| Year |
Citation |
Score |
| 2023 |
Adak S, Ye N, Calderone LA, Schäfer RJB, Lukowski AL, Pandelia ME, Drennan CL, Moore BS. Oxidative rearrangement of tryptophan to indole nitrile by a single diiron enzyme. Biorxiv : the Preprint Server For Biology. PMID 37577561 DOI: 10.1101/2023.08.03.551874 |
0.568 |
|
| 2023 |
Vaccaro FA, Born DA, Drennan CL. Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery. Proceedings of the National Academy of Sciences of the United States of America. 120: e2214085120. PMID 36787360 DOI: 10.1073/pnas.2214085120 |
0.313 |
|
| 2022 |
Biester A, Marcano-Delgado AN, Drennan CL. Structural Insights into Microbial One-Carbon Metabolic Enzymes Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenases and Acetyl-CoA Synthases. Biochemistry. PMID 36137563 DOI: 10.1021/acs.biochem.2c00425 |
0.321 |
|
| 2022 |
Bridwell-Rabb J, Li B, Drennan CL. Cobalamin-Dependent Radical -Adenosylmethionine Enzymes: Capitalizing on Old Motifs for New Functions. Acs Bio & Med Chem Au. 2: 173-186. PMID 35726326 DOI: 10.1021/acsbiomedchemau.1c00051 |
0.773 |
|
| 2022 |
King-Roberts D, Andorfer M, Drennan C. Characterization of an S-adenosylmethionine Dependent X-Succinate Synthase Activating Enzyme. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35560623 DOI: 10.1096/fasebj.2022.36.S1.R2841 |
0.318 |
|
| 2022 |
Avalos D, Fan PH, Geng Y, Liu HW, Drennan CL. Structural Investigation of AlsA, a Radical S-adenosylmethionine Enzyme Involved in the Biosynthesis of the Oxetane-containing Herbicide Albucidin. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35556550 DOI: 10.1096/fasebj.2022.36.S1.L7794 |
0.36 |
|
| 2022 |
Drennan CL, Andorfer MC, Backman LRF, Li PL, Ulrich EC. Repairing enzymes using spare parts. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35554970 DOI: 10.1096/fasebj.2022.36.S1.0I119 |
0.31 |
|
| 2022 |
Backman LRF, Huang YY, Andorfer MC, Gold B, Raines RT, Balskus EP, Drennan CL. Structurally investigating a niche pathway for chemical reversal of proline hydroxylation in the pathogen Clostridioides difficile. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. PMID 35553565 DOI: 10.1096/fasebj.2022.36.S1.R2341 |
0.368 |
|
| 2022 |
Ulrich EC, Drennan CL. The Atypical Cobalamin-Dependent -Adenosyl-l-Methionine Nonradical Methylase TsrM and Its Radical Counterparts. Journal of the American Chemical Society. 144: 5673-5684. PMID 35344653 DOI: 10.1021/jacs.1c12064 |
0.333 |
|
| 2022 |
Ohmer CJ, Dasgupta M, Patwardhan A, Bogacz I, Kaminsky C, Doyle MD, Chen PY, Keable SM, Makita H, Simon PS, Massad R, Fransson T, Chatterjee R, Bhowmick A, Paley DW, ... ... Drennan CL, et al. XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase. Journal of Inorganic Biochemistry. 230: 111768. PMID 35202981 DOI: 10.1016/j.jinorgbio.2022.111768 |
0.824 |
|
| 2021 |
Andorfer MC, Backman LRF, Li PL, Ulrich EC, Drennan CL. Rescuing activity of oxygen-damaged pyruvate formate-lyase by a spare part protein. The Journal of Biological Chemistry. 101423. PMID 34801558 DOI: 10.1016/j.jbc.2021.101423 |
0.311 |
|
| 2021 |
Feliciano PR, Carroll KS, Drennan CL. Crystal Structure of the [4Fe-4S] Cluster-Containing Adenosine-5'-phosphosulfate Reductase from . Acs Omega. 6: 13756-13765. PMID 34095667 DOI: 10.1021/acsomega.1c01043 |
0.338 |
|
| 2021 |
Dawson CD, Irwin SM, Backman LRF, Le C, Wang JX, Vennelakanti V, Yang Z, Kulik HJ, Drennan CL, Balskus EP. Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase. Cell Chemical Biology. PMID 33773110 DOI: 10.1016/j.chembiol.2021.03.001 |
0.361 |
|
| 2021 |
Knox HL, Chen PY, Blaszczyk AJ, Mukherjee A, Grove TL, Schwalm EL, Wang B, Drennan CL, Booker SJ. Structural basis for non-radical catalysis by TsrM, a radical SAM methylase. Nature Chemical Biology. PMID 33462497 DOI: 10.1038/s41589-020-00717-y |
0.797 |
|
| 2020 |
Cohen SE, Can M, Wittenborn EC, Hendrickson RA, Ragsdale SW, Drennan CL. Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase. Acs Catalysis. 10: 9741-9746. PMID 33495716 DOI: 10.1021/acscatal.0c03033 |
0.813 |
|
| 2020 |
Jonnalagadda R, Del Rio Flores A, Cai W, Mehmood R, Narayanamoorthy M, Ren C, Zaragoza JPT, Kulik HJ, Zhang W, Drennan CL. Biochemical and crystallographic investigations into isonitrile formation by a non-heme iron-dependent oxidase/decarboxylase. The Journal of Biological Chemistry. PMID 33361191 DOI: 10.1074/jbc.RA120.015932 |
0.327 |
|
| 2020 |
Bollenbach M, Ortega M, Orman M, Drennan CL, Balskus EP. Discovery of a Cyclic Choline Analog That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. Acs Medicinal Chemistry Letters. 11: 1980-1985. PMID 33062182 DOI: 10.1021/Acsmedchemlett.0C00005 |
0.797 |
|
| 2020 |
Cohen SE, Brignole EJ, Wittenborn EC, Can M, Thompson S, Ragsdale SW, Drennan CL. Negative-Stain Electron Microscopy Reveals Dramatic Structural Rearrangements in Ni-Fe-S-Dependent Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase. Structure (London, England : 1993). PMID 32937101 DOI: 10.1016/J.Str.2020.08.011 |
0.81 |
|
| 2020 |
Wittenborn EC, Guendon C, Merrouch M, Benvenuti M, Fourmond V, Léger C, Drennan CL, Dementin S. The Solvent-Exposed Fe-S D-Cluster Contributes to Oxygen-Resistance in Ni-Fe Carbon Monoxide Dehydrogenase. Acs Catalysis. 10: 7328-7335. PMID 32655979 DOI: 10.1021/Acscatal.0C00934 |
0.799 |
|
| 2020 |
Reinhardt CR, Li P, Kang G, Stubbe J, Drennan CL, Hammes-Schiffer S. Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase. Journal of the American Chemical Society. PMID 32631052 DOI: 10.1021/Jacs.0C04325 |
0.321 |
|
| 2020 |
Greene BL, Kang G, Cui C, Bennati M, Nocera DG, Drennan CL, Stubbe J. Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets. Annual Review of Biochemistry. 89: 45-75. PMID 32569524 DOI: 10.1146/Annurev-Biochem-013118-111843 |
0.374 |
|
| 2020 |
Rizzolo K, Weitz AC, Cohen S, Drennan CL, Hendrich MP, Elliott SJ. A stable ferryl porphyrin at the active site of Y463M BthA. Journal of the American Chemical Society. PMID 32564595 DOI: 10.1021/Jacs.0C04023 |
0.682 |
|
| 2020 |
Kang G, Taguchi AT, Stubbe J, Drennan CL. Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex. Science (New York, N.Y.). PMID 32217749 DOI: 10.1126/Science.Aba6794 |
0.395 |
|
| 2020 |
Backman LR, Huang YY, Andorfer MC, Gold B, Raines RT, Balskus EP, Drennan CL. Molecular basis for catabolism of the abundant metabolite -4-hydroxy-L-proline by a microbial glycyl radical enzyme. Elife. 9. PMID 32180548 DOI: 10.7554/Elife.51420 |
0.815 |
|
| 2020 |
Backman LR, Huang YY, Andorfer MC, Gold B, Raines RT, Balskus EP, Drennan CL. Author response: Molecular basis for catabolism of the abundant metabolite trans-4-hydroxy-L-proline by a microbial glycyl radical enzyme Elife. DOI: 10.7554/Elife.51420.Sa2 |
0.787 |
|
| 2020 |
Knox HL, Chen PY, Blaszczyk AJ, Grove TL, Schwalm EL, Wang B, Drennan CL, Booker SJ. Crystallographic snapshots of TsrM, a radical S‐adenosylmethionine enzyme whose reaction is not so radical The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.00561 |
0.777 |
|
| 2020 |
Cohen SE, Can M, Wittenborn EC, Hendrickson RA, Ragsdale SW, Drennan CL. Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Acs Catalysis. 10: 9741-9746. DOI: 10.1021/Acscatal.0C03033 |
0.795 |
|
| 2019 |
Feliciano PR, Drennan CL. Structural and biochemical investigations of the [4Fe-4S] cluster-containing fumarate hydratase from . Biochemistry. PMID 31743022 DOI: 10.1021/acs.biochem.9b00923 |
0.383 |
|
| 2019 |
Wittenborn EC, Cohen SE, Merrouch M, Léger C, Fourmond V, Dementin S, Drennan CL. Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase. The Journal of Biological Chemistry. PMID 31296570 DOI: 10.2210/Pdb6Ond/Pdb |
0.8 |
|
| 2019 |
Bowman SEJ, Backman LRF, Bjork RE, Andorfer MC, Yori S, Caruso A, Stultz CM, Drennan CL. Solution structure and biochemical characterization of a spare part protein that restores activity to an oxygen-damaged glycyl radical enzyme. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 31250200 DOI: 10.1007/s00775-019-01681-2 |
0.799 |
|
| 2019 |
Chen PY, DeColli AA, Freel Meyers CL, Drennan CL. X-ray crystallography-based structural elucidation of enzyme-bound intermediates along the 1‑deoxy‑d‑xylulose 5-phosphate synthase reaction coordinate. The Journal of Biological Chemistry. PMID 31239351 DOI: 10.2210/Pdb6Ouv/Pdb |
0.807 |
|
| 2019 |
Bian K, Lenz SAP, Tang Q, Chen F, Qi R, Jost M, Drennan CL, Essigmann JM, Wetmore SD, Li D. DNA repair enzymes ALKBH2, ALKBH3, and AlkB oxidize 5-methylcytosine to 5-hydroxymethylcytosine, 5-formylcytosine and 5-carboxylcytosine in vitro. Nucleic Acids Research. PMID 31114894 DOI: 10.1093/Nar/Gkz395 |
0.381 |
|
| 2019 |
Chen PY, Li B, Drennan CL, Elliott SJ. A reverse TCA cycle 2-oxoacid:ferredoxin oxidoreductase that makes C-C bonds from CO. Joule. 3: 595-611. PMID 31080943 DOI: 10.1016/J.Joule.2018.12.006 |
0.809 |
|
| 2019 |
Rizzolo K, Cohen SE, Weitz AC, López Muñoz MM, Hendrich MP, Drennan CL, Elliott SJ. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Nature Communications. 10: 1101. PMID 30846684 DOI: 10.1038/S41467-019-09020-4 |
0.703 |
|
| 2019 |
Feliciano PR, Drennan CL, Nonato MC. Crystal structures of fumarate hydratases from Leishmania major in a complex with inhibitor 2-thiomalate. Acs Chemical Biology. PMID 30645090 DOI: 10.1021/Acschembio.8B00972 |
0.365 |
|
| 2019 |
Feliciano PR, Drennan CL. Structural and Biochemical Investigations of the [4Fe-4S] Cluster-Containing Fumarate Hydratase fromLeishmania major. Biochemistry. 58: 5011-5021. DOI: 10.2210/Pdb6Unz/Pdb |
0.412 |
|
| 2018 |
Orman M, Bodea S, Funk MA, Campo AM, Bollenbach M, Drennan CL, Balskus EP. Structure-Guided Identification of a Small Molecule That Inhibits Anaerobic Choline Metabolism by Human Gut Bacteria. Journal of the American Chemical Society. PMID 30557011 DOI: 10.2210/Pdb6Nd3/Pdb |
0.596 |
|
| 2018 |
Grell TAJ, Bell BN, Nguyen C, Dowling DP, Bruender NA, Bandarian V, Drennan CL. Crystal structure of AdoMet radical enzyme 7-carboxy-7-deazaguanine synthase from Escherichia coli suggests how modifications near [4Fe-4S] cluster engender flavodoxin specificity. Protein Science : a Publication of the Protein Society. PMID 30341796 DOI: 10.2210/Pdb6Nhl/Pdb |
0.831 |
|
| 2018 |
Wittenborn EC, Merrouch M, Ueda C, Fradale L, Léger C, Fourmond V, Pandelia ME, Dementin S, Drennan CL. Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife. 7. PMID 30277213 DOI: 10.2210/Pdb6B6W/Pdb |
0.802 |
|
| 2018 |
Grell TAJ, Kincannon WM, Bruender NA, Blaesi EJ, Krebs C, Bandarian V, Drennan CL. Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. The Journal of Biological Chemistry. PMID 30217813 DOI: 10.1074/Jbc.Ra118.005369 |
0.516 |
|
| 2018 |
Ryan KS, Drennan CL. Metalloenzymes in natural product biosynthetic pathways. Natural Product Reports. PMID 30009301 DOI: 10.1039/C8Np90023J |
0.61 |
|
| 2018 |
Bridwell-Rabb J, Grell TAJ, Drennan CL. A Rich Man, Poor Man Story of S-Adenosylmethionine and Cobalamin Revisited. Annual Review of Biochemistry. 87: 555-584. PMID 29925255 DOI: 10.1146/Annurev-Biochem-062917-012500 |
0.786 |
|
| 2018 |
Harris N, Born D, Cai W, Huang Y, Martin J, Khalaf R, Drennan C, Zhang W. Isonitrile Formation by a Non-heme Iron(II)-Dependent Oxidase/Decarboxylase. Angewandte Chemie (International Ed. in English). PMID 29906336 DOI: 10.1002/Anie.201804307 |
0.367 |
|
| 2018 |
Nakashige TG, Bowman SEJ, Zygiel EM, Drennan CL, Nolan EM. Biophysical Examination of the Calcium-Modulated Nickel-Binding Properties of Human Calprotectin Reveals Conformational Change in the EF-Hand Domains and His3Asp Site. Biochemistry. PMID 29890074 DOI: 10.1021/Acs.Biochem.8B00415 |
0.323 |
|
| 2018 |
Grell TAJ, Young AP, Drennan CL, Bandarian V. Biochemical and Structural Characterization of a Schiff Base in the Radical-Mediated Biosynthesis of 4-Demethylwyosine by TYW1. Journal of the American Chemical Society. PMID 29792696 DOI: 10.1021/Jacs.8B01493 |
0.464 |
|
| 2018 |
Chen PY, Funk MA, Brignole EJ, Drennan CL. Disruption of an oligomeric interface prevents allosteric inhibition of class Ia ribonucleotide reductase. The Journal of Biological Chemistry. PMID 29700111 DOI: 10.1074/Jbc.Ra118.002569 |
0.786 |
|
| 2018 |
Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from. Proceedings of the National Academy of Sciences of the United States of America. PMID 29581263 DOI: 10.1073/pnas.1722329115 |
0.84 |
|
| 2018 |
Brignole EJ, Tsai KL, Chittuluru J, Li H, Aye Y, Penczek PA, Stubbe J, Drennan CL, Asturias F. 3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound. Elife. 7. PMID 29460780 DOI: 10.7554/Elife.31502 |
0.42 |
|
| 2018 |
Wittenborn EC, Merrouch M, Ueda C, Fradale L, Léger C, Fourmond V, Pandelia M, Dementin S, Drennan CL. Author response: Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase Elife. DOI: 10.7554/Elife.39451.031 |
0.787 |
|
| 2018 |
Grell TAJ, Kincannon WM, Bruender NA, Blaesi EJ, Krebs C, Bandarian V, Drennan CL. Structure of a RiPP maturase, SkfB Journal of Biological Chemistry. DOI: 10.2210/Pdb6Efn/Pdb |
0.32 |
|
| 2018 |
Chen PY, Aman H, Can M, Ragsdale SW, Drennan CL. Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica Proceedings of the National Academy of Sciences of the United States of America. 115: 3846-3851. DOI: 10.2210/Pdb6Cin/Pdb |
0.681 |
|
| 2018 |
Cory SA, Van Vranken JG, Brignole EJ, Patra S, Winge DR, Drennan CL, Rutter J, Barondeau DP. Structure of the human Fe–S cluster assembly sub-complex: implications in Friedreich's ataxia and primary metabolism Acta Crystallographica Section a Foundations and Advances. 74: a80-a80. DOI: 10.1107/S0108767318099191 |
0.702 |
|
| 2017 |
Born DA, Ulrich EC, Ju KS, Peck SC, van der Donk WA, Drennan CL. Structural basis for methylphosphonate biosynthesis. Science (New York, N.Y.). 358: 1336-1339. PMID 29217579 DOI: 10.1126/Science.Aao3435 |
0.601 |
|
| 2017 |
Backman LRF, Funk MA, Dawson CD, Drennan CL. New tricks for the glycyl radical enzyme family. Critical Reviews in Biochemistry and Molecular Biology. 1-22. PMID 28901199 DOI: 10.1080/10409238.2017.1373741 |
0.651 |
|
| 2017 |
Shisler KA, Hutcheson RU, Horitani M, Duschene KS, Crain AV, Byer AS, Shepard EM, Rasmussen A, Yang J, Broderick WE, Vey JL, Drennan CL, Hoffman BM, Broderick JB. Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme. Journal of the American Chemical Society. PMID 28768413 DOI: 10.1021/Jacs.7B04883 |
0.806 |
|
| 2017 |
Cory SA, Van Vranken JG, Brignole EJ, Patra S, Winge DR, Drennan CL, Rutter J, Barondeau DP. Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. Proceedings of the National Academy of Sciences of the United States of America. PMID 28634302 DOI: 10.1073/Pnas.1702849114 |
0.743 |
|
| 2017 |
Nakashige TG, Zygiel EM, Drennan CL, Nolan EM. Nickel Sequestration by the Host-Defense Protein Human Calprotectin. Journal of the American Chemical Society. PMID 28573847 DOI: 10.1021/Jacs.7B01212 |
0.319 |
|
| 2017 |
Lin Q, Parker MJ, Taguchi AT, Ravichandran K, Kim A, Kang G, Shao J, Drennan CL, Stubbe J. Glutamate 52-β at the α/β Subunit Interface of E. coli Class Ia Ribonucleotide Reductase is essential for Conformational Gating of Radical Transfer. The Journal of Biological Chemistry. PMID 28377505 DOI: 10.1074/Jbc.M117.783092 |
0.313 |
|
| 2017 |
Bridwell-Rabb J, Zhong A, Sun HG, Drennan CL, Liu HW. A B12-dependent radical SAM enzyme involved in oxetanocin A biosynthesis. Nature. 544: 322-326. PMID 28346939 DOI: 10.1038/Nature21689 |
0.781 |
|
| 2017 |
Bridwell-Rabb J, Drennan CL. Vitamin B12 in the spotlight again. Current Opinion in Chemical Biology. 37: 63-70. PMID 28167430 DOI: 10.1016/J.Cbpa.2017.01.013 |
0.763 |
|
| 2017 |
Bruender NA, Grell TA, Dowling DP, McCarty RM, Drennan CL, Bandarian V. 7-Carboxy-7-deazaguanine synthase - A radical S-adenosyl-L-methionine enzyme with polar tendencies. Journal of the American Chemical Society. PMID 28045519 DOI: 10.1021/Jacs.6B11381 |
0.672 |
|
| 2017 |
Cory SA, Van Vranken JG, Brignole EJ, Patra S, Winge DR, Drennan CL, Rutter J, Barondeau DP. Structure of human Fe–S assembly sub-complex Acta Crystallographica Section a Foundations and Advances. 73: a113-a113. DOI: 10.1107/S0108767317098877 |
0.68 |
|
| 2016 |
Bridwell-Rabb J, Kang G, Zhong A, Liu HW, Drennan CL. An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 113: 13750-13755. PMID 27849620 DOI: 10.1073/Pnas.1613610113 |
0.787 |
|
| 2016 |
Dowling DP, Kung Y, Croft AK, Taghizadeh K, Kelly WL, Walsh CT, Drennan CL. Structural elements of an NRPS cyclization domain and its intermodule docking domain. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791103 DOI: 10.1073/Pnas.1608615113 |
0.72 |
|
| 2016 |
Wittenborn EC, Jost M, Wei Y, Stubbe J, Drennan CL. Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator. The Journal of Biological Chemistry. PMID 27742839 DOI: 10.1074/Jbc.M116.756833 |
0.822 |
|
| 2016 |
Bodea S, Funk MA, Balskus EP, Drennan CL. Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase. Cell Chemical Biology. PMID 27642068 DOI: 10.1016/J.Chembiol.2016.07.020 |
0.654 |
|
| 2016 |
Dowling DP, Miles ZD, Köhrer C, Maiocco SJ, Elliott SJ, Bandarian V, Drennan CL. Molecular basis of cobalamin-dependent RNA modification. Nucleic Acids Research. PMID 27638883 DOI: 10.1093/Nar/Gkw806 |
0.666 |
|
| 2016 |
Feliciano PR, Drennan CL, Nonato MC. Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold. Proceedings of the National Academy of Sciences of the United States of America. PMID 27528683 DOI: 10.1073/Pnas.1605031113 |
0.486 |
|
| 2016 |
McLaughlin MI, Lanz ND, Goldman PJ, Lee KH, Booker SJ, Drennan CL. Crystallographic snapshots of sulfur insertion by lipoyl synthase. Proceedings of the National Academy of Sciences of the United States of America. PMID 27506792 DOI: 10.1073/Pnas.1602486113 |
0.421 |
|
| 2016 |
Gibson MI, Chen PY, Drennan CL. A structural phylogeny for understanding 2-oxoacid oxidoreductase function. Current Opinion in Structural Biology. 41: 54-61. PMID 27315560 DOI: 10.1016/J.Sbi.2016.05.011 |
0.799 |
|
| 2016 |
Oyala PH, Ravichandran KR, Funk MA, Stucky PA, Stich TA, Drennan CL, Britt RD, Stubbe J. Biophysical characterization of fluorotyrosine probes site-specifically incorporated into enzymes: E. coli ribonucleotide reductase as an example. Journal of the American Chemical Society. PMID 27276098 DOI: 10.1021/Jacs.6B03605 |
0.601 |
|
| 2016 |
Bridwell-Rabb J, Drennan CL. BIOCHEMISTRY. A radically unexpected mechanism. Science (New York, N.Y.). 351: 1266-7. PMID 26989237 DOI: 10.1126/Science.Aaf4942 |
0.774 |
|
| 2016 |
Bowman SE, Bridwell-Rabb J, Drennan CL. Metalloprotein Crystallography: More than a Structure. Accounts of Chemical Research. 49: 695-702. PMID 26975689 DOI: 10.1021/Acs.Accounts.5B00538 |
0.776 |
|
| 2016 |
Chen PY, Wittenborn EC, Drennan CL. Waltzing around cofactors. Elife. 5. PMID 26843316 DOI: 10.7554/Elife.13977 |
0.764 |
|
| 2016 |
Zimanyi CM, Chen PY, Kang G, Funk MA, Drennan CL. Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli. Elife. 5. PMID 26754917 DOI: 10.7554/Elife.07141 |
0.821 |
|
| 2016 |
Ando N, Li H, Brignole EJ, Thompson S, McLaughlin MI, Page JE, Asturias FJ, Stubbe J, Drennan CL. Allosteric Inhibition of Human Ribonucleotide Reductase by dATP Entails the Stabilization of a Hexamer. Biochemistry. PMID 26727048 DOI: 10.1021/Acs.Biochem.5B01207 |
0.545 |
|
| 2015 |
Gibson MI, Chen PY, Johnson AC, Pierce E, Can M, Ragsdale SW, Drennan CL. One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. PMID 26712008 DOI: 10.1073/Pnas.1518537113 |
0.815 |
|
| 2015 |
Bandarian V, Drennan CL. Radical-mediated ring contraction in the biosynthesis of 7-deazapurines. Current Opinion in Structural Biology. 35: 116-124. PMID 26643180 DOI: 10.1016/J.Sbi.2015.11.005 |
0.36 |
|
| 2015 |
Jost M, Fernández-Zapata J, Polanco MC, Ortiz-Guerrero JM, Chen PY, Kang G, Padmanabhan S, Elías-Arnanz M, Drennan CL. Structural basis for gene regulation by a B12-dependent photoreceptor. Nature. PMID 26416754 DOI: 10.1038/Nature14950 |
0.76 |
|
| 2015 |
Jost M, Born DA, Cracan V, Banerjee R, Drennan CL. Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases. The Journal of Biological Chemistry. 290: 26882-98. PMID 26318610 DOI: 10.1074/Jbc.M115.676890 |
0.489 |
|
| 2015 |
Funk MA, Marsh EN, Drennan CL. Substrate-bound Structures of Benzylsuccinate Synthase Reveal How Toluene Is Activated in Anaerobic Hydrocarbon Degradation. The Journal of Biological Chemistry. 290: 22398-22408. PMID 26224635 DOI: 10.1074/Jbc.M115.670737 |
0.689 |
|
| 2015 |
Gibson MI, Brignole EJ, Pierce E, Can M, Ragsdale SW, Drennan CL. The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism. Biochemistry. 54: 4112-20. PMID 26061898 DOI: 10.1021/Acs.Biochem.5B00521 |
0.652 |
|
| 2015 |
Mattaini KR, Brignole EJ, Kini M, Davidson SM, Fiske BP, Drennan CL, Vander Heiden MG. An epitope tag alters phosphoglycerate dehydrogenase structure and impairs ability to support cell proliferation. Cancer & Metabolism. 3: 5. PMID 25926973 DOI: 10.1186/S40170-015-0131-7 |
0.409 |
|
| 2015 |
Bewley KD, Dey M, Bjork RE, Mitra S, Chobot SE, Drennan CL, Elliott SJ. Rheostat re-wired: alternative hypotheses for the control of thioredoxin reduction potentials. Plos One. 10: e0122466. PMID 25874934 DOI: 10.1371/Journal.Pone.0122466 |
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| 2015 |
Jost M, Cracan V, Hubbard PA, Banerjee R, Drennan CL. Visualization of a radical B12 enzyme with its G-protein chaperone. Proceedings of the National Academy of Sciences of the United States of America. 112: 2419-24. PMID 25675500 DOI: 10.1073/Pnas.1419582112 |
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| 2015 |
Gagnon DM, Brophy MB, Bowman SE, Stich TA, Drennan CL, Britt RD, Nolan EM. Manganese binding properties of human calprotectin under conditions of high and low calcium: X-ray crystallographic and advanced electron paramagnetic resonance spectroscopic analysis. Journal of the American Chemical Society. 137: 3004-16. PMID 25597447 DOI: 10.1021/Ja512204S |
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| 2015 |
Grell TA, Goldman PJ, Drennan CL. SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes. The Journal of Biological Chemistry. 290: 3964-71. PMID 25477505 DOI: 10.1074/Jbc.R114.581249 |
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| 2015 |
Brignole E, Wittenborn E, Thompson S, Ragsdale S, Drennan C. Dramatic Conformational Flexibility of Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Revealed by Electron Microscopy The Faseb Journal. 29. DOI: 10.1096/Fasebj.29.1_Supplement.573.37 |
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| 2014 |
Liu DS, Nivón LG, Richter F, Goldman PJ, Deerinck TJ, Yao JZ, Richardson D, Phipps WS, Ye AZ, Ellisman MH, Drennan CL, Baker D, Ting AY. Computational design of a red fluorophore ligase for site-specific protein labeling in living cells. Proceedings of the National Academy of Sciences of the United States of America. 111: E4551-9. PMID 25313043 DOI: 10.1073/Pnas.1404736111 |
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| 2014 |
Setser JW, Heemstra JR, Walsh CT, Drennan CL. Crystallographic evidence of drastic conformational changes in the active site of a flavin-dependent N-hydroxylase. Biochemistry. 53: 6063-77. PMID 25184411 DOI: 10.1021/Bi500655Q |
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| 2014 |
Wei Y, Funk MA, Rosado LA, Baek J, Drennan CL, Stubbe J. The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proceedings of the National Academy of Sciences of the United States of America. 111: E3756-65. PMID 25157154 DOI: 10.1073/Pnas.1414396111 |
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| 2014 |
Funk MA, Judd ET, Marsh EN, Elliott SJ, Drennan CL. Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity. Proceedings of the National Academy of Sciences of the United States of America. 111: 10161-6. PMID 24982148 DOI: 10.1073/Pnas.1405983111 |
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| 2014 |
Dowling DP, Bruender NA, Young AP, McCarty RM, Bandarian V, Drennan CL. Radical SAM enzyme QueE defines a new minimal core fold and metal-dependent mechanism. Nature Chemical Biology. 10: 106-12. PMID 24362703 DOI: 10.1038/Nchembio.1426 |
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| 2014 |
Ullman O, Zimanyi CM, Drennan CL, Stultz CM. Finding the Missing Link - Modeling the Conformational Space of the Active and Inactive forms of E. Coli Ribonucleotide Reductase Biophysical Journal. 106: 52a. DOI: 10.1016/J.Bpj.2013.11.368 |
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| 2013 |
Sydor AM, Jost M, Ryan KS, Turo KE, Douglas CD, Drennan CL, Zamble DB. Metal binding properties of Escherichia coli YjiA, a member of the metal homeostasis-associated COG0523 family of GTPases. Biochemistry. 52: 1788-1801. PMID 24449932 DOI: 10.1021/Bi301600Z |
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| 2013 |
Goldman PJ, Grove TL, Booker SJ, Drennan CL. X-ray analysis of butirosin biosynthetic enzyme BtrN redefines structural motifs for AdoMet radical chemistry. Proceedings of the National Academy of Sciences of the United States of America. 110: 15949-54. PMID 24048029 DOI: 10.1073/Pnas.1312228110 |
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| 2013 |
Goldman PJ, Grove TL, Sites LA, McLaughlin MI, Booker SJ, Drennan CL. X-ray structure of an AdoMet radical activase reveals an anaerobic solution for formylglycine posttranslational modification. Proceedings of the National Academy of Sciences of the United States of America. 110: 8519-24. PMID 23650368 DOI: 10.1073/Pnas.1302417110 |
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| 2013 |
Chang WC, Dey M, Liu P, Mansoorabadi SO, Moon SJ, Zhao ZK, Drennan CL, Liu HW. Mechanistic studies of an unprecedented enzyme-catalysed 1,2-phosphono-migration reaction. Nature. 496: 114-8. PMID 23552950 DOI: 10.1038/Nature11998 |
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| 2013 |
Kulik HJ, Drennan CL. Substrate placement influences reactivity in non-heme Fe(II) halogenases and hydroxylases. The Journal of Biological Chemistry. 288: 11233-41. PMID 23449977 DOI: 10.1074/Jbc.M112.415570 |
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| 2013 |
Minnihan EC, Ando N, Brignole EJ, Olshansky L, Chittuluru J, Asturias FJ, Drennan CL, Nocera DG, Stubbe J. Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase. Proceedings of the National Academy of Sciences of the United States of America. 110: 3835-40. PMID 23431160 DOI: 10.1073/Pnas.1220691110 |
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| 2013 |
Maiocco SJ, Grove T, Goldman P, Booker S, Drennan C, Elliott S. Electrochemical investigation of a radical sadenosylmethionine enzyme: BtrN from Bacillus circulans The Faseb Journal. 27. DOI: 10.1096/Fasebj.27.1_Supplement.Lb57 |
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| 2013 |
Sydor AM, Jost M, Ryan KS, Turo KE, Douglas CD, Drennan CL, Zamble DB. Correction to Metal Binding Properties of Escherichia coli YjiA, a Member of the Metal Homeostasis-Associated COG0523 Family of GTPases Biochemistry. 52: 4105-4105. DOI: 10.1021/Bi4006094 |
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| 2012 |
Hamill MJ, Jost M, Wong C, Bene NC, Drennan CL, Elliott SJ. Electrochemical characterization of Escherichia coli adaptive response protein AidB. International Journal of Molecular Sciences. 13: 16899-915. PMID 23443126 DOI: 10.3390/Ijms131216899 |
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| 2012 |
Bewley KD, Firer-Sherwood MA, Mock JY, Ando N, Drennan CL, Elliott SJ. Mind the gap: diversity and reactivity relationships among multihaem cytochromes of the MtrA/DmsE family. Biochemical Society Transactions. 40: 1268-73. PMID 23176466 DOI: 10.1042/Bst20120106 |
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| 2012 |
Ando N, Kung Y, Can M, Bender G, Ragsdale SW, Drennan CL. Transient B12-dependent methyltransferase complexes revealed by small-angle X-ray scattering. Journal of the American Chemical Society. 134: 17945-54. PMID 23051056 DOI: 10.1021/Ja3055782 |
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| 2012 |
Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, Elliott SJ, Drennan CL. An unusual role for a mobile flavin in StaC-like indolocarbazole biosynthetic enzymes. Chemistry & Biology. 19: 855-65. PMID 22840773 DOI: 10.1016/J.Chembiol.2012.05.016 |
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| 2012 |
Aye Y, Brignole EJ, Long MJ, Chittuluru J, Drennan CL, Asturias FJ, Stubbe J. Clofarabine targets the large subunit (α) of human ribonucleotide reductase in live cells by assembly into persistent hexamers. Chemistry & Biology. 19: 799-805. PMID 22840768 DOI: 10.1016/J.Chembiol.2012.05.015 |
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| 2012 |
Zimanyi CM, Ando N, Brignole EJ, Asturias FJ, Stubbe J, Drennan CL. Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase. Structure (London, England : 1993). 20: 1374-83. PMID 22727814 DOI: 10.1016/J.Str.2012.05.009 |
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Brignole EJ, Ando N, Zimanyi CM, Drennan CL. The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years. Biochemical Society Transactions. 40: 523-30. PMID 22616862 DOI: 10.1042/Bst20120081 |
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Ragsdale SW, Yi L, Bender G, Gupta N, Kung Y, Yan L, Stich TA, Doukov T, Leichert L, Jenkins PM, Bianchetti CM, George SJ, Cramer SP, Britt RD, Jakob U, ... ... Drennan CL, et al. Redox, haem and CO in enzymatic catalysis and regulation. Biochemical Society Transactions. 40: 501-7. PMID 22616859 DOI: 10.1042/Bst20120083 |
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Dowling DP, Vey JL, Croft AK, Drennan CL. Structural diversity in the AdoMet radical enzyme superfamily. Biochimica Et Biophysica Acta. 1824: 1178-95. PMID 22579873 DOI: 10.1016/J.Bbapap.2012.04.006 |
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Dowling DP, Croft AK, Drennan CL. Radical use of Rossmann and TIM barrel architectures for controlling coenzyme B12 chemistry. Annual Review of Biophysics. 41: 403-27. PMID 22577824 DOI: 10.1146/Annurev-Biophys-050511-102225 |
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Li D, Delaney JC, Page CM, Yang X, Chen AS, Wong C, Drennan CL, Essigmann JM. Exocyclic carbons adjacent to the N6 of adenine are targets for oxidation by the Escherichia coli adaptive response protein AlkB. Journal of the American Chemical Society. 134: 8896-901. PMID 22512456 DOI: 10.1021/Ja3010094 |
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Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, Drennan CL. Visualizing molecular juggling within a B12-dependent methyltransferase complex. Nature. 484: 265-9. PMID 22419154 DOI: 10.1038/Nature10916 |
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Bowman S, Drennan CL, Stultz CM. Probing the Nickel Coordination Environment in Helicobacter Pylori NikR Biophysical Journal. 102: 252a. DOI: 10.1016/J.Bpj.2011.11.1390 |
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Ando N, Brignole EJ, Zimanyi CM, Funk MA, Yokoyama K, Asturias FJ, Stubbe J, Drennan CL. Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase. Proceedings of the National Academy of Sciences of the United States of America. 108: 21046-51. PMID 22160671 DOI: 10.1073/Pnas.1112715108 |
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Hamill MJ, Jost M, Wong C, Elliott SJ, Drennan CL. Flavin-induced oligomerization in Escherichia coli adaptive response protein AidB. Biochemistry. 50: 10159-69. PMID 22004173 DOI: 10.1021/Bi201340T |
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Firer-Sherwood MA, Ando N, Drennan CL, Elliott SJ. Solution-based structural analysis of the decaheme cytochrome, MtrA, by small-angle X-ray scattering and analytical ultracentrifugation. The Journal of Physical Chemistry. B. 115: 11208-14. PMID 21838277 DOI: 10.1021/Jp203603R |
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| 2011 |
Yun D, Dey M, Higgins LJ, Yan F, Liu HW, Drennan CL. Structural basis of regiospecificity of a mononuclear iron enzyme in antibiotic fosfomycin biosynthesis. Journal of the American Chemical Society. 133: 11262-9. PMID 21682308 DOI: 10.1021/Ja2025728 |
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| 2011 |
Vey JL, Drennan CL. Structural insights into radical generation by the radical SAM superfamily. Chemical Reviews. 111: 2487-506. PMID 21370834 DOI: 10.1021/Cr9002616 |
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| 2011 |
Lingaraju GM, Davis CA, Setser JW, Samson LD, Drennan CL. Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3,N4-ethenocytosine-containing DNA. The Journal of Biological Chemistry. 286: 13205-13. PMID 21349833 DOI: 10.1074/Jbc.M110.192435 |
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Kung Y, Drennan CL. A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization. Current Opinion in Chemical Biology. 15: 276-83. PMID 21130022 DOI: 10.1016/J.Cbpa.2010.11.005 |
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Li D, Delaney JC, Page CM, Chen AS, Wong C, Drennan CL, Essigmann JM. Repair of DNA Alkylation Damage by the Escherichia coli Adaptive Response Protein AlkB as Studied by ESI-TOF Mass Spectrometry. Journal of Nucleic Acids. 2010: 369434. PMID 21048928 DOI: 10.4061/2010/369434 |
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Phillips CM, Schreiter ER, Stultz CM, Drennan CL. Structural basis of low-affinity nickel binding to the nickel-responsive transcription factor NikR from Escherichia coli. Biochemistry. 49: 7830-8. PMID 20704276 DOI: 10.1021/Bi100923J |
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Kulik HJ, Blasiak LC, Marzari N, Drennan CL. First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity. Journal of the American Chemical Society. 131: 14426-33. PMID 19807187 DOI: 10.1016/J.Bpj.2009.12.2453 |
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| 2009 |
Phillips CM, Nerenberg PS, Drennan CL, Stultz CM. Physical basis of metal-binding specificity in Escherichia coli NikR. Journal of the American Chemical Society. 131: 10220-8. PMID 19621966 DOI: 10.1021/Ja9026314 |
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Kung Y, Doukov TI, Seravalli J, Ragsdale SW, Drennan CL. Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 48: 7432-40. PMID 19583207 DOI: 10.1021/Bi900574H |
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| 2009 |
Ryan KS, Drennan CL. Divergent pathways in the biosynthesis of bisindole natural products. Chemistry & Biology. 16: 351-64. PMID 19389622 DOI: 10.1016/J.Chembiol.2009.01.017 |
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| 2009 |
Wong C, Fujimori DG, Walsh CT, Drennan CL. Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. Journal of the American Chemical Society. 131: 4872-9. PMID 19281171 DOI: 10.1021/Ja8097355 |
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| 2009 |
Blasiak LC, Drennan CL. Structural perspective on enzymatic halogenation. Accounts of Chemical Research. 42: 147-55. PMID 18774824 DOI: 10.1021/Ar800088R |
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| 2009 |
Phillips CM, Nerenberg PS, Drennan CL, Stultz CM. Metal Preference At The Second Metal Binding Site Of E. coli NikR Biophysical Journal. 96: 58a. DOI: 10.1016/J.Bpj.2008.12.196 |
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| 2008 |
Ryan KS, Chakraborty S, Howard-Jones AR, Walsh CT, Ballou DP, Drennan CL. The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction. Biochemistry. 47: 13506-13. PMID 19035832 DOI: 10.1021/Bi801229W |
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| 2008 |
Vey JL, Yang J, Li M, Broderick WE, Broderick JB, Drennan CL. Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme. Proceedings of the National Academy of Sciences of the United States of America. 105: 16137-41. PMID 18852451 DOI: 10.1073/Pnas.0806640105 |
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| 2008 |
Hamill MJ, Chobot SE, Hernandez HH, Drennan CL, Elliott SJ. Direct electrochemical analyses of a thermophilic thioredoxin reductase: interplay between conformational change and redox chemistry. Biochemistry. 47: 9738-46. PMID 18717594 DOI: 10.1021/Bi800676G |
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| 2008 |
Hernandez HH, Jaquez OA, Hamill MJ, Elliott SJ, Drennan CL. Thioredoxin reductase from Thermoplasma acidophilum: a new twist on redox regulation. Biochemistry. 47: 9728-37. PMID 18717593 DOI: 10.1021/Bi8006753 |
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Doukov TI, Blasiak LC, Seravalli J, Ragsdale SW, Drennan CL. Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry. 47: 3474-83. PMID 18293927 DOI: 10.1021/Bi702386T |
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| 2008 |
Phillips CM, Schreiter ER, Guo Y, Wang SC, Zamble DB, Drennan CL. Structural basis of the metal specificity for nickel regulatory protein NikR. Biochemistry. 47: 1938-46. PMID 18193897 DOI: 10.1021/Bi702006H |
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| 2008 |
Ryan KS, Balibar CJ, Turo KE, Walsh CT, Drennan CL. The violacein biosynthetic enzyme VioE shares a fold with lipoprotein transporter proteins. The Journal of Biological Chemistry. 283: 6467-75. PMID 18171675 DOI: 10.1074/Jbc.M708573200 |
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| 2007 |
Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL. Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC. Proceedings of the National Academy of Sciences of the United States of America. 104: 15311-6. PMID 17873060 DOI: 10.1073/Pnas.0707190104 |
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| 2007 |
Hubbard PA, Padovani D, Labunska T, Mahlstedt SA, Banerjee R, Drennan CL. Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria. The Journal of Biological Chemistry. 282: 31308-16. PMID 17728257 DOI: 10.1074/Jbc.M704850200 |
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Schreiter ER, Drennan CL. Ribbon-helix-helix transcription factors: variations on a theme. Nature Reviews. Microbiology. 5: 710-20. PMID 17676053 DOI: 10.1038/Nrmicro1717 |
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Yeh E, Blasiak LC, Koglin A, Drennan CL, Walsh CT. Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases. Biochemistry. 46: 1284-92. PMID 17260957 DOI: 10.1021/Bi0621213 |
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Frick LE, Delaney JC, Wong C, Drennan CL, Essigmann JM. Alleviation of 1,N6-ethanoadenine genotoxicity by the Escherichia coli adaptive response protein AlkB. Proceedings of the National Academy of Sciences of the United States of America. 104: 755-60. PMID 17213319 DOI: 10.1073/Pnas.0607377104 |
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Doukov TI, Hemmi H, Drennan CL, Ragsdale SW. Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases. The Journal of Biological Chemistry. 282: 6609-18. PMID 17172470 DOI: 10.1074/Jbc.M609828200 |
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Schreiter ER, Wang SC, Zamble DB, Drennan CL. NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proceedings of the National Academy of Sciences of the United States of America. 103: 13676-81. PMID 16945905 DOI: 10.1073/Pnas.0606247103 |
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Blasiak LC, Vaillancourt FH, Walsh CT, Drennan CL. Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Nature. 440: 368-71. PMID 16541079 DOI: 10.1038/Nature04544 |
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Delaney JC, Smeester L, Wong C, Frick LE, Taghizadeh K, Wishnok JS, Drennan CL, Samson LD, Essigmann JM. AlkB reverses etheno DNA lesions caused by lipid oxidation in vitro and in vivo. Nature Structural & Molecular Biology. 12: 855-60. PMID 16200073 DOI: 10.1038/Nsmb996 |
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| 2005 |
Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature. 437: 838-44. PMID 16015285 DOI: 10.1038/Nature03924 |
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| 2005 |
Andrade SL, Cruz F, Drennan CL, Ramakrishnan V, Rees DC, Ferry JG, Einsle O. Structures of the iron-sulfur flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus. Journal of Bacteriology. 187: 3848-54. PMID 15901710 DOI: 10.1128/Jb.187.11.3848-3854.2005 |
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| 2004 |
Berkovitch F, Behshad E, Tang KH, Enns EA, Frey PA, Drennan CL. A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase. Proceedings of the National Academy of Sciences of the United States of America. 101: 15870-5. PMID 15514022 DOI: 10.1073/Pnas.0407074101 |
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| 2004 |
Midelfort KS, Hernandez HH, Lippow SM, Tidor B, Drennan CL, Wittrup KD. Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. Journal of Molecular Biology. 343: 685-701. PMID 15465055 DOI: 10.1016/J.Jmb.2004.08.019 |
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| 2004 |
Tirupati B, Vey JL, Drennan CL, Bollinger JM. Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803. Biochemistry. 43: 12210-9. PMID 15379559 DOI: 10.1021/Bi0491447 |
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Nicolet Y, Drennan CL. AdoMet radical proteins--from structure to evolution--alignment of divergent protein sequences reveals strong secondary structure element conservation. Nucleic Acids Research. 32: 4015-25. PMID 15289575 DOI: 10.1093/Nar/Gkh728 |
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Drennan CL, Doukov TI, Ragsdale SW. The metalloclusters of carbon monoxide dehydrogenase/acetyl-CoA synthase: a story in pictures. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 511-5. PMID 15221484 DOI: 10.1007/S00775-004-0563-Y |
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Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science (New York, N.Y.). 303: 76-9. PMID 14704425 DOI: 10.1126/Science.1088493 |
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Schreiter ER, Sintchak MD, Guo Y, Chivers PT, Sauer RT, Drennan CL. Crystal structure of the nickel-responsive transcription factor NikR. Nature Structural Biology. 10: 794-9. PMID 12970756 DOI: 10.1038/Nsb985 |
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Drennan CL, Peters JW. Surprising cofactors in metalloenzymes. Current Opinion in Structural Biology. 13: 220-6. PMID 12727516 DOI: 10.1016/S0959-440X(03)00038-1 |
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Drennan CL, Schreiter E, Doukov TI, Chivers PT, Seravalli J, Ragsdale SW. Unique nickel sites in proteins Journal of Inorganic Biochemistry. 96: 47. DOI: 10.1016/S0162-0134(03)80485-3 |
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Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science (New York, N.Y.). 298: 567-72. PMID 12386327 DOI: 10.1126/Science.1075843 |
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Sintchak MD, Arjara G, Kellogg BA, Stubbe J, Drennan CL. The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Nature Structural Biology. 9: 293-300. PMID 11875520 DOI: 10.1038/Nsb774 |
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Drennan CL, Sintchak MD, Arjara G, Kellogg BA, Stubbe J. Crystal structure of class II ribonucleotide reductase: how an allosterically regulated monomer mimics a dimer Acta Crystallographica Section a Foundations of Crystallography. 58: c193-c193. DOI: 10.1107/S0108767302092723 |
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Drennan CL, Heo J, Sintchak MD, Schreiter E, Ludden PW. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 98: 11973-8. PMID 11593006 DOI: 10.1073/Pnas.211429998 |
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Marsh EN, Drennan CL. Adenosylcobalamin-dependent isomerases: new insights into structure and mechanism. Current Opinion in Chemical Biology. 5: 499-505. PMID 11578922 DOI: 10.1016/S1367-5931(00)00238-6 |
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Hoover DM, Drennan CL, Metzger AL, Osborne C, Weber CH, Pattridge KA, Ludwig ML. Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials. Journal of Molecular Biology. 294: 725-43. PMID 10610792 DOI: 10.1006/Jmbi.1999.3152 |
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Drennan CL, Pattridge KA, Weber CH, Metzger AL, Hoover DM, Ludwig ML. Refined structures of oxidized flavodoxin from Anacystis nidulans. Journal of Molecular Biology. 294: 711-24. PMID 10610791 DOI: 10.1006/Jmbi.1999.3151 |
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Jarrett JT, Drennan CL, Amaratunga M, Scholten JD, Ludwig ML, Matthews RG. A protein radical cage slows photolysis of methylcobalamin in methionine synthase from Escherichia coli. Bioorganic & Medicinal Chemistry. 4: 1237-46. PMID 8879545 DOI: 10.1016/0968-0896(96)00119-8 |
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Ludwig ML, Drennan CL, Matthews RG. The reactivity of B12 cofactors: the proteins make a difference. Structure (London, England : 1993). 4: 505-12. PMID 8736549 DOI: 10.1016/S0969-2126(96)00056-1 |
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Jarrett JT, Amaratunga M, Drennan CL, Scholten JD, Sands RH, Ludwig ML, Matthews RG. Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity. Biochemistry. 35: 2464-75. PMID 8652590 DOI: 10.1021/Bi952389M |
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Amaratunga M, Fluhr K, Jarrett JT, Drennan CL, Ludwig ML, Matthews RG, Scholten JD. A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: initial characterization of seven mutant proteins. Biochemistry. 35: 2453-63. PMID 8652589 DOI: 10.1021/Bi952388U |
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| 1996 |
Drennan CL, Matthews RG, Rosenblatt DS, Ledley FD, Fenton WA, Ludwig ML. Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 93: 5550-5. PMID 8643613 DOI: 10.1073/Pnas.93.11.5550 |
0.632 |
|
| 1996 |
Drennan CL. Cobalamin-dependent methionine synthase: piecing together the structure of a large enzyme Faseb Journal. 10: A1112. |
0.316 |
|
| 1996 |
Jarrett JT, Hoover DM, Drennan CL, Ludwig ML, Matthews BG. Protein residues control methylcobalamin reactivity in methionine synthase Faseb Journal. 10: A968. |
0.535 |
|
| 1994 |
Drennan CL, Huang S, Drummond JT, Matthews RG, Lidwig ML. How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase. Science (New York, N.Y.). 266: 1669-74. PMID 7992050 DOI: 10.1126/Science.7992050 |
0.406 |
|
| 1994 |
Drennan CL, Matthews RG, Ludwig ML. Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes. Current Opinion in Structural Biology. 4: 919-29. PMID 7712296 DOI: 10.1016/0959-440X(94)90275-5 |
0.675 |
|
| 1994 |
Drennan CL, Huang S, Drummond JT, Matthews RG, Ludwig ML. How a Protein Binds B 12 : A 3.0 overset{circ}{A} X-ray Structure of B 12 Domains of Methionine Synthase Science. 266: 1669-1674. DOI: 10.1126/Science.266.5191.1669 |
0.589 |
|
| Show low-probability matches. |
