Year |
Citation |
Score |
2023 |
Hoang T-M, Huang W, Gans J, Weiner J, Nowak E, Barbier M, Wilks A, Kane MA, Oglesby AG. The heme-responsive PrrH sRNA regulates pyochelin gene expression. Msphere. 8: e0039223. PMID 37800921 DOI: 10.1128/msphere.00392-23 |
0.497 |
|
2023 |
Hoang TM, Huang W, Gans J, Nowak E, Barbier M, Wilks A, Kane MA, Oglesby AG. The heme-responsive PrrH sRNA regulates pyochelin gene expression. Biorxiv : the Preprint Server For Biology. PMID 36712080 DOI: 10.1101/2023.01.19.524833 |
0.42 |
|
2021 |
Mouriño S, Wilks A. Extracellular haem utilization by the opportunistic pathogen Pseudomonas aeruginosa and its role in virulence and pathogenesis. Advances in Microbial Physiology. 79: 89-132. PMID 34836613 DOI: 10.1016/bs.ampbs.2021.07.004 |
0.477 |
|
2021 |
Kihn KC, Wilson T, Smith AK, Bradshaw RT, Wintrode PL, Forrest LR, Wilks A, Deredge DJ. Modeling the native ensemble of PhuS using enhanced sampling MD and HDX-ensemble reweighting. Biophysical Journal. PMID 34767787 DOI: 10.1016/j.bpj.2021.11.010 |
0.366 |
|
2021 |
Dent AT, Brimberry M, Albert T, Lanzilotta WN, Moënne-Loccoz P, Wilks A. Axial Heme Coordination by the Tyr-His Motif in the Extracellular Hemophore HasAp Is Critical for the Release of Heme to the HasR Receptor of . Biochemistry. PMID 34324310 DOI: 10.1021/acs.biochem.1c00389 |
0.332 |
|
2021 |
Robinson EA, Wilks A, Xue F. Repurposing Acitretin as an Antipseudomonal Agent Targeting the Iron-Regulated Heme Oxygenase. Biochemistry. PMID 33621054 DOI: 10.1021/acs.biochem.0c00895 |
0.449 |
|
2021 |
Wilson T, Mouriño S, Wilks A. The heme binding protein PhuS transcriptionally regulates the Pseudomonas aeruginosa tandem sRNA prrF1,F2 locus. The Journal of Biological Chemistry. 100275. PMID 33428928 DOI: 10.1016/j.jbc.2021.100275 |
0.549 |
|
2020 |
Centola G, Xue F, Wilks A. Metallotherapeutics development in the age of iron-clad bacteria. Metallomics : Integrated Biometal Science. PMID 33242314 DOI: 10.1039/d0mt00206b |
0.392 |
|
2020 |
Centola G, Deredge D, Hom K, Ai Y, Dent A, Xue F, Wilks A. Gallium (III) Salophen as a Dual Inhibitor of Pseudomonas aeruginosa Heme Sensing and Iron Acquisition. Acs Infectious Diseases. PMID 32551497 DOI: 10.1021/Acsinfecdis.0C00138 |
0.541 |
|
2020 |
Dent AT, Wilks A. Contributions of the heme coordinating ligands of the Pseudomonas aeruginosa outer membrane receptor HasR to extracellular heme sensing and transport. The Journal of Biological Chemistry. PMID 32522817 DOI: 10.1074/Jbc.Ra120.014081 |
0.461 |
|
2019 |
Giardina BJ, Shahzad S, Huang W, Wilks A. Heme uptake and utilization by hypervirulent Acinetobacter baumannii LAC-4 is dependent on a canonical heme oxygenase (abHemO). Archives of Biochemistry and Biophysics. 108066. PMID 31398314 DOI: 10.1016/J.Abb.2019.108066 |
0.54 |
|
2019 |
Nelson CE, Huang W, Brewer LK, Nguyen AT, Kane MA, Wilks A, Oglesby-Sherrouse AG. Proteomic analysis of the iron starvation response reveals PrrF sRNA-dependent iron regulation of twitching motility, amino acid metabolism, and zinc homeostasis proteins. Journal of Bacteriology. PMID 30962354 DOI: 10.1128/Jb.00754-18 |
0.568 |
|
2018 |
Dent AT, Mouriño S, Huang W, Wilks A. Post-transcriptional regulation of the Pseudomonas aeruginosa heme assimilation system (Has) fine-tunes extracellular heme sensing. The Journal of Biological Chemistry. PMID 30593511 DOI: 10.1074/Jbc.Ra118.006185 |
0.438 |
|
2018 |
Heinzl GA, Huang W, Robinson E, Xue F, Möenne-Loccoz P, Wilks A. The Asp99-Arg188 salt bridge of the Pseudomonas aeruginosa HemO is critical in allowing conformational flexibility during catalysis. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 30194537 DOI: 10.1007/S00775-018-1609-X |
0.504 |
|
2017 |
Huang W, Brewer LK, Jones JW, Nguyen AT, Marcu A, Wishart DS, Oglesby-Sherrouse AG, Kane MA, Wilks A. PAMDB: a comprehensive Pseudomonas aeruginosa metabolome database. Nucleic Acids Research. PMID 29106626 DOI: 10.1093/Nar/Gkx1061 |
0.337 |
|
2017 |
Huang W, Wilks A. A rapid seamless method for gene knockout in Pseudomonas aeruginosa. Bmc Microbiology. 17: 199. PMID 28927382 DOI: 10.1186/S12866-017-1112-5 |
0.307 |
|
2017 |
Huang W, Wilks A. Extracellular Heme Uptake and the Challenge of Bacterial Cell Membranes. Annual Review of Biochemistry. PMID 28426241 DOI: 10.1146/annurev-biochem-060815-014214 |
0.467 |
|
2017 |
Deredge DJ, Huang W, Hui C, Matsumura H, Yue Z, Moënne-Loccoz P, Shen J, Wintrode PL, Wilks A. Ligand-induced allostery in the interaction of the Pseudomonas aeruginosa heme binding protein with heme oxygenase. Proceedings of the National Academy of Sciences of the United States of America. PMID 28289188 DOI: 10.1073/Pnas.1606931114 |
0.359 |
|
2016 |
Damron FH, Oglesby-Sherrouse AG, Wilks A, Barbier M. Dual-seq transcriptomics reveals the battle for iron during Pseudomonas aeruginosa acute murine pneumonia. Scientific Reports. 6: 39172. PMID 27982111 DOI: 10.1038/Srep39172 |
0.47 |
|
2016 |
Mourino S, Giardina BJ, Reyes-Caballero H, Wilks A. Metabolite Driven Regulation of Heme Uptake by the Biliverdin IXβ/δ Selective HemO of Pseudomonas aeruginosa. The Journal of Biological Chemistry. PMID 27493207 DOI: 10.1074/Jbc.M116.728527 |
0.543 |
|
2016 |
Heinzl GA, Huang W, Yu W, Giardina BJ, Zhou Y, MacKerell AD, Wilks A, Xue F. Iminoguanidines as Allosteric Inhibitors of the Iron-Regulated Heme Oxygenase (HemO) of Pseudomonas aeruginosa. Journal of Medicinal Chemistry. PMID 27353344 DOI: 10.1021/Acs.Jmedchem.6B00757 |
0.524 |
|
2016 |
Deredge DJ, Huang W, Hui C, Moenne-Loccoz P, Wilks A, Wintrode P. Ligand Induced Allostery in Pseudomonas Aeruginosa Cytoplasmic Heme Binding Protein (Phus) Drives the Protein-Protein Interaction with Heme Oxygenase Biophysical Journal. 110: 221a. DOI: 10.1016/J.Bpj.2015.11.1225 |
0.409 |
|
2015 |
Smith AD, Modi AR, Sun S, Dawson JH, Wilks A. Spectroscopic Determination of Distinct Heme Ligands in Outer-Membrane Receptors PhuR and HasR of Pseudomonas aeruginosa. Biochemistry. 54: 2601-12. PMID 25849630 DOI: 10.1021/Acs.Biochem.5B00017 |
0.419 |
|
2015 |
Smith AD, Wilks A. Differential contributions of the outer membrane receptors PhuR and HasR to heme acquisition in Pseudomonas aeruginosa. The Journal of Biological Chemistry. 290: 7756-66. PMID 25616666 DOI: 10.1074/Jbc.M114.633495 |
0.452 |
|
2015 |
Reinhart AA, Powell DA, Nguyen AT, O'Neill M, Djapgne L, Wilks A, Ernst RK, Oglesby-Sherrouse AG. The prrF-encoded small regulatory RNAs are required for iron homeostasis and virulence of Pseudomonas aeruginosa. Infection and Immunity. 83: 863-75. PMID 25510881 DOI: 10.1128/Iai.02707-14 |
0.674 |
|
2014 |
Wilks A, Ikeda-Saito M. Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin. Accounts of Chemical Research. 47: 2291-8. PMID 24873177 DOI: 10.1021/Ar500028N |
0.552 |
|
2014 |
Nguyen AT, O'Neill MJ, Watts AM, Robson CL, Lamont IL, Wilks A, Oglesby-Sherrouse AG. Adaptation of iron homeostasis pathways by a Pseudomonas aeruginosa pyoverdine mutant in the cystic fibrosis lung. Journal of Bacteriology. 196: 2265-76. PMID 24727222 DOI: 10.1128/Jb.01491-14 |
0.613 |
|
2014 |
Wilks A, Heinzl G. Heme oxygenation and the widening paradigm of heme degradation. Archives of Biochemistry and Biophysics. 544: 87-95. PMID 24161941 DOI: 10.1016/J.Abb.2013.10.013 |
0.503 |
|
2013 |
Tripathi S, O'Neill MJ, Wilks A, Poulos TL. Crystal structure of the Pseudomonas aeruginosa cytoplasmic heme binding protein, Apo-PhuS. Journal of Inorganic Biochemistry. 128: 131-6. PMID 23973453 DOI: 10.1016/J.Jinorgbio.2013.07.030 |
0.672 |
|
2013 |
O'Neill MJ, Wilks A. The P. aeruginosa heme binding protein PhuS is a heme oxygenase titratable regulator of heme uptake. Acs Chemical Biology. 8: 1794-802. PMID 23947366 DOI: 10.1021/Cb400165B |
0.677 |
|
2013 |
Hom K, Heinzl GA, Eakanunkul S, Lopes PE, Xue F, MacKerell AD, Wilks A. Small molecule antivirulents targeting the iron-regulated heme oxygenase (HemO) of P. aeruginosa. Journal of Medicinal Chemistry. 56: 2097-109. PMID 23379514 DOI: 10.1021/Jm301819K |
0.444 |
|
2012 |
Smith AD, Wilks A. Extracellular heme uptake and the challenges of bacterial cell membranes. Current Topics in Membranes. 69: 359-92. PMID 23046657 DOI: 10.1016/B978-0-12-394390-3.00013-6 |
0.569 |
|
2012 |
Barker KD, Barkovits K, Wilks A. Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO). The Journal of Biological Chemistry. 287: 18342-50. PMID 22493498 DOI: 10.1074/Jbc.M112.359265 |
0.597 |
|
2012 |
O'Neill MJ, Bhakta MN, Fleming KG, Wilks A. Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO). Proceedings of the National Academy of Sciences of the United States of America. 109: 5639-44. PMID 22451925 DOI: 10.1073/Pnas.1121549109 |
0.657 |
|
2012 |
Barker KD, Barkovits K, Wilks A. Metabolic flux of extracellular heme uptake in Pseudomonas aeruginosa is driven by the iron-regulated heme oxygenase (HemO) ( The Journal of Biological Chemistry (2012) 287, (18342-18350)) Journal of Biological Chemistry. 287: 27447. DOI: 10.1074/jbc.A112.359265 |
0.448 |
|
2009 |
Kaur AP, Lansky IB, Wilks A. The role of the cytoplasmic heme-binding protein (PhuS) of Pseudomonas aeruginosa in intracellular heme trafficking and iron homeostasis. The Journal of Biological Chemistry. 284: 56-66. PMID 18990702 DOI: 10.1074/jbc.M806068200 |
0.557 |
|
2007 |
Block DR, Lukat-Rodgers GS, Rodgers KR, Wilks A, Bhakta MN, Lansky IB. Identification of two heme-binding sites in the cytoplasmic heme-trafficking protein PhuS from Pseudomonas aeruginosa and their relevance to function. Biochemistry. 46: 14391-402. PMID 18020455 DOI: 10.1021/Bi701509N |
0.372 |
|
2007 |
Ho WW, Li H, Eakanunkul S, Tong Y, Wilks A, Guo M, Poulos TL. Holo- and apo-bound structures of bacterial periplasmic heme-binding proteins. The Journal of Biological Chemistry. 282: 35796-802. PMID 17925389 DOI: 10.1074/Jbc.M706761200 |
0.402 |
|
2007 |
Furci LM, Lopes P, Eakanunkul S, Zhong S, MacKerell AD, Wilks A. Inhibition of the bacterial heme oxygenases from Pseudomonas aeruginosa and Neisseria meningitidis: novel antimicrobial targets. Journal of Medicinal Chemistry. 50: 3804-13. PMID 17629261 DOI: 10.1021/Jm0700969 |
0.387 |
|
2007 |
Wilks A, Burkhard KA. Heme and virulence: how bacterial pathogens regulate, transport and utilize heme. Natural Product Reports. 24: 511-22. PMID 17534527 DOI: 10.1039/b604193k |
0.331 |
|
2007 |
Burkhard KA, Wilks A. Characterization of the outer membrane receptor ShuA from the heme uptake system of Shigella dysenteriae. Substrate specificity and identification of the heme protein ligands. The Journal of Biological Chemistry. 282: 15126-36. PMID 17387178 DOI: 10.1074/jbc.M611121200 |
0.348 |
|
2007 |
Kaur AP, Wilks A. Heme inhibits the DNA binding properties of the cytoplasmic heme binding protein of Shigella dysenteriae (ShuS). Biochemistry. 46: 2994-3000. PMID 17323920 DOI: 10.1021/bi061722r |
0.323 |
|
2007 |
Friedman J, Meharenna YT, Wilks A, Poulos TL. Diatomic ligand discrimination by the heme oxygenases from Neisseria meningitidis and Pseudomonas aeruginosa. The Journal of Biological Chemistry. 282: 1066-71. PMID 17095508 DOI: 10.1074/Jbc.M609112200 |
0.302 |
|
2006 |
Bhakta MN, Wilks A. The mechanism of heme transfer from the cytoplasmic heme binding protein PhuS to the delta-regioselective heme oxygenase of Pseudomonas aeruginosa. Biochemistry. 45: 11642-9. PMID 16981723 DOI: 10.1021/bi060980l |
0.432 |
|
2006 |
Rodríguez JC, Wilks A, Rivera M. Backbone NMR assignments and H/D exchange studies on the ferric azide- and cyanide-inhibited forms of Pseudomonas aeruginosa heme oxygenase. Biochemistry. 45: 4578-92. PMID 16584193 DOI: 10.1021/Bi0600188 |
0.343 |
|
2006 |
Lansky IB, Lukat-Rodgers GS, Block D, Rodgers KR, Ratliff M, Wilks A. The cytoplasmic heme-binding protein (PhuS) from the heme uptake system of Pseudomonas aeruginosa is an intracellular heme-trafficking protein to the delta-regioselective heme oxygenase. The Journal of Biological Chemistry. 281: 13652-62. PMID 16533806 DOI: 10.1074/Jbc.M600824200 |
0.491 |
|
2005 |
Deshmukh R, Zeng Y, Furci LM, Huang HW, Morgan BN, Sander S, Alontaga AY, Bunce RA, Moënne-Loccoz P, Rivera M, Wilks A. Heme oxidation in a chimeric protein of the alpha-selective Neisseriae meningitidis heme oxygenase with the distal helix of the delta-selective Pseudomonas aeruginosa. Biochemistry. 44: 13713-23. PMID 16229461 DOI: 10.1021/Bi050810T |
0.411 |
|
2005 |
Eakanunkul S, Lukat-Rodgers GS, Sumithran S, Ghosh A, Rodgers KR, Dawson JH, Wilks A. Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae. Biochemistry. 44: 13179-91. PMID 16185086 DOI: 10.1021/Bi050422R |
0.49 |
|
2004 |
Wyckoff EE, Schmitt M, Wilks A, Payne SM. HutZ is required for efficient heme utilization in Vibrio cholerae. Journal of Bacteriology. 186: 4142-51. PMID 15205415 DOI: 10.1128/Jb.186.13.4142-4151.2004 |
0.596 |
|
2003 |
Wilks A. Purification and characterization of heme oxygenase. Current Protocols in Toxicology / Editorial Board, Mahin D. Maines (Editor-in-Chief) ... [Et Al.]. Unit9.9. PMID 23045096 DOI: 10.1002/0471140856.Tx0909S15 |
0.361 |
|
2003 |
Friedman J, Lad L, Deshmukh R, Li H, Wilks A, Poulos TL. Crystal structures of the NO- and CO-bound heme oxygenase from Neisseriae meningitidis: Implications for O2 activation Journal of Biological Chemistry. 278: 34654-34659. PMID 12819228 DOI: 10.1074/Jbc.M302985200 |
0.478 |
|
2002 |
Caignan GA, Deshmukh R, Wilks A, Zeng Y, Huang HW, Moënne-Loccoz P, Bunce RA, Eastman MA, Rivera M. Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme. Journal of the American Chemical Society. 124: 14879-92. PMID 12475329 DOI: 10.1021/Ja0274960 |
0.388 |
|
2002 |
Wilks A. Heme oxygenase: evolution, structure, and mechanism. Antioxidants & Redox Signaling. 4: 603-14. PMID 12230872 DOI: 10.1089/15230860260220102 |
0.483 |
|
2001 |
Ratliff M, Zhu W, Deshmukh R, Wilks A, Stojiljkovic I. Homologues of neisserial heme oxygenase in gram-negative bacteria: Degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa Journal of Bacteriology. 183: 6394-6403. PMID 11591684 DOI: 10.1128/Jb.183.21.6394-6403.2001 |
0.591 |
|
2001 |
Schuller DJ, Zhu W, Stojiljkovic I, Wilks A, Poulos TL. Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1 Biochemistry. 40: 11552-11558. PMID 11560504 DOI: 10.1021/Bi0110239 |
0.389 |
|
2001 |
Wilks A. The ShuS protein of Shigella dysenteriae is a heme-sequestering protein that also binds DNA. Archives of Biochemistry and Biophysics. 387: 137-42. PMID 11368175 DOI: 10.1006/Abbi.2000.2250 |
0.477 |
|
2000 |
Zhu W, Wilks A, Stojiljkovic I. Degradation of heme in gram-negative bacteria: The product of the hemO gene of neisseriae is a heme oxygenase Journal of Bacteriology. 182: 6783-6790. PMID 11073924 DOI: 10.1128/Jb.182.23.6783-6790.2000 |
0.529 |
|
2000 |
Wilks A, Moënne-Loccoz P. Identification of the proximal ligand His-20 in heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Oxidative cleavage of the heme macrocycle does not require the proximal histidine. The Journal of Biological Chemistry. 275: 11686-92. PMID 10766788 DOI: 10.1074/Jbc.275.16.11686 |
0.371 |
|
1999 |
Schuller DJ, Wilks A, Ortiz De Montellano PR, Poulos TL. Crystal structure of human heme oxygenase-1 Nature Structural Biology. 6: 860-867. PMID 10467099 DOI: 10.1038/12319 |
0.4 |
|
1999 |
Liu Y, Moënne-Loccoz P, Hildebrand DP, Wilks A, Loehr TM, Mauk AG, Ortiz De Montellano PR. Replacement of the proximal histidine iron ligand by a cysteine or tyrosine converts heme oxygenase to an oxidase Biochemistry. 38: 3733-3743. PMID 10090762 DOI: 10.1021/Bi982707S |
0.391 |
|
1998 |
Wilks A, Medzihradszky KF, Ortiz de Montellano PR. Heme oxygenase active-site residues identified by heme-protein cross- linking during reduction of CBrCl3 Biochemistry. 37: 2889-2896. PMID 9485440 DOI: 10.1021/bi972720x |
0.331 |
|
1998 |
Wilks A, Schmitt MP. Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocycle. The Journal of Biological Chemistry. 273: 837-41. PMID 9422739 DOI: 10.1074/jbc.273.2.837 |
0.442 |
|
1996 |
Hawkins BK, Wilks A, Powers LS, Ortiz de Montellano PR, Dawson JH. Ligation of the iron in the heme-heme oxygenase complex: X-ray absorption, electronic absorption and magnetic circular dichroism studies. Biochimica Et Biophysica Acta. 1295: 165-73. PMID 8695642 DOI: 10.1016/0167-4838(96)00031-3 |
0.344 |
|
1996 |
Wilks A, Ortiz de Montellano PR, Sun J, Loehr TM. Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis. Biochemistry. 35: 930-6. PMID 8547275 DOI: 10.1021/bi952405f |
0.479 |
|
1995 |
Wilks A, Black SM, Miller WL, Ortiz de Montellano PR. Expression and characterization of truncated human heme oxygenase (hHO-1) and a fusion protein of hHO-1 with human cytochrome P450 reductase. Biochemistry. 34: 4421-7. PMID 7703255 DOI: 10.1021/bi00013a034 |
0.304 |
|
1995 |
Wilks A, Sun J, Loehr TM, Ortiz de Montellano PR. Heme Oxygenase His25Ala Mutant: Replacement of the Proximal Histidine Iron Ligand by Exogenous Bases Restores Catalytic Activity Journal of the American Chemical Society. 117: 2925-2926. DOI: 10.1021/ja00115a027 |
0.445 |
|
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