI: 10.1021/Bi048191W |
0.634 |
|
| 2004 |
Nelson SW, Honzatko RB, Fromm HJ. Origin of cooperativity in the activation of fructose-1,6-bisphosphatase by Mg2+. The Journal of Biological Chemistry. 279: 18481-7. PMID 14978036 DOI: 10.1074/Jbc.M308811200 |
0.613 |
|
| 2003 |
Choe JY, Nelson SW, Arienti KL, Axe FU, Collins TL, Jones TK, Kimmich RD, Newman MJ, Norvell K, Ripka WC, Romano SJ, Short KM, Slee DH, Fromm HJ, Honzatko RB. Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors. The Journal of Biological Chemistry. 278: 51176-83. PMID 14530289 DOI: 10.1074/Jbc.M308396200 |
0.613 |
|
| 2003 |
Choe JY, Nelson SW, Fromm HJ, Honzatko RB. Interaction of Tl+ with product complexes of fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 278: 16008-14. PMID 12595529 DOI: 10.1074/Jbc.M212394200 |
0.583 |
|
| 2003 |
Choe JY, Iancu CV, Fromm HJ, Honzatko RB. Metaphosphate in the active site of fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 278: 16015-20. PMID 12595528 DOI: 10.1074/Jbc.M212395200 |
0.447 |
|
| 2003 |
Borza T, Iancu CV, Pike E, Honzatko RB, Fromm HJ. Variations in the response of mouse isozymes of adenylosuccinate synthetase to inhibitors of physiological relevance. The Journal of Biological Chemistry. 278: 6673-9. PMID 12482871 DOI: 10.1074/Jbc.M210838200 |
0.437 |
|
| 2002 |
Iancu CV, Borza T, Fromm HJ, Honzatko RB. Feedback inhibition and product complexes of recombinant mouse muscle adenylosuccinate synthetase. The Journal of Biological Chemistry. 277: 40536-43. PMID 12186864 DOI: 10.1074/Jbc.M204952200 |
0.428 |
|
| 2002 |
Iancu CV, Borza T, Fromm HJ, Honzatko RB. IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase. The Journal of Biological Chemistry. 277: 26779-87. PMID 12004071 DOI: 10.1074/Jbc.M203730200 |
0.464 |
|
| 2002 |
Nelson SW, Honzatko RB, Fromm HJ. Hybrid tetramers of porcine liver fructose-1,6-bisphosphatase reveal multiple pathways of allosteric inhibition. The Journal of Biological Chemistry. 277: 15539-45. PMID 11854289 DOI: 10.1074/Jbc.M112304200 |
0.574 |
|
| 2002 |
Gorrell A, Wang W, Underbakke E, Hou Z, Honzatko RB, Fromm HJ. Determinants of L-aspartate and IMP recognition in Escherichia coli adenylosuccinate synthetase. The Journal of Biological Chemistry. 277: 8817-21. PMID 11781326 DOI: 10.1074/Jbc.M111810200 |
0.766 |
|
| 2002 |
Hou Z, Wang W, Fromm HJ, Honzatko RB. IMP Alone Organizes the Active Site of Adenylosuccinate Synthetase from Escherichia coli. The Journal of Biological Chemistry. 277: 5970-6. PMID 11741996 DOI: 10.1074/Jbc.M109561200 |
0.472 |
|
| 2001 |
Wen J, Nelson SW, Honzatko RB, Fromm HJ, Petrich JW. Environment of tryptophan 57 in porcine fructose-1,6-bisphosphatase studied by time-resolved fluorescence and site-directed mutagenesis. Photochemistry and Photobiology. 74: 679-85. PMID 11723795 DOI: 10.1562/0031-8655(2001)074<0679:Eotipf>2.0.Co;2 |
0.528 |
|
| 2001 |
Iancu CV, Borza T, Choe JY, Fromm HJ, Honzatko RB. Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure. The Journal of Biological Chemistry. 276: 42146-52. PMID 11560929 DOI: 10.1074/Jbc.M106294200 |
0.487 |
|
| 2001 |
Nelson SW, Honzatko RB, Fromm HJ. Spontaneous subunit exchange in porcine liver fructose-1,6-bisphosphatase Febs Letters. 492: 254-258. PMID 11257504 DOI: 10.1016/S0014-5793(01)02262-1 |
0.571 |
|
| 2001 |
Nelson SW, Kurbanov FT, Honzatko RB, Fromm HJ. The N-terminal Segment of Recombinant Porcine Fructose-1,6-bisphosphatase Participates in the Allosteric Regulation of Catalysis Journal of Biological Chemistry. 276: 6119-6124. PMID 11096109 DOI: 10.1074/Jbc.M009485200 |
0.638 |
|
| 2000 |
Nelson SW, Iancu CV, Choe JY, Honzatko RB, Fromm HJ. Tryptophan fluorescence reveals the conformational state of a dynamic loop in recombinant porcine fructose-1,6-bisphosphatase. Biochemistry. 39: 11100-6. PMID 10998248 DOI: 10.1021/Bi000609C |
0.536 |
|
| 2000 |
Choe JY, Fromm HJ, Honzatko RB. Crystal structures of fructose 1,6-bisphosphatase: Mechanism of catalysis and allosteric inhibition revealed in product complexes Biochemistry. 39: 8565-8574. PMID 10913263 DOI: 10.1021/Bi000574G |
0.416 |
|
| 2000 |
Nelson SW, Choe JY, Honzatko RB, Fromm HJ. Mutations in the hinge of a dynamic loop broadly influence functional properties of fructose-1,6-bisphosphatase Journal of Biological Chemistry. 275: 29986-29992. PMID 10896931 DOI: 10.1074/Jbc.M000473200 |
0.577 |
|
| 2000 |
Aleshin AE, Kirby C, Liu X, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB. Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes revelant to allosteric regulation Journal of Molecular Biology. 296: 1001-1015. PMID 10686099 DOI: 10.1006/Jmbi.1999.3494 |
0.438 |
|
| 1999 |
Lee P, Gorrell A, Fromm HJ, Colman RF. 8-(4-Bromo-2,3-dioxobutylthio)guanosine 5'-triphosphate: a new affinity label for purine nucleotide sites in proteins. Archives of Biochemistry and Biophysics. 372: 205-13. PMID 10562435 DOI: 10.1006/Abbi.1999.1488 |
0.807 |
|
| 1999 |
Fromm SJ, Fromm HJ. A two-step computer-assisted method for deriving steady-state rate equations Biochemical and Biophysical Research Communications. 265: 448-452. PMID 10558887 DOI: 10.1006/Bbrc.1999.1679 |
0.381 |
|
| 1999 |
Liu X, Kim CS, Kurbanov FT, Honzatko RB, Fromm HJ. Dual mechanisms for glucose 6-phosphate inhibition of human brain hexokinase Journal of Biological Chemistry. 274: 31155-31159. PMID 10531306 DOI: 10.1074/Jbc.274.44.31155 |
0.438 |
|
| 1999 |
Honzatko RB, Fromm HJ. Structure-function studies of adenylosuccinate synthetase from Escherichia coli Archives of Biochemistry and Biophysics. 370: 1-8. PMID 10496970 DOI: 10.1006/Abbi.1999.1383 |
0.509 |
|
| 1999 |
Aleshin AE, Malfois M, Liu X, Kim CS, Fromm HJ, Honzatko RB, Koch MHJ, Svergun DI. Nonaggregating mutant of recombinant human hexokinase I exhibits wild- type kinetics and rod-like conformations in solution Biochemistry. 38: 8359-8366. PMID 10387081 DOI: 10.1021/Bi990523N |
0.391 |
|
| 1999 |
Hou Z, Cashel M, Fromm HJ, Honzatko RB. Effectors of the stringent response target the active site of Escherichia coli adenylosuccinate synthetase Journal of Biological Chemistry. 274: 17505-17510. PMID 10364182 DOI: 10.1074/jbc.274.25.17505 |
0.303 |
|
| 1999 |
Choe JY, Poland BW, Fromm HJ, Honzatko RB. Mechanistic implications from crystalline complexes of wild-type and mutant adenylosuccinate synthetases from Escherichia coli Biochemistry. 38: 6953-6961. PMID 10346917 DOI: 10.1021/Bi990159S |
0.453 |
|
| 1999 |
Lee P, Gorrell A, Fromm HJ, Colman RF. Implication of arginine-131 and arginine-303 in the substrate site of adenylosuccinate synthetase of Escherichia coli by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5'-monophosphate. Biochemistry. 38: 5754-63. PMID 10231526 DOI: 10.1021/Bi982779J |
0.812 |
|
| 1999 |
Honzatko RB, Stayton MM, Fromm HJ. Adenylosuccinate synthetase: recent developments. Advances in Enzymology and Related Areas of Molecular Biology. 73: 57-102, ix-x. PMID 10218106 |
0.408 |
|
| 1999 |
Honzatko RB, Stayton MM, Fromm HJ. Adenylosuccinate synthetase: Recent developments Advances in Enzymology and Related Areas of Molecular Biology. 73: 57-102. DOI: 10.1002/9780470123195.Ch3 |
0.408 |
|
| 1998 |
Aleshin AE, Fromm HJ, Honzatko RB. Multiple crystal forms of hexokinase I: New insights regarding conformational dynamics, subunit interactions, and membrane association Febs Letters. 434: 42-46. PMID 9738448 DOI: 10.1016/S0014-5793(98)00952-1 |
0.314 |
|
| 1998 |
Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB. Regulation of hexokinase I: Crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate Journal of Molecular Biology. 282: 345-357. PMID 9735292 DOI: 10.1006/Jmbi.1998.2017 |
0.421 |
|
| 1998 |
Choe JY, Poland BW, Fromm HJ, Honzatko RB. Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase Biochemistry. 37: 11441-11450. PMID 9708979 DOI: 10.1021/Bi981112U |
0.456 |
|
| 1998 |
Fang TY, Alechina O, Aleshin AE, Fromm HJ, Honzatko RB. Identification of a phosphate regulatory site and a low affinity binding site for glucose 6-phosphate in the N-terminal half of human brain hexokinase Journal of Biological Chemistry. 273: 19548-19553. PMID 9677378 DOI: 10.1074/Jbc.273.31.19548 |
0.489 |
|
| 1998 |
Kurbanov FT, Choe JY, Honzatko RB, Fromm HJ. Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition Journal of Biological Chemistry. 273: 17511-17516. PMID 9651342 DOI: 10.1074/Jbc.273.28.17511 |
0.528 |
|
| 1998 |
Wang W, Gorrell A, Hou Z, Honzatko RB, Fromm HJ. Ambiguities in mapping the active site of a conformationally dynamic enzyme by directed mutation. Role of dynamics in structure-function correlations in Escherichia coli adenylosuccinate synthetase. The Journal of Biological Chemistry. 273: 16000-4. PMID 9632649 DOI: 10.1074/Jbc.273.26.16000 |
0.806 |
|
| 1998 |
Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB. The mechanism of regulation of hexokinase: New insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate Structure. 6: 39-50. PMID 9493266 DOI: 10.1016/S0969-2126(98)00006-9 |
0.337 |
|
| 1998 |
Zeng C, Aleshin AE, Chen G, Honzatko RB, Fromm HJ. The roles of glycine residues in the ATP binding site of human brain hexokinase Journal of Biological Chemistry. 273: 700-704. PMID 9422720 DOI: 10.1074/Jbc.273.2.700 |
0.528 |
|
| 1998 |
Shyur LF, Honzatko RB, Fromm HJ, Traut T. Major changes in the kinetic mechanism of AMP inhibition and AMP cooperativity attend the mutation of Arg49 in Fructose-1,6-bisphosphatase Chemtracts. 11: 762-764. DOI: 10.1074/Jbc.272.42.26295 |
0.542 |
|
| 1998 |
Liu XF, Aleshin AE, Fang TY, Honzatko RB, Fromm HJ. The ATP and glucose-6-P binding sites in human brain hexokinase Faseb Journal. 12: A1445. |
0.337 |
|
| 1997 |
Wang W, Hou Z, Honzatko RB, Fromm HJ. Relationship of conserved residues in the IMP binding site to substrate recognition and catalysis in Escherichia coli adenylosuccinate synthetase Journal of Biological Chemistry. 272: 16911-16916. PMID 9202000 DOI: 10.1074/Jbc.272.27.16911 |
0.522 |
|
| 1997 |
Poland BW, Bruns C, Fromm HJ, Honzatko RB. Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli Journal of Biological Chemistry. 272: 15200-15205. PMID 9182542 DOI: 10.1074/Jbc.272.24.15200 |
0.439 |
|
| 1997 |
Kang C, Sun N, Poland BW, Gorrell A, Honzatko RB, Fromm HJ. Residues essential for catalysis and stability of the active site of Escherichia coli adenylosuccinate synthetase as revealed by directed mutation and kinetics. The Journal of Biological Chemistry. 272: 11881-5. PMID 9115248 DOI: 10.1074/Jbc.272.18.11881 |
0.801 |
|
| 1997 |
Wang W, Gorrell A, Honzatko RB, Fromm HJ. A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer. The Journal of Biological Chemistry. 272: 7078-84. PMID 9054400 DOI: 10.1074/Jbc.272.11.7078 |
0.811 |
|
| 1997 |
Gorrell A, Wang W, Fromm HJ. Modification of adenylosuccinate synthetase purine nucleotide triphosphate binding site Faseb Journal. 11: A1303. |
0.756 |
|
| 1996 |
Poland BW, Fromm HJ, Honzatko RB. Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with GDP, IMP hadacidin, NO3 -, and Mg2+ Journal of Molecular Biology. 264: 1013-1027. PMID 9000627 DOI: 10.1006/Jmbi.1996.0693 |
0.405 |
|
| 1996 |
Shyur LF, Aleshin AE, Honzatko RB, Fromm HJ. Biochemical properties of mutant and wild-type fructose-1,6-bisphosphatases are consistent with the coupling of intra- and intersubunit conformational changes in the T- and R-state transition Journal of Biological Chemistry. 271: 33301-33307. PMID 8969189 DOI: 10.1074/Jbc.271.52.33301 |
0.504 |
|
| 1996 |
Poland BW, Lee SF, Subramanian MV, Siehl DL, Anderson RJ, Fromm HJ, Honzatko RB. Refined crystal structure of adenylosuccinate synthetase from Escherichia coli complexed with hydantocidin 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin. Biochemistry. 35: 15753-9. PMID 8961938 DOI: 10.2210/Pdb1Juy/Pdb |
0.355 |
|
| 1996 |
Kang C, Kim S, Fromm HJ. Subunit complementation of Escherichia coli adenylosuccinate synthetase Journal of Biological Chemistry. 271: 29722-29728. PMID 8939906 DOI: 10.1074/Jbc.271.47.29722 |
0.485 |
|
| 1996 |
Zeng C, Aleshin AE, Hardie JB, Harrison RW, Fromm HJ. ATP-binding site of human brain hexokinase as studied by molecular modeling and site-directed mutagenesis. Biochemistry. 35: 13157-64. PMID 8855953 DOI: 10.1021/Bi960750E |
0.517 |
|
| 1996 |
Fonné-Pfister R, Chemla P, Ward E, Girardet M, Kreuz KE, Honzatko RB, Fromm HJ, Schär HP, Grutter MG, Cowan-Jacob SW. The mode of action and the structure of a herbicide in complex with its target: Binding of activated hydantocidin to the feedback regulation site of adenylosuccinate synthetase Proceedings of the National Academy of Sciences of the United States of America. 93: 9431-9436. PMID 8790347 DOI: 10.1073/pnas.93.18.9431 |
0.354 |
|
| 1996 |
Moe OA, Baker-Malcolm JF, Wang W, Kang C, Fromm HJ, Colman RF. Involvement of arginine 143 in nucleotide substrate binding at the active site of adenylosuccinate synthetase from Escherichia coli. Biochemistry. 35: 9024-33. PMID 8703905 DOI: 10.1021/Bi960426J |
0.524 |
|
| 1996 |
Poland BW, Hou Z, Bruns C, Fromm HJ, Honzatko RB. Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli Journal of Biological Chemistry. 271: 15407-15413. PMID 8663109 DOI: 10.1074/Jbc.271.26.15407 |
0.394 |
|
| 1996 |
Shyur LF, Aleshin AE, Fromm HJ. A study of subunit interface residues of fructose-1,6-bisphosphatase by site-directed mutagenesis: Effects on AMP and Mg2+ affinities Biochemistry. 35: 7492-7498. PMID 8652527 DOI: 10.1021/Bi960367+ |
0.521 |
|
| 1996 |
Shyur LF, Aleshin AE, Honzatko RB, Fromm HJ. Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase Journal of Biological Chemistry. 271: 3005-3010. PMID 8621693 DOI: 10.1074/Jbc.271.6.3005 |
0.515 |
|
| 1996 |
Zhang R, Villeret V, Lipscomb WN, Fromm HJ. Kinetics and mechanisms of activation and inhibition of porcine liver fructose-1,6-bisphosphatase by monovalent cations. Biochemistry. 35: 3038-43. PMID 8608143 DOI: 10.1021/Bi952188I |
0.474 |
|
| 1996 |
Wang W, Fromm HJ. Adenylosuccinate synthetase from Eschericliia coli functions as a dimer Faseb Journal. 10: A1384. |
0.453 |
|
| 1995 |
Zhang R, Chen L, Villeret V, Fromm HJ. Glycine 122 is essential for cooperativity and binding of Mg2+ to porcine fructose-1,6-bisphosphatase Journal of Biological Chemistry. 270: 54-58. PMID 7814419 DOI: 10.1074/Jbc.270.1.54 |
0.548 |
|
| 1995 |
Kang C, Fromm HJ. Identification of an essential second metal ion in the reaction mechanism of Escherichia coli adenylosuccinate synthetase Journal of Biological Chemistry. 270: 15539-15544. PMID 7797548 DOI: 10.1074/Jbc.270.26.15539 |
0.415 |
|
| 1995 |
Zhang R, Fromm HJ. Mutation of arginine 276 to methionine changes Mg2+ cooperativity and the kinetic mechanism of fructose-1,6-bisphosphatase Biochemistry. 34: 8190-8195. PMID 7794933 DOI: 10.1021/Bi00025A026 |
0.548 |
|
| 1995 |
Fromm HJ. Reversible enzyme inhibitors as mechanistic probes Methods in Enzymology. 249: 123-143. PMID 7791609 DOI: 10.1016/0076-6879(95)49033-7 |
0.478 |
|
| 1995 |
Shyur LF, Zhang R, Fromm HJ. Site-directed mutagenesis of the substrate binding site of porcine fructose-1,6-bisphosphatase Archives of Biochemistry and Biophysics. 319: 123-127. PMID 7771775 DOI: 10.1006/Abbi.1995.1273 |
0.563 |
|
| 1995 |
Wang W, Poland BW, Honzatko RB, Fromm HJ. Identification of arginine residues in the putative L-aspartate binding site of Escherichia coil adenylosuccinate synthetase Journal of Biological Chemistry. 270: 13160-13163. PMID 7768911 DOI: 10.1074/Jbc.270.22.13160 |
0.539 |
|
| 1995 |
Zeng C, Fromm HJ. Active site residues of human brain hexokinase as studied by site-specific mutagenesis Journal of Biological Chemistry. 270: 10509-10513. PMID 7737985 DOI: 10.1074/Jbc.270.18.10509 |
0.473 |
|
| 1995 |
Villeret V, Huang S, Fromm HJ, Lipscomb WN. Crystallographic evidence for the action of potassium, thallium, and lithium ions on fructose-1,6-bisphosphatase. Proceedings of the National Academy of Sciences of the United States of America. 92: 8916-20. PMID 7568043 DOI: 10.1073/Pnas.92.19.8916 |
0.366 |
|
| 1995 |
Silva MM, Poland BW, Hoffman CR, Fromm HJ, Honzatko RB. Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli. Journal of Molecular Biology. 254: 431-46. PMID 7490761 DOI: 10.1006/Jmbi.1995.0629 |
0.376 |
|
| 1994 |
Kang C, Fromm HJ. Characterization of the putative GTP-binding site residues of Escherichia coli adenylosuccinate synthetase by site-directed mutagenesis Archives of Biochemistry and Biophysics. 310: 475-480. PMID 8179335 DOI: 10.1006/Abbi.1994.1195 |
0.52 |
|
| 1994 |
Kang C, Sun N, Honzatko RB, Fromm HJ. Replacement of Asp333 with Asn by Site-directed Mutagenesis Changes the Substrate Specificity of Escherichia coli Adenylosuccinate Synthetase from Guanosine 5′-Triphosphate to Xanthosine 5′-Triphosphate Journal of Biological Chemistry. 269: 24046-24049. PMID 7929056 |
0.431 |
|
| 1994 |
Chen M, Chen L, Fromm HJ. Replacement of glutamic acid 29 with glutamine leads to a loss of cooperativity for AMP with porcine fructose-1,6-bisphosphatase Journal of Biological Chemistry. 269: 5554-5558. PMID 7907084 |
0.572 |
|
| 1993 |
Burton VA, Chen M, Ong WC, Ling T, Fromm HJ, Stayton MM. High-level expression of porcine fructose-1,6-bisphosphatase in Escherichia coli: purification and characterization of the enzyme. Biochemical and Biophysical Research Communications. 192: 511-7. PMID 8387281 DOI: 10.1006/Bbrc.1993.1445 |
0.519 |
|
| 1993 |
Chen LR, Hegde R, Chen M, Fromm HJ. Site-Specific Mutagenesis of the Metal Binding Sites of Porcine Fructose-1,6-Bisphosphatase Archives of Biochemistry and Biophysics. 307: 350-354. PMID 8274021 DOI: 10.1006/Abbi.1993.1599 |
0.56 |
|
| 1992 |
Liu F, Dong Q, Fromm HJ. Site-directed mutagenesis of the phosphate-binding consensus sequence in Escherichia coli adenylosuccinate synthetase Journal of Biological Chemistry. 267: 2388-2392. PMID 1733940 |
0.411 |
|
| 1991 |
Dong Q, Liu F, Myers AM, Fromm HJ. Evidence for an arginine residue at the substrate binding site of Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis. The Journal of Biological Chemistry. 266: 12228-33. PMID 2061308 |
0.482 |
|
| 1991 |
Liu F, Dong Q, Myers AM, Fromm HJ. Expression of human brain hexokinase in Escherichia coli: purification and characterization of the expressed enzyme. Biochemical and Biophysical Research Communications. 177: 305-11. PMID 2043117 DOI: 10.1016/0006-291X(91)91983-J |
0.372 |
|
| 1991 |
Soans C, Fromm HJ. Studies of ligand binding to Escherichia coli adenylosuccinate synthetase Archives of Biochemistry and Biophysics. 291: 107-112. PMID 1929424 DOI: 10.1016/0003-9861(91)90111-U |
0.486 |
|
| 1990 |
Dong Q, Soans C, Liu F, Fromm HJ. Identification of different classes of nonessential sulfhydryl groups in Escherichia coli adenylosuccinate synthetase Archives of Biochemistry and Biophysics. 276: 77-84. PMID 2153366 DOI: 10.1016/0003-9861(90)90012-N |
0.52 |
|
| 1990 |
Dong Q, Fromm HJ. Chemical modification of adenylosuccinate synthetase from Escherichia coli by pyridoxal 5′-phosphate: Identification of an active site lysyl residue Journal of Biological Chemistry. 265: 6235-6240. PMID 2108156 |
0.453 |
|
| 1989 |
Liu F, Fromm HJ. Investigation of the relationship between tyrosyl residues and the adenosine 5'-monophosphate binding site of rabbit liver fructose-1,6-bisphosphatase as studied by chemical modification and nuclear magnetic resonance spectroscopy Journal of Biological Chemistry. 264: 18320-18325. PMID 2553704 |
0.346 |
|
| 1989 |
Liu F, Roy M, Fromm HJ. The site of substrate and fructose 2,6-bisphosphate binding to rabbit liver fructose-1,6-bisphosphatase Biochemical and Biophysical Research Communications. 161: 689-695. PMID 2544170 DOI: 10.1016/0006-291X(89)92654-5 |
0.379 |
|
| 1988 |
Serra MA, Bass MB, Fromm HJ, Honzatko RB. Preliminary X-ray crystallographic study of adenylosuccinate synthetase from Escherichia coli Journal of Molecular Biology. 200: 753-754. PMID 3045328 DOI: 10.1016/0022-2836(88)90489-5 |
0.352 |
|
| 1988 |
Liu F, Fromm HJ. Relationship between thiol group modification and the binding site for fructose 2,6-bisphosphate on rabbit liver fructose-1,6-bisphosphatase Journal of Biological Chemistry. 263: 10035-10039. PMID 2838468 |
0.456 |
|
| 1988 |
Liu F, Fromm HJ. Interaction of fructose 2,6-bisphosphate and AMP with fructose-1,6-bisphosphatase as studied by nuclear magnetic resonance spectroscopy Journal of Biological Chemistry. 263: 9122-9128. PMID 2837477 |
0.306 |
|
| 1988 |
Liu F, Fromm HJ. Purification and characterization of fructose-1,6-bisphosphatase from bovine brain Archives of Biochemistry and Biophysics. 260: 609-615. PMID 2829736 DOI: 10.1016/0003-9861(88)90488-2 |
0.422 |
|
| 1987 |
Bass MB, Fromm HJ. Is rat skeletal muscle hexokinase an allosteric enzyme? Archives of Biochemistry and Biophysics. 256: 708-711. PMID 3619453 DOI: 10.1016/0003-9861(87)90629-1 |
0.349 |
|
| 1987 |
Bass MB, Fromm HJ, Stayton MM. Overproduction, purification, and characterization of adenylosuccinate synthetase from Escherichia coli. Archives of Biochemistry and Biophysics. 256: 335-42. PMID 3038024 DOI: 10.1016/0003-9861(87)90454-1 |
0.449 |
|
| 1986 |
Cooper BF, Fromm HJ, Rudolph FB. Isotope exchange at equilibrium studies with rat muscle adenylosuccinate synthetase. Biochemistry. 25: 7323-7. PMID 3542024 DOI: 10.1021/Bi00371A013 |
0.637 |
|
| 1986 |
Scheffler JE, Fromm HJ. Regulation of rabbit liver fructose-1,6-bisphosphatase by metals, nucleotides, and fructose 2,6-bisphosphate as determined from fluorescence studies Biochemistry. 25: 6659-6665. PMID 3024716 DOI: 10.1021/Bi00369A050 |
0.431 |
|
| 1985 |
Bass MB, Fromm HJ. trans-1,2-diaminocyclohexane-N,N,N′,N′-tetraacetic acid is superior to ethylenediamine-N,N,N′,N′-tetraacetic acid for sequestering Mg2+ in 31P NMR experiments involving ATP spectra at neutral and acidic pH Analytical Biochemistry. 145: 292-301. PMID 3925810 DOI: 10.1016/0003-2697(85)90364-1 |
0.314 |
|
| 1984 |
Bass MB, Fromm HJ, Rudolph FB. The mechanism of the adenylosuccinate synthetase reaction as studied by positional isotope exchange Journal of Biological Chemistry. 259: 12330-12333. PMID 6490614 |
0.587 |
|
| 1984 |
Ganson NJ, Fromm HJ. Mechanism and regulation of bovine liver fructose-1,6-bisphosphatase. Current Topics in Cellular Regulation. 24: 197-207. PMID 6094107 DOI: 10.1016/B978-0-12-152824-9.50026-5 |
0.434 |
|
| 1983 |
Solheim LP, Fromm HJ. Effect of inorganic phosphate on the reverse reaction of bovine brain hexokinase Biochemistry. 22: 2234-2239. PMID 6860661 DOI: 10.1021/Bi00278A027 |
0.408 |
|
| 1983 |
Stayton MM, Rudolph FB, Fromm HJ. Regulation, genetics, and properties of adenylosuccinate synthetase: a review. Current Topics in Cellular Regulation. 22: 103-41. PMID 6347525 DOI: 10.1016/B978-0-12-152822-5.50008-7 |
0.652 |
|
| 1982 |
Ganson NJ, Fromm HJ. The effect of fructose 2,6-bisphosphate on the reverse reaction kinetics of fructose 1,6-bisphosphatase from bovine liver. Biochemical and Biophysical Research Communications. 108: 233-9. PMID 6293482 DOI: 10.1016/0006-291X(82)91856-3 |
0.36 |
|
| 1981 |
Solheim LP, Fromm HJ. Kinetic evidence that the high-affinity glucose 6-phosphate site on hexokinase I Is the active site Archives of Biochemistry and Biophysics. 211: 92-99. PMID 7305385 DOI: 10.1016/0003-9861(81)90433-1 |
0.402 |
|
| 1981 |
Shone CC, Fromm HJ. Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli Biochemistry. 20: 7494-7501. PMID 7034777 DOI: 10.1021/Bi00529A026 |
0.531 |
|
| 1980 |
Solheim LP, Fromm HJ. pH kinetic studies of bovine brain hexokinase Biochemistry. 19: 6074-6080. PMID 7470451 DOI: 10.1021/Bi00567A020 |
0.404 |
|
| 1980 |
Stone SR, Fromm HJ. Studies on the mechanism of adenosine 5'-monophosphate inhibition of bovine liver fructose 1,6-bisphosphatase. Biochemistry. 19: 620-625. PMID 6243953 DOI: 10.1021/Bi00545A003 |
0.44 |
|
| 1980 |
Shone CC, Fromm HJ. Initial rate and inhibition studies on pig brain hexokinase Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 67: 697-699. DOI: 10.1016/0305-0491(80)90434-4 |
0.312 |
|
| 1979 |
Rudolph FB, Fromm HJ. Plotting methods for analyzing enzyme rate data. Methods in Enzymology. 63: 138-59. PMID 502858 DOI: 10.1016/0076-6879(79)63009-4 |
0.636 |
|
| 1979 |
Casazza JP, Stone SR, Fromm HJ. Kinetic studies of bovine liver fructose-1,6-bisphosphatase Journal of Biological Chemistry. 254: 4661-4665. PMID 220258 |
0.362 |
|
| 1979 |
Fromm HJ. [18] Use of competitive inhibitors to study substrate binding order Methods in Enzymology. 63: 467-486. DOI: 10.1016/0076-6879(79)63020-3 |
0.359 |
|
| 1979 |
Rudolph FB, Fromm HJ. [7] Plotting methods for analyzing enzyme rate data Methods in Enzymology. 63: 138-159. DOI: 10.1016/0076-6879(79)63009-4 |
0.601 |
|
| 1978 |
Balinsky D, Fromm HJ. Hexokinase III from Rana catesbeiana Comparative Biochemistry and Physiology -- Part B: Biochemistry And. 60: 71-75. PMID 318544 DOI: 10.1016/0305-0491(78)90030-5 |
0.313 |
|
| 1977 |
Casazza JP, Fromm HJ. Purification and initial rate kinetics of acyl-phosphate-hexose phosphotransferase from Aerobacter aerogenes Biochemistry. 16: 3091-3097. PMID 196625 DOI: 10.1021/Bi00633A008 |
0.54 |
|
| 1976 |
Casazza JP, Fromm HJ. Studies on the mode of sugar-phosphate product inhibition of brain hexokinase Archives of Biochemistry and Biophysics. 177: 480-487. PMID 1015830 DOI: 10.1016/0003-9861(76)90459-8 |
0.34 |
|
| 1975 |
Siano DB, Zyskind JW, Fromm HJ. A computer program for fitting and statistically analyzing initial rate data applied to bovine hexokinase type III isozyme Archives of Biochemistry and Biophysics. 170: 587-600. PMID 1190781 DOI: 10.1016/0003-9861(75)90154-X |
0.373 |
|
| 1975 |
Ellison WR, Lueck JD, Fromm HJ. Studies on the mechanism of orthophosphate regulation of bovine brain hexokinase. The Journal of Biological Chemistry. 250: 1864-71. PMID 1112835 |
0.327 |
|
| 1974 |
Ellison WR, Lueck JD, Fromm HJ. Studies on the kinetics and mechanism of orthophosphate activation of bovine brain hexokinase. Biochemical and Biophysical Research Communications. 57: 1214-20. PMID 4857460 DOI: 10.1016/0006-291X(74)90826-2 |
0.428 |
|
| 1973 |
Rudolph FB, Fromm HJ. Kinetics of three substrate enzyme systems. Treatment of partially random mechanisms using equilibrium assumptions Journal of Theoretical Biology. 39: 363-371. PMID 4728723 DOI: 10.1016/0022-5193(73)90105-7 |
0.662 |
|
| 1973 |
Lueck JD, Fromm HJ. Analysis of exchange rates for the Ping Pong Bi Bi mechanism and the concept of substrate synergism. Febs Letters. 32: 184-6. PMID 4715683 DOI: 10.1016/0014-5793(73)80767-7 |
0.351 |
|
| 1973 |
Lueck JD, Ellison WR, Fromm HJ. The point of convergence of sequential double reciprocal plots as a criterion of bireactant enzyme kinetic mechanisms. Evaluation of the yeast hexokinase reaction. Febs Letters. 30: 321-4. PMID 4700752 DOI: 10.1016/0014-5793(73)80679-9 |
0.442 |
|
| 1973 |
Purich DL, Fromm HJ, Rudolph FB. The hexokinases: kinetic, physical, and regulatory properties Advances in Enzymology and Related Areas of Molecular Biology. 39: 249-326. PMID 4583639 DOI: 10.1002/9780470122846.Ch4 |
0.548 |
|
| 1972 |
Purich DL, Fromm HJ. Inhibition of rabbit skeletal muscle adenylate kinase by the transition state analogue, P1,P4-di(adenosine-5′)tetraphosphate Bba - Enzymology. 276: 563-567. PMID 5068828 DOI: 10.1016/0005-2744(72)91021-2 |
0.356 |
|
| 1972 |
Purich DL, Fromm HJ. Application of equilibrium exchange kinetics to studies of kinetic properties at high enzyme concentrations: Experiments with yeast hexokinase P-II Biochemical and Biophysical Research Communications. 47: 916-922. PMID 5026301 DOI: 10.1016/0006-291X(72)90580-3 |
0.475 |
|
| 1972 |
Purich DL, Fromm HJ. Activation of brain hexokinase by magnesium ions and by magnesium ion--adenosine triphosphate complex Biochemical Journal. 130: 63-69. PMID 4655453 DOI: 10.1042/Bj1300063 |
0.45 |
|
| 1972 |
Purich DL, Fromm HJ. Limitations in the use of dixon plots to evaluate enzyme inhibition Bba - Enzymology. 268: 1-3. PMID 4622931 DOI: 10.1016/0005-2744(72)90189-1 |
0.476 |
|
| 1972 |
Purich DL, Fromm HJ. Evaluation of the phosphoryl-enzyme intermediate concept in the acetate kinase and hexokinase reactions from kinetic studies Archives of Biochemistry and Biophysics. 149: 307-315. PMID 4552801 DOI: 10.1016/0003-9861(72)90326-8 |
0.457 |
|
| 1972 |
Purich DL, Fromm HJ. A Possible Role for Kinetic Reaction Mechanism Dependent Substrate and Product Effects in Enzyme Regulation Current Topics in Cellular Regulation. 6: 131-167. DOI: 10.1016/B978-0-12-152806-5.50011-4 |
0.528 |
|
| 1971 |
Rudolph FB, Fromm HJ. Use of isotope competition and alternative substrates for studying the kinetic mechanism of enzyme action. II. Rate equations for three substrate enzyme systems Archives of Biochemistry and Biophysics. 147: 515-526. PMID 5136100 DOI: 10.1016/0003-9861(71)90409-7 |
0.672 |
|
| 1971 |
Rudolph FB, Fromm HJ. Computer simulation studies with yeast hexokinase and additional evidence for the random Bi Bi mechanism Journal of Biological Chemistry. 246: 6611-6619. PMID 5132674 |
0.49 |
|
| 1971 |
Rudolph FB, Fromm HJ. The purification and properties of aspartase from Escherichia coli Archives of Biochemistry and Biophysics. 147: 92-98. PMID 5000448 DOI: 10.1016/0003-9861(71)90313-4 |
0.666 |
|
| 1971 |
Rudolph FB, Fromm HJ. A study on the kinetics and mechanism of D-lyxose and D-xylose activation of the adenosine triphosphatase activity associated with yeast hexokinase Journal of Biological Chemistry. 246: 2104-2110. PMID 4252220 |
0.52 |
|
| 1970 |
Rudolph FB, Fromm HJ. Use of isotope competition and alternative substrates for studying the kinetic mechanism of enzyme action. I. Experiments with hexokinase and alcohol dehydrogenase Biochemistry. 9: 4660-4665. PMID 4320539 |
0.603 |
|
| 1970 |
Rudolph FB, Fromm HJ. Kinetic studies of the adenosine 5'-triphosphatase activity of yeast hexokinase and its relationship to the mechanism of action of the enzyme Journal of Biological Chemistry. 245: 4047-4052. PMID 4250551 |
0.645 |
|
| 1969 |
Fromm HJ. Comments on the kinetics and mechanism of yeast hexokinase action. Is the binding sequence of substrates to the enzyme ordered or random? European Journal of Biochemistry. 7: 385-392. PMID 5791583 |
0.374 |
|
| 1969 |
Rudolph FB, Fromm HJ. Initial rate studies of adenylosuccinate synthetase with product and competitive inhibitors Journal of Biological Chemistry. 244: 3832-3839. PMID 4896485 |
0.515 |
|
| 1968 |
Fromm HJ, Ning J. Kinetic studies of solubilized brain hexokinase with D-fructose as a substrate Biochemical and Biophysical Research Communications. 32: 672-677. PMID 5682290 DOI: 10.1016/0006-291X(68)90291-X |
0.314 |
|
| 1968 |
Rudolph FB, Purich DL, Fromm HJ. Coenzyme A-linked aldehyde dehydrogenase from Escherichia coli. I. Partial purification, properties, and kinetic studies of the enzyme Journal of Biological Chemistry. 243: 5539-5545. PMID 4301680 |
0.663 |
|
| 1967 |
Copley M, Fromm HJ. Kinetic studies of the brain hexokinase reaction. A reinvestigation with the solubilized bovine enzyme Biochemistry. 6: 3503-3509. PMID 6073035 DOI: 10.1021/Bi00863A023 |
0.477 |
|
| 1967 |
Fromm HJ. The use of competitive inhibitors in studying the mechanism of action of some enzyme systems utilizing three substrates Bba - Enzymology. 139: 221-230. PMID 6034669 DOI: 10.1016/0005-2744(67)90026-5 |
0.479 |
|
| 1966 |
Fromm HJ, Bietz JA. Ribitol dehydrogenase. IV. Purification and crystallization of the enzyme Archives of Biochemistry and Biophysics. 115: 510-514. |
0.364 |
|
| 1965 |
Zewe V, Fromm HJ. Kinetic studies of rabbit muscle lactate dehydrogenase. II. Mechanism of the reaction Biochemistry. 4: 782-792. DOI: 10.1021/Bi00880A024 |
0.489 |
|
| 1964 |
Fromm HJ. The use of alternative substrates in studying enzymic mechanisms involving two substrate Bba - Enzymological Subjects. 81: 413-417. PMID 14170314 |
0.372 |
|
| 1962 |
Fromm HJ. The enzymic determination of ribitol Bba - Biochimica Et Biophysica Acta. 57: 369-370. PMID 13895502 DOI: 10.1016/0006-3002(62)91131-9 |
0.483 |
|
| 1959 |
Fromm HJ, Nordlie RC. On the purification and kinetics of rat liver thetin-homocysteine transmethylase Archives of Biochemistry and Biophysics. 81: 363-376. PMID 13637998 DOI: 10.1016/0003-9861(59)90214-0 |
0.37 |
|
| 1958 |
FROMM HJ. Ribitol dehydrogenase. I. Purification and properties of the enzyme The Journal of Biological Chemistry. 233: 1049-1052. PMID 13598730 |
0.367 |
|
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