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Amie K. Boal, Ph.D. - Publications

Affiliations: 
Chemistry Pennsylvania State University, State College, PA, United States 
Area:
biochemistry
Website:
http://www.chem.psu.edu/directory/akb20
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53 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
2023 Slater JW, Lin CY, Neugebauer ME, McBride MJ, Sil D, Nair MA, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biochemistry. PMID 37542461 DOI: 10.1021/acs.biochem.3c00248  0.701
2023 Slater JW, Neugebauer ME, McBride MJ, Sil D, Lin CY, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biorxiv : the Preprint Server For Biology. PMID 37205437 DOI: 10.1101/2023.05.02.539147  0.696
2023 McBride MJ, Pope SR, Nair MA, Sil D, Salas-Solá XE, Krebs C, Martin Bollinger J, Boal AK. Methods for Biophysical Characterization of SznF, a Member of the Heme-Oxygenase-Like Diiron Oxidase/Oxygenase Superfamily. Methods in Molecular Biology (Clifton, N.J.). 2648: 123-154. PMID 37039989 DOI: 10.1007/978-1-0716-3080-8_9  0.331
2022 Lin CY, Muñoz AL, Laremore TN, Silakov A, Krebs C, Boal AK, Bollinger JM. Use of Noncanonical Tyrosine Analogues to Probe Control of Radical Intermediates during Endoperoxide Installation by Verruculogen Synthase (FtmOx1). Acs Catalysis. 12: 6968-6979. PMID 37744570 DOI: 10.1021/acscatal.2c01037  0.671
2022 Jeyachandran VR, Boal AK. Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes. Current Opinion in Chemical Biology. 68: 102153. PMID 35512465 DOI: 10.1016/j.cbpa.2022.102153  0.347
2022 McBride MJ, Nair MA, Sil D, Slater JW, Neugebauer ME, Chang MCY, Boal AK, Krebs C, Bollinger JM. Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro-l-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate. Biochemistry. PMID 35380785 DOI: 10.1021/acs.biochem.1c00774  0.316
2022 Braffman NR, Ruskoski TB, Davis KM, Glasser NR, Johnson C, Okafor CD, Boal AK, Balskus EP. Structural basis for an unprecedented enzymatic alkylation in cylindrocyclophane biosynthesis. Elife. 11. PMID 35212625 DOI: 10.7554/eLife.75761  0.643
2021 Ruskoski TB, Boal AK. The periodic table of ribonucleotide reductases. The Journal of Biological Chemistry. 101137. PMID 34461093 DOI: 10.1016/j.jbc.2021.101137  0.314
2021 Copeland RA, Davis KM, Shoda TKC, Blaesi EJ, Boal AK, Krebs C, Bollinger JM. An Iron(IV)-Oxo Intermediate Initiating l-Arginine Oxidation but Not Ethylene Production by the 2-Oxoglutarate-Dependent Oxygenase, Ethylene-Forming Enzyme. Journal of the American Chemical Society. PMID 33522811 DOI: 10.1021/jacs.0c10923  0.703
2021 McBride MJ, Pope SR, Hu K, Okafor CD, Balskus EP, Bollinger JM, Boal AK. Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of the -nitrosourea-producing enzyme SznF. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33468680 DOI: 10.1073/pnas.2015931118  0.383
2020 McBride M, Sil D, Ng TL, Crooke AM, Kenney GE, Tysoe CR, Zhang B, Balskus EP, Boal AK, Krebs C, Bollinger JM. A peroxodiiron(III) intermediate mediating both -hydroxylation steps in biosynthesis of the -nitrosourea pharmacophore of streptozotocin by SznF. Journal of the American Chemical Society. PMID 32511919 DOI: 10.1021/Jacs.0C03431  0.779
2019 Zhou S, Pan J, Davis KM, Schaperdoth I, Wang B, Boal AK, Krebs C, Bollinger JM. Steric enforcement of cis-epoxide formation in the radical C-O-coupling reaction by which (S)-2-hydroxypropylphosphonate epoxidase (HppE) produces Fosfomycin. Journal of the American Chemical Society. PMID 31769979 DOI: 10.1021/Jacs.9B10974  0.653
2019 Davis KM, Altmyer M, Martinie RJ, Schaperdoth I, Krebs C, Bollinger JM, Boal AK. Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD. Biochemistry. PMID 31503454 DOI: 10.1021/Acs.Biochem.9B00598  0.717
2019 Zhang B, Rajakovich LJ, Van Cura D, Blaesi EJ, Mitchell AJ, Tysoe CR, Zhu X, Streit BR, Rui Z, Zhang W, Boal AK, Krebs C, Bollinger JM. Substrate-triggered Formation of a Peroxo-Fe(III/III) Intermediate during Fatty Acid Decarboxylation by UndA. Journal of the American Chemical Society. PMID 31487162 DOI: 10.1021/Jacs.9B06093  0.669
2019 Gumkowski JD, Martinie RJ, Corrigan P, Pan J, Bauerle MR, Almarei M, Booker SJ, Silakov A, Krebs C, Boal AK. Analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an iron-binding accessory domain in a clostridial enzyme. Biochemistry. PMID 31246421 DOI: 10.1021/Acs.Biochem.9B00197  0.69
2019 Dunham NP, Del Río Pantoja JM, Zhang B, Rajakovich LJ, Allen BD, Krebs C, Boal AK, Bollinger JM. Hydrogen Donation but not Abstraction by a Tyrosine (Y68) During Endoperoxide Installation by Verruculogen Synthase (FtmOx1). Journal of the American Chemical Society. PMID 31117657 DOI: 10.2210/Pdb6Oxj/Pdb  0.46
2019 Featherston ER, Rose HR, McBride MJ, Taylor E, Boal AK, Cotruvo J. Biochemical and structural characterization of XoxG and XoxJ and their roles in activity of the lanthanide-dependent methanol dehydrogenase, XoxF. Chembiochem : a European Journal of Chemical Biology. PMID 31017712 DOI: 10.1002/Cbic.201900184  0.362
2019 Rose HR, Maggiolo AO, McBride MJ, Palowitch GM, Pandelia ME, Davis KM, Yennawar NH, Boal AK. Structures of class Id ribonucleotide reductase catalytic subunits reveal a minimal architecture for deoxynucleotide biosynthesis. Biochemistry. PMID 30855138 DOI: 10.2210/Pdb6Dqx/Pdb  0.684
2019 Rajakovich L, Pandelia ME, Mitchell AJ, Chang WC, Zhang B, Boal AK, Krebs C, Bollinger JM. A new microbial pathway for organophosphonate degradation catalyzed by two previously misannotated non-heme-iron oxygenases. Biochemistry. PMID 30789718 DOI: 10.1021/acs.biochem.9b00044  0.616
2019 Ng TL, Rohac R, Mitchell AJ, Boal AK, Balskus EP. An N-nitrosating metalloenzyme constructs the pharmacophore of streptozotocin. Nature. 566: 94-99. PMID 30728519 DOI: 10.1038/S41586-019-0894-Z  0.562
2018 Dunham NP, Mitchell AJ, Del Río Pantoja JM, Krebs C, Bollinger JM, Boal AK. α-Amine Desaturation of d-Arginine by the Iron(II)- and 2-(Oxo)glutarate-Dependent l-Arginine 3-Hydroxylase, VioC. Biochemistry. PMID 30403469 DOI: 10.1021/Acs.Biochem.8B00901  0.66
2018 Blaesi EJ, Palowitch GM, Hu K, Kim AJ, Rose HR, Alapati R, Lougee MG, Kim HJ, Taguchi AT, Tan KO, Laremore TN, Griffin RG, Krebs C, Matthews ML, Silakov A, ... ... Boal AK, et al. Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical. Proceedings of the National Academy of Sciences of the United States of America. PMID 30224458 DOI: 10.1073/Pnas.1811993115  0.704
2018 Parker MJ, Maggiolo AO, Thomas WC, Kim A, Meisburger SP, Ando N, Boal AK, Stubbe J. An endogenous dAMP ligand in class Ib RNR promotes assembly of a noncanonical dimer for regulation by dATP. Proceedings of the National Academy of Sciences of the United States of America. PMID 29712847 DOI: 10.1073/Pnas.1800356115  0.554
2018 Dunham NP, Chang WC, Mitchell AJ, Martinie RJ, Zhang B, Bergman JA, Rajakovich LJ, Wang B, Silakov A, Krebs C, Boal AK, Bollinger JM. Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of α-Heteroatom Assistance. Journal of the American Chemical Society. PMID 29708749 DOI: 10.1021/Jacs.8B01933  0.769
2018 Rose H, Ghosh M, Maggiolo A, Pollock CJ, Blaesi EJ, Hajj V, Wei Y, Rajakovich LJ, Chang WC, Han Y, Hajj M, Krebs C, Silakov A, Pandelia ME, Bollinger JM, ... Boal AK, et al. Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by its Dimanganese Cofactor. Biochemistry. PMID 29609464 DOI: 10.1021/Acs.Biochem.8B00247  0.706
2017 Davis KM, Boal AK. Mechanism-Based Strategies for Structural Characterization of Radical SAM Reaction Intermediates. Methods in Enzymology. 595: 331-359. PMID 28882206 DOI: 10.1016/Bs.Mie.2017.07.008  0.67
2017 Mitchell AJ, Dunham NP, Martinie RJ, Bergman JA, Pollock CJ, Hu K, Allen BD, Chang WC, Silakov A, Bollinger JM, Krebs C, Boal AK. Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. Journal of the American Chemical Society. 139: 13830-13836. PMID 28823155 DOI: 10.1021/Jacs.7B07374  0.764
2017 Badding E, Grove TL, Gadsby L, LaMattina J, Boal AK, Booker SJ. Rerouting the Pathway for the Biosynthesis of the Side Ring System of Nosiheptide: The Roles of NosI, NosJ, and NosK. Journal of the American Chemical Society. PMID 28343381 DOI: 10.1021/Jacs.7B01497  0.372
2016 Mitchell AJ, Dunham NP, Bergman JA, Wang B, Zhu Q, Chang WC, Liu X, Boal AK. Structure-guided reprogramming of a hydroxylase to halogenate its small molecule substrate. Biochemistry. PMID 28029241 DOI: 10.1021/Acs.Biochem.6B01173  0.565
2016 Mitchell AJ, Zhu Q, Maggiolo AO, Ananth NR, Hillwig ML, Liu X, Boal AK. Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5. Nature Chemical Biology. PMID 27348090 DOI: 10.1038/Nchembio.2112  0.551
2016 Schwalm EL, Grove TL, Booker SJ, Boal AK. Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA. Science (New York, N.Y.). 352: 309-12. PMID 27081063 DOI: 10.1126/Science.Aad5367  0.313
2015 Boal AK, Bollinger JM, Chang WC. Assembly of the unusual oxacycles in the orthosomycin antibiotics. Proceedings of the National Academy of Sciences of the United States of America. 112: 11989-90. PMID 26378126 DOI: 10.1073/Pnas.1514689112  0.413
2015 Boal AK, Rosenzweig AC. Response from Boal and Rosenzweig to Crystallography and chemistry should always go together: a cautionary tale of protein complexes with cisplatin and carboplatin. Acta Crystallographica. Section D, Biological Crystallography. 71: 1984-6. PMID 26327389 DOI: 10.1107/S1399004715014352  0.537
2014 Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. Journal of the American Chemical Society. 136: 8221-8. PMID 24806349 DOI: 10.1021/Ja410560P  0.74
2014 Chang WC, Guo Y, Wang C, Butch SE, Rosenzweig AC, Boal AK, Krebs C, Bollinger JM. Mechanism of the C5 stereoinversion reaction in the biosynthesis of carbapenem antibiotics. Science (New York, N.Y.). 343: 1140-4. PMID 24604200 DOI: 10.1126/Science.1248000  0.695
2014 Makhlynets O, Boal AK, Rhodes DV, Kitten T, Rosenzweig AC, Stubbe J. Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights. The Journal of Biological Chemistry. 289: 6259-72. PMID 24381172 DOI: 10.1074/Jbc.M113.533554  0.688
2013 Wörsdörfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proceedings of the National Academy of Sciences of the United States of America. 110: 18874-9. PMID 24198335 DOI: 10.1073/Pnas.1315927110  0.509
2013 Dassama LM, Krebs C, Bollinger JM, Rosenzweig AC, Boal AK. Structural basis for assembly of the Mn(IV)/Fe(III) cofactor in the class Ic ribonucleotide reductase from Chlamydia trachomatis. Biochemistry. 52: 6424-36. PMID 23924396 DOI: 10.1021/Bi400819X  0.787
2012 Boal AK, Rosenzweig AC. Biochemistry. A radical route for nitrogenase carbide insertion. Science (New York, N.Y.). 337: 1617-8. PMID 23019640 DOI: 10.1126/Science.1229088  0.636
2012 Boal AK, Cotruvo JA, Stubbe J, Rosenzweig AC. The dimanganese(II) site of Bacillus subtilis class Ib ribonucleotide reductase. Biochemistry. 51: 3861-71. PMID 22443445 DOI: 10.1021/Bi201925T  0.658
2012 Dassama LM, Boal AK, Krebs C, Rosenzweig AC, Bollinger JM. Evidence that the β subunit of Chlamydia trachomatis ribonucleotide reductase is active with the manganese ion of its manganese(IV)/iron(III) cofactor in site 1. Journal of the American Chemical Society. 134: 2520-3. PMID 22242660 DOI: 10.1021/Ja211314P  0.792
2011 Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC. Structural basis for methyl transfer by a radical SAM enzyme. Science (New York, N.Y.). 332: 1089-92. PMID 21527678 DOI: 10.1126/Science.1205358  0.619
2010 Boal AK, Cotruvo JA, Stubbe J, Rosenzweig AC. Structural basis for activation of class Ib ribonucleotide reductase. Science (New York, N.Y.). 329: 1526-30. PMID 20688982 DOI: 10.1126/Science.1190187  0.679
2010 Genereux JC, Boal AK, Barton JK. DNA-mediated charge transport in redox sensing and signaling. Journal of the American Chemical Society. 132: 891-905. PMID 20047321 DOI: 10.1021/Ja907669C  0.523
2009 Boal AK, Rosenzweig AC. Structural biology of copper trafficking. Chemical Reviews. 109: 4760-79. PMID 19824702 DOI: 10.1021/Cr900104Z  0.621
2009 Boal AK, Rosenzweig AC. Crystal structures of cisplatin bound to a human copper chaperone. Journal of the American Chemical Society. 131: 14196-7. PMID 19807176 DOI: 10.1021/Ja906363T  0.556
2009 Boal AK, Genereux JC, Sontz PA, Gralnick JA, Newman DK, Barton JK. Redox signaling between DNA repair proteins for efficient lesion detection. Proceedings of the National Academy of Sciences of the United States of America. 106: 15237-42. PMID 19720997 DOI: 10.1073/Pnas.0908059106  0.752
2008 Merino EJ, Boal AK, Barton JK. Biological contexts for DNA charge transport chemistry. Current Opinion in Chemical Biology. 12: 229-37. PMID 18314014 DOI: 10.1016/J.Cbpa.2008.01.046  0.524
2007 Boal AK, Yavin E, Barton JK. DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport? Journal of Inorganic Biochemistry. 101: 1913-21. PMID 17599416 DOI: 10.1016/J.Jinorgbio.2007.05.001  0.588
2006 Gorodetsky AA, Boal AK, Barton JK. Direct electrochemistry of endonuclease III in the presence and absence of DNA. Journal of the American Chemical Society. 128: 12082-3. PMID 16967954 DOI: 10.1021/Ja064784D  0.697
2005 Boal AK, Yavin E, Lukianova OA, O'Shea VL, David SS, Barton JK. DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters. Biochemistry. 44: 8397-407. PMID 15938629 DOI: 10.1021/Bi047494N  0.588
2005 Boal AK, Barton JK. Electrochemical detection of lesions in DNA. Bioconjugate Chemistry. 16: 312-21. PMID 15769084 DOI: 10.1021/Bc0497362  0.509
2005 Yavin E, Boal AK, Stemp ED, Boon EM, Livingston AL, O'Shea VL, David SS, Barton JK. Protein-DNA charge transport: redox activation of a DNA repair protein by guanine radical. Proceedings of the National Academy of Sciences of the United States of America. 102: 3546-51. PMID 15738421 DOI: 10.1073/Pnas.0409410102  0.777
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