Year |
Citation |
Score |
2015 |
Huang X, Hernick M. Recombinant Expression of a Functional Myo-Inositol-1-Phosphate Synthase (MIPS) in Mycobacterium smegmatis. The Protein Journal. PMID 26420670 DOI: 10.1007/S10930-015-9632-Z |
0.318 |
|
2015 |
Kocabas E, Liu H, Hernick M. Identity of cofactor bound to mycothiol conjugate amidase (Mca) influenced by expression and purification conditions. Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 28: 755-63. PMID 26044118 DOI: 10.1007/S10534-015-9864-6 |
0.388 |
|
2015 |
Huang X, Hernick M. Molecular Determinants of N-Acetylglucosamine Recognition and Turnover by N-Acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside Deacetylase (MshB). Biochemistry. 54: 3784-90. PMID 26024468 DOI: 10.1021/Acs.Biochem.5B00068 |
0.365 |
|
2014 |
Huang X, Hernick M. Automated docking studies provide insights into molecular determinants of ligand recognition by N-acetyl-1-d-myo-inosityl-2-amino-2-deoxy-α-d-glucopyranoside deacetylase (MshB). Biopolymers. 101: 406-17. PMID 24037975 DOI: 10.1002/Bip.22397 |
0.397 |
|
2013 |
Hernick M. Mycothiol: a target for potentiation of rifampin and other antibiotics against Mycobacterium tuberculosis. Expert Review of Anti-Infective Therapy. 11: 49-67. PMID 23428102 DOI: 10.1586/Eri.12.152 |
0.358 |
|
2012 |
Huang X, Hernick M. Examination of mechanism of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase (MshB) reveals unexpected role for dynamic tyrosine. The Journal of Biological Chemistry. 287: 10424-34. PMID 22315231 DOI: 10.1074/Jbc.M111.320184 |
0.396 |
|
2011 |
Huang X, Hernick M. A limitation of the continuous spectrophotometric assay for the measurement of myo-inositol-1-phosphate synthase activity. Analytical Biochemistry. 417: 228-32. PMID 21729692 DOI: 10.1016/J.Ab.2011.06.010 |
0.395 |
|
2011 |
Huang X, Kocabas E, Hernick M. The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions. The Journal of Biological Chemistry. 286: 20275-82. PMID 21507949 DOI: 10.1074/Jbc.M111.234229 |
0.411 |
|
2011 |
Huang X, Hernick M. A fluorescence-based assay for measuring N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-α-D-glucopyranoside deacetylase activity. Analytical Biochemistry. 414: 278-81. PMID 21477577 DOI: 10.1016/J.Ab.2011.04.001 |
0.37 |
|
2010 |
Gattis SG, Hernick M, Fierke CA. Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions. The Journal of Biological Chemistry. 285: 33788-96. PMID 20709752 DOI: 10.1074/Jbc.M110.147173 |
0.35 |
|
2010 |
Hernick M, Gattis SG, Penner-Hahn JE, Fierke CA. Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity. Biochemistry. 49: 2246-55. PMID 20136146 DOI: 10.1021/Bi902066T |
0.391 |
|
2006 |
Hernick M, Fierke CA. Catalytic mechanism and molecular recognition of E. coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase probed by mutagenesis. Biochemistry. 45: 15240-8. PMID 17176046 DOI: 10.1021/Bi061405K |
0.392 |
|
2006 |
Hernick M, Fierke CA. Molecular recognition by Escherichia coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase is modulated by bound metal ions. Biochemistry. 45: 14573-81. PMID 17144651 DOI: 10.1021/Bi061625Y |
0.384 |
|
2005 |
Hernick M, Gennadios HA, Whittington DA, Rusche KM, Christianson DW, Fierke CA. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. The Journal of Biological Chemistry. 280: 16969-78. PMID 15705580 DOI: 10.1074/Jbc.M413560200 |
0.358 |
|
2005 |
Hernick M, Fierke CA. Zinc hydrolases: the mechanisms of zinc-dependent deacetylases. Archives of Biochemistry and Biophysics. 433: 71-84. PMID 15581567 DOI: 10.1016/J.Abb.2004.08.006 |
0.346 |
|
2003 |
Hernick M, Borch RF. Studies on the mechanisms of activation of indolequinone phosphoramidate prodrugs. Journal of Medicinal Chemistry. 46: 148-54. PMID 12502368 DOI: 10.1021/Jm0203229 |
0.537 |
|
2002 |
Hernick M, Flader C, Borch RF. Design, synthesis, and biological evaluation of indolequinone phosphoramidate prodrugs targeted to DT-diaphorase. Journal of Medicinal Chemistry. 45: 3540-8. PMID 12139465 DOI: 10.1021/Jm020191B |
0.541 |
|
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