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Susan M. Miller - Publications

Affiliations: 
University of California, San Francisco, San Francisco, CA 
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26 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Bewley KD, Bennallack PR, Burlingame MA, Robison RA, Griffitts JS, Miller SM. Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791142 DOI: 10.1073/Pnas.1612161113  0.339
2016 Bennallack PR, Bewley KD, Burlingame MA, Robison RA, Miller SM, Griffitts JS. Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis. Journal of Bacteriology. PMID 27381911 DOI: 10.1128/Jb.00396-16  0.314
2011 Johs A, Parks JM, Harwood I, Guo H, Smith J, Miller SM, Summers AO, Liang L. Biomolecular Mechanisms of Microbial Mercury Resistance in the Environment Biophysical Journal. 100: 313a. DOI: 10.1016/J.Bpj.2010.12.1910  0.311
2011 Song B, Galande AK, Kodukula K, Moos WH, Miller SM. Evaluation of the pKa values and ionization sequence of bumetanide using 1H and 13C NMR and UV spectroscopy Drug Development Research. 72: 416-426. DOI: 10.1002/Ddr.20443  0.563
2010 Ledwidge R, Hong B, Dötsch V, Miller SM. NmerA of Tn501 mercuric ion reductase: structural modulation of the pKa values of the metal binding cysteine thiols. Biochemistry. 49: 8988-98. PMID 20828160 DOI: 10.1021/Bi100537F  0.31
2010 Hong B, Nauss R, Harwood IM, Miller SM. Direct measurement of mercury(II) removal from organomercurial lyase (MerB) by tryptophan fluorescence: NmerA domain of coevolved γ-proteobacterial mercuric ion reductase (MerA) is more efficient than MerA catalytic core or glutathione . Biochemistry. 49: 8187-96. PMID 20722420 DOI: 10.1021/Bi100802K  0.311
2009 Parks JM, Guo H, Momany C, Liang L, Miller SM, Summers AO, Smith JC. Mechanism of Hg-C protonolysis in the organomercurial lyase MerB. Journal of the American Chemical Society. 131: 13278-85. PMID 19719173 DOI: 10.1021/Ja9016123  0.337
2009 Moos WH, Rurka JE, Miller SM. Bright lights, clearly visible in the healthcare R&D tunnel, could burn out for lack of funds Drug Development Research. 70: 457-460. DOI: 10.1002/Ddr.20354  0.539
2007 Miller SM. Cleaving C-Hg bonds: two thiolates are better than one. Nature Chemical Biology. 3: 537-8. PMID 17710098 DOI: 10.1038/Nchembio0907-537  0.32
2005 Ledwidge R, Patel B, Dong A, Fiedler D, Falkowski M, Zelikova J, Summers AO, Pai EF, Miller SM. NmerA, the metal binding domain of mercuric ion reductase, removes Hg2+ from proteins, delivers it to the catalytic core, and protects cells under glutathione-depleted conditions. Biochemistry. 44: 11402-16. PMID 16114877 DOI: 10.1021/Bi050519D  0.315
2005 Ledwidge R, Soinski R, Miller SM. Direct monitoring of metal ion transfer between two trafficking proteins. Journal of the American Chemical Society. 127: 10842-3. PMID 16076185 DOI: 10.1021/Ja052872C  0.314
2003 Barkay T, Miller SM, Summers AO. Bacterial mercury resistance from atoms to ecosystems. Fems Microbiology Reviews. 27: 355-84. PMID 12829275 DOI: 10.1016/S0168-6445(03)00046-9  0.301
2000 Buckman J, Miller SM. Stabilization of a novel enzyme.substrate intermediate in the Y206F mutant of Candida albicans EBP1: evidence for acid catalysis. Biochemistry. 39: 10532-10541. PMID 10956044 DOI: 10.1021/Bi000653S  0.341
2000 Buckman J, Miller SM. Transient kinetics and intermediates formed during the electron transfer reaction catalyzed by Candida albicans estrogen binding protein. Biochemistry. 39: 10521-10531. PMID 10956043 DOI: 10.1021/Bi0006520  0.306
1999 Samuels NM, Gibson BW, Miller SM. Investigation of the kinetic mechanism of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi with new insights on rate-limiting steps from product inhibition analysis. Biochemistry. 38: 6195-203. PMID 10320348 DOI: 10.1021/Bi990282J  0.341
1999 Engst S, Miller SM. Alternative routes for entry of HgX2 into the active site of mercuric ion reductase depend on the nature of the X ligands. Biochemistry. 38: 3519-3529. PMID 10090738 DOI: 10.1021/Bi982680C  0.344
1998 Engst S, Miller SM. Rapid reduction of Hg(II) by mercuric ion reductase does not require the conserved C-terminal cysteine pair using HgBr2 as the substrate. Biochemistry. 37: 11496-11507. PMID 9708985 DOI: 10.1021/Bi9808161  0.359
1995 Miller SM. 2'-fluoro-2'-deoxy-D-arabinoflavin: characterization of a novel flavin and its effects on the formation and stability of two-electron-reduced mercuric ion reductase. Biochemistry. 34: 13066-13073. PMID 7548066 DOI: 10.1021/Bi00040A018  0.312
1995 Miller SM, Simon RJ, Ng S, Zuckermann RN, Kerr JM, Moos WH. Comparison of the proteolytic susceptibilities of homologous L-amino acid, D-amino acid, and N-substituted glycine peptide and peptoid oligomers Drug Development Research. 35: 20-32. DOI: 10.1002/Ddr.430350105  0.558
1994 Miller SM, Simon RJ, Ng S, Zuckermann RN, Kerr JM, Moos WH. Proteolytic studies of homologous peptide and N-substituted glycine peptoid oligomers Bioorganic and Medicinal Chemistry Letters. 4: 2657-2662. DOI: 10.1016/S0960-894X(01)80691-0  0.599
1994 Simon RJ, Martin EJ, Miller SM, Zuckermann RN, Blaney JM, Moos WH. Using Peptoid Libraries [Oligo N-Substituted Glycines] for Drug Discovery Techniques in Protein Chemistry. 5: 533-539. DOI: 10.1016/B978-0-12-194710-1.50065-5  0.58
1992 Moore MJ, Miller SM, Walsh CT. C-terminal cysteines of Tn501 mercuric ion reductase. Biochemistry. 31: 1677-85. PMID 1531297 DOI: 10.1021/Bi00121A015  0.35
1991 Miller SM, Massey V, Williams CH, Ballou DP, Walsh CT. Communication between the active sites in dimeric mercuric ion reductase: an alternating sites hypothesis for catalysis. Biochemistry. 30: 2600-12. PMID 2001350 DOI: 10.1021/Bi00224A006  0.336
1990 Miller SM, Massey V, Ballou D, Williams CH, Distefano MD, Moore MJ, Walsh CT. Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry. 29: 2831-41. PMID 2189497 DOI: 10.1021/Bi00463A028  0.344
1989 Miller SM, Moore MJ, Massey V, Williams CH, Distefano MD, Ballou DP, Walsh CT. Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry. 28: 1194-205. PMID 2653437 DOI: 10.1021/Bi00429A037  0.332
1985 Miller SM, Klinman JP. Secondary isotope effects and structure-reactivity correlations in the dopamine beta-monooxygenase reaction: evidence for a chemical mechanism. Biochemistry. 24: 2114-27. PMID 3995006 DOI: 10.1021/Bi00330A004  0.308
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