| Year |
Citation |
Score |
| 2018 |
Culbertson AT, Ehrlich JJ, Choe JY, Honzatko RB, Zabotina OA. Structure of xyloglucan xylosyltransferase 1 reveals simple steric rules that define biological patterns of xyloglucan polymers. Proceedings of the National Academy of Sciences of the United States of America. PMID 29784804 DOI: 10.1073/Pnas.1801105115 |
0.389 |
|
| 2016 |
Milton ME, Choe JY, Honzatko RB, Nelson SW. Crystal structure of the apicoplast DNA polymerase from Plasmodium falciparum: the first look at a plastidic A-family DNA polymerase. Journal of Molecular Biology. PMID 27487482 DOI: 10.1016/J.Jmb.2016.07.016 |
0.323 |
|
| 2015 |
Milton ME, Choe JY, Honzatko RB, Nelson SW. Crystallization and preliminary X-ray analysis of the Plasmodium falciparum apicoplast DNA polymerase. Acta Crystallographica. Section F, Structural Biology Communications. 71: 333-7. PMID 25760711 DOI: 10.1107/S2053230X15002423 |
0.31 |
|
| 2014 |
Gao Y, Shen L, Honzatko RB. Central cavity of fructose-1,6-bisphosphatase and the evolution of AMP/fructose 2,6-bisphosphate synergism in eukaryotic organisms. The Journal of Biological Chemistry. 289: 8450-61. PMID 24436333 DOI: 10.1074/Jbc.M114.548586 |
0.504 |
|
| 2013 |
Gao Y, Iancu CV, Mukind S, Choe JY, Honzatko RB. Mechanism of displacement of a catalytically essential loop from the active site of mammalian fructose-1,6-bisphosphatase. Biochemistry. 52: 5206-16. PMID 23844654 DOI: 10.1021/Bi400532N |
0.709 |
|
| 2012 |
Joseph RE, Ginder ND, Hoy JA, Nix JC, Fulton DB, Honzatko RB, Andreotti AH. Structure of the interleukin-2 tyrosine kinase Src homology 2 domain; comparison between X-ray and NMR-derived structures. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 68: 145-53. PMID 22297986 DOI: 10.1107/S1744309111049761 |
0.726 |
|
| 2012 |
Zhou K, Gao Y, Hoy JA, Mann FM, Honzatko RB, Peters RJ. Insights into diterpene cyclization from structure of bifunctional abietadiene synthase from Abies grandis. The Journal of Biological Chemistry. 287: 6840-50. PMID 22219188 DOI: 10.1074/Jbc.M111.337592 |
0.346 |
|
| 2011 |
Joseph RE, Ginder ND, Hoy JA, Nix JC, Honzatko RB, Andreotti AH. Purification, crystallization and preliminary crystallographic analysis of the SH2 domain of IL-2-inducible T-cell kinase. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 269-73. PMID 21301103 DOI: 10.1107/S1744309110052346 |
0.733 |
|
| 2010 |
Leung DW, Borek D, Farahbakhsh M, Ramanan P, Nix JC, Wang T, Prins KC, Otwinowski Z, Honzatko RB, Helgeson LA, Basler CF, Amarasinghe GK. Crystallization and preliminary X-ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 66: 689-692. PMID 20516601 DOI: 10.1107/S1744309110013266 |
0.675 |
|
| 2010 |
Leung DW, Prins KC, Borek DM, Farahbakhsh M, Tufariello JM, Ramanan P, Nix JC, Helgeson LA, Otwinowski Z, Honzatko RB, Basler CF, Amarasinghe GK. Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35 Nature Structural and Molecular Biology. 17: 165-172. PMID 20081868 DOI: 10.1038/Nsmb.1765 |
0.656 |
|
| 2010 |
Warner CD, Hoy JA, Shilling TC, Linnen MJ, Ginder ND, Ford CF, Honzatko RB, Reilly PJ. Tertiary structure and characterization of a glycoside hydrolase family 44 endoglucanase from Clostridium acetobutylicum. Applied and Environmental Microbiology. 76: 338-46. PMID 19915043 DOI: 10.1128/Aem.02026-09 |
0.749 |
|
| 2009 |
Leung DW, Ginder ND, Nix JC, Basler CF, Honzatko RB, Amarasinghe GK. Expression, purification, crystallization and preliminary X-ray studies of the Ebola VP35 interferon inhibitory domain Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 163-165. PMID 19194011 DOI: 10.1107/S1744309108044187 |
0.721 |
|
| 2009 |
Leung DW, Ginder ND, Fulton DB, Nix J, Basler CF, Honzatko RB, Amarasinghe GK. Structure of the Ebola VP35 interferon inhibitory domain Proceedings of the National Academy of Sciences of the United States of America. 106: 411-416. PMID 19122151 DOI: 10.1073/Pnas.0807854106 |
0.735 |
|
| 2008 |
Ginder ND, Binkowski DJ, Chen X, Nix JC, Fromm HJ, Honzatko RB. Entrapment of Phosphoryl Intermediates by SAICAR Synthetase The Faseb Journal. 22: 233-233. DOI: 10.1096/Fasebj.22.2_Supplement.233 |
0.712 |
|
| 2008 |
Warner CD, Hoy JA, Shilling TC, Linnen MJ, Ginder ND, Ford CF, Honzatko RB, Reilly PJ. Tertiary structure and properties of a glycoside hydrolase family 44 endoglucanase from clostridium acetobutylicum Aiche Annual Meeting, Conference Proceedings. |
0.677 |
|
| 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 |
0.737 |
|
| 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 |
0.756 |
|
| 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 |
0.766 |
|
| 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 |
0.739 |
|
| 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 |
0.761 |
|
| 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 |
0.78 |
|
| 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 |
0.766 |
|
| 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 |
0.741 |
|
| 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 |
0.771 |
|
| 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 |
0.41 |
|
| 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 |
0.492 |
|
| 2003 |
Aleshin AE, Feng PH, Honzatko RB, Reilly PJ. Crystal structure and evolution of a prokaryotic glucoamylase. Journal of Molecular Biology. 327: 61-73. PMID 12614608 DOI: 10.1016/S0022-2836(03)00084-6 |
0.343 |
|
| 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 |
0.435 |
|
| 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 |
0.737 |
|
| 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 |
0.736 |
|
| 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 |
0.756 |
|
| 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 |
0.764 |
|
| 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 |
0.44 |
|
| 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 |
0.355 |
|
| 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 |
0.49 |
|
| 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 |
0.37 |
|
| 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 |
0.75 |
|
| 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 |
0.408 |
|
| 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 |
0.472 |
|
| 2000 |
Mallis RJ, Poland BW, Chatterjee TK, Fisher RA, Darmawan S, Honzatko RB, Thomas JA. Crystal structure of S-glutathiolated carbonic anhydrase III Febs Letters. 482: 237-241. PMID 11024467 DOI: 10.1016/S0014-5793(00)02022-6 |
0.33 |
|
| 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 |
0.718 |
|
| 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 |
0.442 |
|
| 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 |
0.385 |
|
| 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 |
0.477 |
|
| 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 |
0.429 |
|
| 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 |
0.521 |
|
| 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 |
0.396 |
|
| 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 |
0.359 |
|
| 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 |
0.502 |
|
| 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 |
0.359 |
|
| 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 |
0.463 |
|
| 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 |
0.386 |
|
| 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 |
0.451 |
|
| 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 |
0.478 |
|
| 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 |
0.474 |
|
| 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 |
0.431 |
|
| 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 |
0.461 |
|
| 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 |
0.411 |
|
| 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 |
0.453 |
|
| 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 |
0.449 |
|
| 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. |
0.326 |
|
| 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 |
0.431 |
|
| 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 |
0.457 |
|
| 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 |
0.45 |
|
| 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 |
0.485 |
|
| 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 |
0.418 |
|
| 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 |
0.45 |
|
| 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 |
0.382 |
|
| 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 |
0.374 |
|
| 1996 |
Aleshin AE, Zeng C, Fromm HJ, Honzatko RB. Crystallization and preliminary X-ray analysis of human brain hexokinase Febs Letters. 391: 9-10. PMID 8706938 DOI: 10.1016/0014-5793(96)00688-6 |
0.305 |
|
| 1996 |
Aleshin AE, Stoffer B, Firsov LM, Svensson B, Honzatko RB. Crystallographic complexes of glucoamylase with maltooligosaccharide analogs: Relationship of stereochemical distortions at the nonreducing end to the catalytic mechanism Biochemistry. 35: 8319-8328. PMID 8679589 DOI: 10.1021/Bi960321G |
0.431 |
|
| 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 |
0.427 |
|
| 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 |
0.438 |
|
| 1995 |
Stoffer B, Aleshin AE, Firsov LM, Svensson B, Honzatko RB. Refined structure for the complex of d-gluco-dihydroacarbose with glucoamylase from Aspergillus awamori var. X100 to 2.2 Å resolution: dual conformations for extended inhibitors bound to the active site of glucoamylase Febs Letters. 358: 57-61. PMID 7821430 DOI: 10.1016/0014-5793(94)01354-4 |
0.405 |
|
| 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 |
0.446 |
|
| 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 |
0.427 |
|
| 1995 |
Frandsen TP, Christensen T, Stoffer B, Lehmbeck J, Dupont C, Honzatko RB, Svensson B. Mutational analysis of the roles in catalysis and substrate recognition of arginines 54 and 305, aspartic acid 309, and tryptophan 317 located at subsites 1 and 2 in glucoamylase from Aspergillus niger Biochemistry. 34: 10162-10169. DOI: 10.1021/Bi00032A009 |
0.365 |
|
| 1994 |
Aleshin AE, Firsov LM, Honzatko RB. Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-Å resolution Journal of Biological Chemistry. 269: 15631-15639. PMID 8195212 DOI: 10.2210/Pdb1Agm/Pdb |
0.408 |
|
| 1994 |
Aleshin AE, Hoffman C, Firsov LM, Honzatko RB. Refined crystal structures of glucoamylase from Aspergillus awamori var. X100 Journal of Molecular Biology. 238: 575-591. PMID 8176747 DOI: 10.1006/Jmbi.1994.1316 |
0.43 |
|
| 1994 |
Frandsen TP, Dupont C, Lehmbeck J, Stoffer B, Sierks MR, Honzatko RB, Svensson B. Site-directed mutagenesis of the catalytic base glutamic acid 400 in glucoamylase from Aspergillus niger and of tyrosine 48 and glutamine 401, both hydrogen-bonded to the γ-carboxylate group of glutamic acid 400 Biochemistry. 33: 13808-13816. PMID 7947792 DOI: 10.1021/Bi00250A035 |
0.436 |
|
| 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 |
0.359 |
|
| 1993 |
Harris EMS, Aleshin AE, Firsov LM, Honzatko RB. Refined structure for the complex of 1-deoxynojirimycin with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution. Biochemistry. 32: 1618-1626. PMID 8431441 DOI: 10.1021/Bi00057A028 |
0.419 |
|
| 1993 |
Poland BW, Silva MM, Serra MA, Cho Y, Kim KH, Harris EMS, Honzatko RB. Crystal structure of adenylosuccinate synthetase from Escherichia coli: Evidence for convergent evolution of GTP-binding domains Journal of Biological Chemistry. 268: 25334-25342. PMID 8244965 |
0.367 |
|
| 1992 |
Aleshin A, Golubev A, Firsov LM, Honzatko RB. Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-Å resolution Journal of Biological Chemistry. 267: 19291-19298. PMID 1527049 DOI: 10.2210/Pdb1Gly/Pdb |
0.358 |
|
| 1988 |
Ke HM, Lipscomb WN, Cho YJ, Honzatko RB. Complex of N-phosphonacetyl-L-aspartate with aspartate carbamoyltransferase. X-ray refinement, analysis of conformational changes and catalytic and allosteric mechanisms. Journal of Molecular Biology. 204: 725-47. PMID 3066911 DOI: 10.1016/0022-2836(88)90365-8 |
0.42 |
|
| 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 |
0.37 |
|
| 1987 |
Kim KH, Honzatko RB, Little RM, Anderson PM. Preliminary X-ray crystallographic study of cyanase from Escherichia coli Journal of Molecular Biology. 198: 137-138. PMID 3323528 DOI: 10.1016/0022-2836(87)90465-7 |
0.335 |
|
| 1987 |
Kim KH, Pan ZX, Honzatko RB, Ke HM, Lipscomb WN. Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli. Journal of Molecular Biology. 196: 853-75. PMID 3316665 DOI: 10.1016/0022-2836(87)90410-4 |
0.446 |
|
| 1986 |
Smith JL, Hendrickson WA, Honzatko RB, Sheriff S. Structural heterogeneity in protein crystals Biochemistry. 25: 5018-5027. PMID 3768328 DOI: 10.1021/Bi00366A008 |
0.363 |
|
| 1986 |
Honzatko RB, Hendrickson WA. Molecular models for the putative dimer of sea lamprey hemoglobin Proceedings of the National Academy of Sciences of the United States of America. 83: 8487-8491. PMID 3464965 DOI: 10.1073/Pnas.83.22.8487 |
0.308 |
|
| 1984 |
Ke HM, Honzatko RB, Lipscomb WN. Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 81: 4037-40. PMID 6377306 DOI: 10.1073/Pnas.81.13.4037 |
0.323 |
|
| 1982 |
Honzatko RB, Williams RW. Raman spectroscopy of avidin: secondary structure, disulfide conformation, and the environment of tyrosine Biochemistry. 21: 6201-6205. PMID 7150551 DOI: 10.1021/Bi00267A027 |
0.359 |
|
| 1982 |
Ladner JE, Kitchell JP, Honzatko RB, Ke HM, Volz KW, Kalb AJ, Ladner RC, Lipscomb WN. Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study. Proceedings of the National Academy of Sciences of the United States of America. 79: 3125-8. PMID 6954462 DOI: 10.1073/Pnas.79.10.3125 |
0.385 |
|
| 1982 |
Honzatko RB, Lipscomb WN. Interactions of metal-nucleotide complexes with aspartate carbamoyltransferase in the crystalline state. Proceedings of the National Academy of Sciences of the United States of America. 79: 7171-4. PMID 6760190 |
0.325 |
|
| 1982 |
Honzatko RB, Crawford JL, Monaco HL, Ladner JE, Ewards BF, Evans DR, Warren SG, Wiley DC, Ladner RC, Lipscomb WN. Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli. Journal of Molecular Biology. 160: 219-63. PMID 6757446 DOI: 10.1016/0022-2836(82)90175-9 |
0.358 |
|
| 1982 |
Honzatko RB, Lipscomb WN. Interactions of phosphate ligands with Escherichia coli aspartate carbamoyltransferase in the crystalline state. Journal of Molecular Biology. 160: 265-86. PMID 6294306 DOI: 10.1016/0022-2836(82)90176-0 |
0.365 |
|
| 1981 |
Rees DC, Lewis M, Honzatko RB, Lipscomb WN, Hardman KD. Zinc environment and cis peptide bonds in carboxypeptidase A at 1.75-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 78: 3408-12. PMID 6943549 DOI: 10.1073/Pnas.78.6.3408 |
0.403 |
|
| 1980 |
Rees DC, Honzatko RB, Lipscomb WN. Structure of an actively exchanging complex between carboxypeptidase A and a substrate analogue. Proceedings of the National Academy of Sciences of the United States of America. 77: 3288-91. PMID 6932021 DOI: 10.1073/Pnas.77.6.3288 |
0.396 |
|
| 1979 |
Honzatko RB, Monaco HL, Lipscomb WN. A 3.0-A resolution study of nucleotide complexes with aspartate carbamoyltransferase. Proceedings of the National Academy of Sciences of the United States of America. 76: 5105-9. PMID 388429 DOI: 10.1073/Pnas.76.10.5105 |
0.472 |
|
| Show low-probability matches. |