J.J.M. Liew, I.M. El Saudi, S.V. Nguyen, D.K. Wicht, D.P. Dowling. “Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer” J. Biol. Chem., 2021, doi:10.1016/j.jbc.2021.100823.
J. Soule, A.D. Gnann, R. Gonzalez, M.J. Parker, K.C. McKenna, S.V. Nguyen, N.T. Phan, D.K. Wicht, D.P. Dowling. “Structure and function of the two-component flavin-dependent methanesulfinate monooxygenase within bacterial sulfur assimilation” Biochem. Biophys. Res. Commun., 2020, 522, 107-112.
T.A.J. Grell, B.N. Bell, C. Nguyen, D.P. Dowling, N.A. Bruender, V. Bandarian, C.L. Drennan. “Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modification near [4Fe-4S] cluster engender flavodoxin specificity” Prot. Sc., 2019, 28, 202-215.
N.A. Bruender, T.A.J. Grell, D.P. Dowling, R.M. McCarty, C.L. Drennan, V. Bandarian. “7-Carboxy-7-deazaguanine synthase: A radical S-adenosyl-L-methionine enzyme with polar tendencies” J. Am. Chem. Soc., 2017, 139, 1912-1920.
D.P. Dowling*, Y. Kung, A.K. Croft, K. Taghizadeh, W.L. Kelly, C.T. Walsh, C.L. Drennan*. “Structural elements of an NRPS cyclization domain and its intermodule docking domain” PNAS, 2016, 2016, 113, 12432-12437.
D.P. Dowling, Z.D. Miles, C. Köhrer, S.J. Maiocco, S.J. Elliott, V. Bandarian, C.L. Drennan. “Molecular basis of cobalamin-dependent RNA modification” Nucleic Acids Res., 2016, 44, 9965-9976.
D.P. Dowling, R.M. McCarty, A.P. Young, N.A. Bruender, V. Bandarian, C.L. Drennan. “Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism” Nat. Chem. Biol., 2014, 10, 106-112.
*Selected as Cover Art Feature
D.P. Dowling, J.L. Vey, A.K. Croft, C.L. Drennan. “Structural diversity in the AdoMet radical enzyme superfamily” BBA-Prot. Proteom., 2012, 1824, 1178-1195.
D.P. Dowling, A.K. Croft, C.L. Drennan. “Radical use of Rossmann and TIM barrel architectures for controlling coenzyme B12 Chemistry” Annu. Rev. Biophys., 2012, 41, 403-427.
M.L. Ilies, D.P. Dowling, P.M. Lombardi, D.W. Christianson. “Synthesis of a new trifluoromethylketone analogue of L-arginine and contrasting inhibitory activity against human arginase I and histone deacetylase 8” Bioorg. Med. Chem. Lett., 2011, 21, 5854-5858.
M.L. Ilies, L.Di Costanzo, D.P. Dowling, K.J. Thorn, D.W. Christianson. “Binding of a,a-disubstituted amino acids to arginase suggests new avenues for inhibitor design” J. Med. Chem., 2011, 54, 5432-5443.
P.M. Lombardi, K.E. Cole, D.P. Dowling, D.W. Christianson. “Structure, mechanism, and inhibition of histone deacetylases and related metalloenzymes” Curr. Opin. Struct. Biol., 2011, 21, 735-743.
K.E. Cole, D.P. Dowling, M.A. Boone, A.J. Phillips, D.W. Christianson. “Structural basis of the antiproliferative activity of largazole, a depsipeptide inhibitor of the histone deacetylases” J. Am. Chem. Soc., 2012, 133, 12474-12477.
D.P. Dowling, M.L. Ilies, K.L. Olszewski, S.P. Portugal, M.M. Mota, M. Llinás, D.W. Christianson. “Crystal structure of arginase from Plasmodium falciparum and implications for L-arginine depletion in malarial infection” Biochemistry, 2010, 49, 5600-5608.
D.P. Dowling, S.G. Gattis, C.A. Fierke, D.W. Christianson. “Metal-substituted histone deacetylase structures” Biochemistry, 2010, 49, 5048-5056.
D.P. Dowling, S.L. Gantt, S.G. Gattis, C.A. Fierke, D.W. Christianson. “Structural studies of histone deacetylase 8 and its site-specific variants complexed with substrate and inhibitors” Biochemistry, 2008, 47, 13554-13563.
D.P. Dowling, L.Di Costanzo, H.A. Gennadios, and D.W. Christianson. “Evolution of the arginase fold and functional diversity” Cell. Mol. Life Sci., 2008, 65, 2039-2055.
C.S. Higham, D.P. Dowling, J.L. Shaw, A. Cetin, C.J. Zielgler, J.R. Farrell. “Multidentate aminophenol ligands prepared with Mannich condensations” Tet. Lett. 2006, 47, 4419-4423.
Select Student Presentations
J. Liew, I. El-Saudi, S. V. Nguyen, D. K. Wicht, and D. P. Dowling. Structural characterization of MsuD: Flavin-dependent monooxygenase involved in the sulfur assimilation pathway from DMSO2 to Pseudomonas fluorescens under the sulfur starvation response. Accepted talk canceled due to COVID-19. ACS online Scimeeting April 2020.