Year |
Citation |
Score |
2019 |
Topaz GR, Epiter-Smith V, Robolo C, Emad M, Ford V, Daley J, Byron J, Stieglitz KA. Characterization of Recombinant Fructose 1,6-bisphosphatase (FBPase) Gene Mutations: Evidence of Inhibition/Activation of FBPase Protein by Gene Mutation. Bioscience Reports. PMID 30683805 DOI: 10.1042/BSR20180960 |
0.356 |
|
2015 |
Djakpa H, Kulkarni A, Barrows-Murphy S, Miller G, Zhou W, Cho H, Török B, Stieglitz K. Identifying new drug targets for potent phospholipase D inhibitors: Combining sequence alignment, molecular docking and enzyme activity/binding assays. Chemical Biology & Drug Design. PMID 26691755 DOI: 10.1111/Cbdd.12705 |
0.335 |
|
2014 |
Kulkarni A, Quang P, Curry V, Keyes R, Zhou W, Cho H, Baffoe J, Török B, Stieglitz K. 1,3-disubstituted-4-aminopyrazolo [3, 4-d] pyrimidines, a new class of potent inhibitors for phospholipase D. Chemical Biology & Drug Design. 84: 270-81. PMID 24641677 DOI: 10.1111/Cbdd.12319 |
0.336 |
|
2014 |
Chang S, Török B, Stieglitz KA. The role of phospholipase D enzyme(s) in modulating cell signaling: Implications for cancer drug development Current Bioactive Compounds. 10: 124-130. |
0.317 |
|
2010 |
Li Z, Stieglitz KA, Shrout AL, Wei Y, Weis RM, Stec B, Roberts MF. Mobile loop mutations in an archaeal inositol monophosphatase: modulating three-metal ion assisted catalysis and lithium inhibition. Protein Science : a Publication of the Protein Society. 19: 309-18. PMID 20027624 DOI: 10.1002/Pro.315 |
0.359 |
|
2007 |
Stieglitz KA, Roberts MF, Li W, Stec B. Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima. The Febs Journal. 274: 2461-9. PMID 17419729 DOI: 10.1111/J.0014-2956.2007.05779.X |
0.355 |
|
2006 |
Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER. T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition. Biochemistry. 45: 10062-71. PMID 16906764 DOI: 10.1021/Bi0601095 |
0.344 |
|
2005 |
Stieglitz KA, Dusinberre KJ, Cardia JP, Tsuruta H, Kantrowitz ER. Structure of the E.coli aspartate transcarbamoylase trapped in the middle of the catalytic cycle. Journal of Molecular Biology. 352: 478-86. PMID 16120448 DOI: 10.1016/J.Jmb.2005.07.046 |
0.384 |
|
2005 |
Wang J, Stieglitz KA, Cardia JP, Kantrowitz ER. Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase. Proceedings of the National Academy of Sciences of the United States of America. 102: 8881-6. PMID 15951418 DOI: 10.1073/Pnas.0503742102 |
0.39 |
|
2005 |
Wang J, Stieglitz KA, Kantrowitz ER. Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. Biochemistry. 44: 8378-86. PMID 15938627 DOI: 10.1021/Bi050155P |
0.421 |
|
2005 |
Stieglitz KA, Pastra-Landis SC, Xia J, Tsuruta H, Kantrowitz ER. A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition. Journal of Molecular Biology. 349: 413-23. PMID 15890205 DOI: 10.1016/J.Jmb.2005.03.073 |
0.412 |
|
2005 |
Stieglitz KA, Yang H, Roberts MF, Stec B. Reaching for mechanistic consensus across life kingdoms: structure and insights into catalysis of the myo-inositol-1-phosphate synthase (mIPS) from Archaeoglobus fulgidus. Biochemistry. 44: 213-24. PMID 15628862 DOI: 10.1021/Bi048267O |
0.43 |
|
2004 |
Alam N, Stieglitz KA, Caban MD, Gourinath S, Tsuruta H, Kantrowitz ER. 240s loop interactions stabilize the T state of Escherichia coli aspartate transcarbamoylase. The Journal of Biological Chemistry. 279: 23302-10. PMID 15014067 DOI: 10.1074/Jbc.M401637200 |
0.329 |
|
2003 |
Stieglitz KA, Seaton BA, Head JF, Stec B, Roberts MF. Unexpected similarity in regulation between an archaeal inositol monophosphatase/fructose bisphosphatase and chloroplast fructose bisphosphatase. Protein Science : a Publication of the Protein Society. 12: 760-7. PMID 12649434 DOI: 10.1110/Ps.0236003 |
0.53 |
|
2002 |
Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. The Journal of Biological Chemistry. 277: 22863-74. PMID 11940584 DOI: 10.1074/Jbc.M201042200 |
0.53 |
|
2001 |
Stieglitz KA, Seaton BA, Roberts MF. Binding of proteolytically processed phospholipase D from Streptomyces chromofuscus to phosphatidylcholine membranes facilitates vesicle aggregation and fusion. Biochemistry. 40: 13954-63. PMID 11705386 DOI: 10.1021/Bi011338O |
0.552 |
|
1999 |
Stieglitz K, Seaton B, Roberts MF. The role of interfacial binding in the activation of Streptomyces chromofuscus phospholipase D by phosphatidic acid. The Journal of Biological Chemistry. 274: 35367-74. PMID 10585404 DOI: 10.1074/Jbc.274.50.35367 |
0.558 |
|
1999 |
Geng D, Baker DP, Foley SF, Zhou C, Stieglitz K, Roberts MF. A 20-kDa domain is required for phosphatidic acid-induced allosteric activation of phospholipase D from Streptomyces chromofuscus. Biochimica Et Biophysica Acta. 1430: 234-44. PMID 10082951 DOI: 10.1016/S0167-4838(99)00005-9 |
0.411 |
|
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