Year |
Citation |
Score |
2022 |
Dye KJ, Vogelaar NJ, O'Hara M, Sobrado P, Santos W, Carlier PR, Yang Z. Discovery of Two Inhibitors of the Type IV Pilus Assembly ATPase PilB as Potential Antivirulence Compounds. Microbiology Spectrum. e0387722. PMID 36377931 DOI: 10.1128/spectrum.03877-22 |
0.555 |
|
2022 |
Lyons NS, Bogner AN, Tanner JJ, Sobrado P. Kinetic and Structural Characterization of a Flavin-Dependent Putrescine -Hydroxylase from . Biochemistry. PMID 36314559 DOI: 10.1021/acs.biochem.2c00493 |
0.322 |
|
2021 |
Valentino H, Sobrado P. Characterization of a Nitro-Forming Enzyme Involved in Fosfazinomycin Biosynthesis. Biochemistry. PMID 34516102 DOI: 10.1021/acs.biochem.1c00512 |
0.821 |
|
2021 |
Valentino H, Korasick DA, Bohac TJ, Shapiro JA, Wencewicz TA, Tanner JJ, Sobrado P. Structural and Biochemical Characterization of the Flavin-Dependent Siderophore-Interacting Protein from . Acs Omega. 6: 18537-18547. PMID 34308084 DOI: 10.1021/acsomega.1c03047 |
0.773 |
|
2021 |
Reis RAG, Li H, Johnson M, Sobrado P. New frontiers in flavin-dependent monooxygenases. Archives of Biochemistry and Biophysics. 108765. PMID 33460580 DOI: 10.1016/j.abb.2021.108765 |
0.425 |
|
2020 |
Li H, Forson B, Eckshtain-Levi M, Valentino H, Martín Del Campo JS, Tanner JJ, Sobrado P. Biochemical Characterization of the Two-Component Flavin-Dependent Monooxygenase Involved in Valanimycin Biosynthesis. Biochemistry. PMID 33350810 DOI: 10.1021/acs.biochem.0c00679 |
0.821 |
|
2020 |
Sobrado P. Role of reduced flavin in dehalogenation reactions. Archives of Biochemistry and Biophysics. 697: 108696. PMID 33245912 DOI: 10.1016/j.abb.2020.108696 |
0.338 |
|
2020 |
Campbell AC, Robinson R, Mena-Aguilar D, Sobrado P, Tanner JJ. Structural Determinants of Flavin Dynamics in a Class B Monooxygenase. Biochemistry. PMID 33226785 DOI: 10.1021/acs.biochem.0c00783 |
0.774 |
|
2020 |
Campbell AC, Stiers KM, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ. Trapping conformational states of a flavin-dependent N-monooxygenase in crystallo reveals protein and flavin dynamics. The Journal of Biological Chemistry. PMID 32723870 DOI: 10.1074/Jbc.Ra120.014750 |
0.444 |
|
2020 |
Valentino H, Campbell AC, Schuermann JP, Sultana N, Nam HG, LeBlanc S, Tanner JJ, Sobrado P. Structure and function of a flavin-dependent S-monooxygenase from garlic (Allium sativum). The Journal of Biological Chemistry. PMID 32527723 DOI: 10.1074/Jbc.Ra120.014484 |
0.824 |
|
2020 |
Hofmann M, Martin Del Campo JS, Sobrado P, Tischler D. Biosynthesis of desferrioxamine siderophores initiated by decarboxylases: A functional investigation of two lysine/ornithine-decarboxylases from Gordonia rubripertincta CWB2 and Pimelobacter simplex 3E. Archives of Biochemistry and Biophysics. 108429. PMID 32479762 DOI: 10.1016/J.Abb.2020.108429 |
0.346 |
|
2019 |
Valentino H, Sobrado P. Performing anaerobic stopped-flow spectrophotometry inside of an anaerobic chamber. Methods in Enzymology. 620: 51-88. PMID 31072501 DOI: 10.1016/Bs.Mie.2019.03.006 |
0.799 |
|
2019 |
Cossio-P Eacute Rez R, Pierdominici-Sottile G, Sobrado P, Palma J. Molecular dynamics simulations of substrate release from Trypanosoma cruzi UDP-galactopyranose mutase. Journal of Chemical Information and Modeling. PMID 30608160 DOI: 10.1021/acs.jcim.8b00675 |
0.309 |
|
2018 |
Robinson RM, Klancher CA, Rodriguez PJ, Sobrado P. Flavin oxidation in flavin-dependent N-monooxygenases. Protein Science : a Publication of the Protein Society. PMID 30098072 DOI: 10.1002/Pro.3487 |
0.783 |
|
2018 |
Gadda G, Sobrado P. Kinetic Solvent Viscosity Effects as Probes to Study the Mechanisms of Enzyme Action. Biochemistry. PMID 29874467 DOI: 10.1021/Acs.Biochem.8B00232 |
0.675 |
|
2018 |
Dai Y, Valentino HR, Sobrado P. Evidence for Formation of a Radical-Mediated Flavin-N5 Covalent Intermediate. Chembiochem : a European Journal of Chemical Biology. PMID 29776001 DOI: 10.1002/Cbic.201800123 |
0.788 |
|
2018 |
Pierdominici-Sottile G, Cossio-P Eacute Rez R, Da Fonseca I, Kizjakina K, Tanner JJ, Sobrado P. Steric control of the rate-limiting step of UDP-galactopyranose mutase. Biochemistry. PMID 29757624 DOI: 10.1021/acs.biochem.8b00323 |
0.805 |
|
2018 |
Liu LK, Dai Y, Abdelwahab H, Sobrado P, Tanner JJ. Structural evidence for rifampicin monooxygenase inactivating rifampicin by cleaving its ansa-bridge. Biochemistry. PMID 29578336 DOI: 10.1021/Acs.Biochem.8B00190 |
0.694 |
|
2017 |
Dai Y, Kizjakina K, Campbell AC, Korasick DA, Tanner JJ, Sobrado P. Flavin-N5 Covalent Intermediate in the Non-redox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme. Chembiochem : a European Journal of Chemical Biology. PMID 29116682 DOI: 10.1002/Cbic.201700594 |
0.802 |
|
2017 |
Martín Del Campo JS, Eckshtain-Levi M, Sobrado P. Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay. Biochemical and Biophysical Research Communications. PMID 28919416 DOI: 10.1016/J.Bbrc.2017.09.074 |
0.349 |
|
2017 |
Martin Del Campo JS, Eckshtain-Levi M, Vogelaar NJ, Sobrado P. Identification of Aspergillus fumigatus UDP-Galactopyranose Mutase Inhibitors. Scientific Reports. 7: 10836. PMID 28883473 DOI: 10.1038/s41598-017-11022-5 |
0.307 |
|
2017 |
Sobrado P, Gadda G. Introduction to flavoproteins: Beyond the classical paradigms. Archives of Biochemistry and Biophysics. PMID 28870454 DOI: 10.1016/J.Abb.2017.08.016 |
0.469 |
|
2017 |
Sobrado P, Tanner JJ. Multiple functionalities of reduced flavin in the non-redox reaction catalyzed by UDP-galactopyranose mutase. Archives of Biochemistry and Biophysics. PMID 28652025 DOI: 10.1016/j.abb.2017.06.015 |
0.378 |
|
2017 |
Dai Y, Kizjakina K, Campbell AC, Korasick DA, Tanner JJ, Sobrado P. Cover Feature: Flavin-N5 Covalent Intermediate in a Nonredox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme Chembiochem. 19: 3-3. DOI: 10.1002/Cbic.201700647 |
0.348 |
|
2016 |
Abdelwahab H, Martin Del Campo JS, Dai Y, Adly C, El-Sohaimy S, Sobrado P. Mechanism of Rifampicin Inactivation in Nocardia farcinica. Plos One. 11: e0162578. PMID 27706151 DOI: 10.1371/Journal.Pone.0162578 |
0.75 |
|
2016 |
Martin Del Campo JS, Vogelaar N, Tolani K, Kizjakina K, Harich KC, Sobrado P. Inhibition of the flavin-dependent monooxygenase Siderophore A (SidA) blocks siderophore biosynthesis and Aspergillus fumigatus growth. Acs Chemical Biology. PMID 27588426 DOI: 10.1021/Acschembio.6B00666 |
0.785 |
|
2016 |
Liu LK, Abdelwahab H, Martin Del Campo JS, Mehra-Chaudhary R, Sobrado P, Tanner JJ. The Structure of the Antibiotic Deactivating, N-hydroxylating Rifampicin Monooxygenase. The Journal of Biological Chemistry. PMID 27557658 DOI: 10.1074/Jbc.M116.745315 |
0.439 |
|
2016 |
Abdelwahab H, Robinson R, Rodriguez P, Adly C, El-Sohaimy S, Sobrado P. Identification of structural determinants of NAD(P)H selectivity and lysine binding in lysine (6)N-monooxygenase. Archives of Biochemistry and Biophysics. PMID 27503802 DOI: 10.1016/J.Abb.2016.08.004 |
0.783 |
|
2016 |
Mehra-Chaudhary R, Dai Y, Sobrado P, Tanner JJ. In Crystallo Capture of a Covalent Intermediate in the UDP-Galactopyranose Mutase Reaction. Biochemistry. PMID 26836146 DOI: 10.1021/Acs.Biochem.6B00035 |
0.736 |
|
2015 |
Robinson R, Qureshi IA, Klancher CA, Rodriguez PJ, Tanner JJ, Sobrado P. Contribution to catalysis of ornithine binding residues in ornithine N5-monooxygenase. Archives of Biochemistry and Biophysics. 585: 25-31. PMID 26375201 DOI: 10.1016/J.Abb.2015.09.008 |
0.803 |
|
2015 |
Bai Y, McCoy JG, Levin EJ, Sobrado P, Rajashankar KR, Fox BG, Zhou M. X-ray structure of a mammalian stearoyl-CoA desaturase. Nature. PMID 26098370 DOI: 10.1038/Nature14549 |
0.581 |
|
2015 |
Binda C, Robinson RM, Martin Del Campo JS, Keul ND, Rodriguez PJ, Robinson HH, Mattevi A, Sobrado P. An unprecedented NADPH domain conformation in lysine monooxygenase NbtG provides insights into uncoupling of oxygen consumption from substrate hydroxylation. The Journal of Biological Chemistry. 290: 12676-88. PMID 25802330 DOI: 10.1074/Jbc.M114.629485 |
0.795 |
|
2015 |
Sohrabi R, Huh JH, Badieyan S, Rakotondraibe LH, Kliebenstein DJ, Sobrado P, Tholl D. In planta variation of volatile biosynthesis: an alternative biosynthetic route to the formation of the pathogen-induced volatile homoterpene DMNT via triterpene degradation in Arabidopsis roots. The Plant Cell. 27: 874-90. PMID 25724638 DOI: 10.1105/Tpc.114.132209 |
0.301 |
|
2015 |
Badieyan S, Bach RD, Sobrado P. Mechanism of N-hydroxylation catalyzed by flavin-dependent monooxygenases. The Journal of Organic Chemistry. 80: 2139-47. PMID 25633869 DOI: 10.1021/Jo502651V |
0.374 |
|
2014 |
Da Fonseca I, Qureshi IA, Mehra-Chaudhary R, Kizjakina K, Tanner JJ, Sobrado P. Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics. Biochemistry. 53: 7794-804. PMID 25412209 DOI: 10.1021/Bi501008Z |
0.816 |
|
2014 |
Robinson RM, Rodriguez PJ, Sobrado P. Mechanistic studies on the flavin-dependent Nâ¶-lysine monooxygenase MbsG reveal an unusual control for catalysis. Archives of Biochemistry and Biophysics. 550: 58-66. PMID 24769337 DOI: 10.1016/J.Abb.2014.04.006 |
0.776 |
|
2014 |
Robinson R, Franceschini S, Fedkenheuer M, Rodriguez PJ, Ellerbrock J, Romero E, Echandi MP, Martin Del Campo JS, Sobrado P. Arg279 is the key regulator of coenzyme selectivity in the flavin-dependent ornithine monooxygenase SidA. Biochimica Et Biophysica Acta. 1844: 778-84. PMID 24534646 DOI: 10.1016/J.Bbapap.2014.02.005 |
0.79 |
|
2014 |
Tanner JJ, Boechi L, Andrew McCammon J, Sobrado P. Structure, mechanism, and dynamics of UDP-galactopyranose mutase. Archives of Biochemistry and Biophysics. 544: 128-41. PMID 24096172 DOI: 10.1016/J.Abb.2013.09.017 |
0.485 |
|
2013 |
Robinson R, Badieyan S, Sobrado P. C4a-hydroperoxyflavin formation in N-hydroxylating flavin monooxygenases is mediated by the 2'-OH of the nicotinamide ribose of NADPâº. Biochemistry. 52: 9089-91. PMID 24321106 DOI: 10.1021/Bi4014903 |
0.773 |
|
2013 |
Komachi Y, Hatakeyama S, Motomatsu H, Futagami T, Kizjakina K, Sobrado P, Ekino K, Takegawa K, Goto M, Nomura Y, Oka T. GfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Molecular Microbiology. 90: 1054-73. PMID 24118544 DOI: 10.1111/Mmi.12416 |
0.768 |
|
2013 |
Shirey C, Badieyan S, Sobrado P. Role of Ser-257 in the sliding mechanism of NADP(H) in the reaction catalyzed by the Aspergillus fumigatus flavin-dependent ornithine N5-monooxygenase SidA. The Journal of Biological Chemistry. 288: 32440-8. PMID 24072704 DOI: 10.1074/Jbc.M113.487181 |
0.464 |
|
2013 |
Fonseca IO, Kizjakina K, Sobrado P. UDP-galactopyranose mutases from Leishmania species that cause visceral and cutaneous leishmaniasis. Archives of Biochemistry and Biophysics. 538: 103-10. PMID 24012809 DOI: 10.1016/J.Abb.2013.08.014 |
0.81 |
|
2013 |
Boechi L, de Oliveira CA, Da Fonseca I, Kizjakina K, Sobrado P, Tanner JJ, McCammon JA. Substrate-dependent dynamics of UDP-galactopyranose mutase: Implications for drug design. Protein Science : a Publication of the Protein Society. 22: 1490-501. PMID 23934860 DOI: 10.1002/Pro.2332 |
0.794 |
|
2013 |
Han A, Robinson RM, Badieyan S, Ellerbrock J, Sobrado P. Tryptophan-47 in the active site of Methylophaga sp. strain SK1 flavin-monooxygenase is important for hydride transfer. Archives of Biochemistry and Biophysics. 532: 46-53. PMID 23357278 DOI: 10.1016/J.Abb.2013.01.004 |
0.801 |
|
2013 |
Kizjakina K, Tanner JJ, Sobrado P. Targeting UDP-galactopyranose mutases from eukaryotic human pathogens. Current Pharmaceutical Design. 19: 2561-73. PMID 23116395 DOI: 10.2174/1381612811319140007 |
0.813 |
|
2012 |
Sobrado P. Noncanonical reactions of flavoenzymes. International Journal of Molecular Sciences. 13: 14219-42. PMID 23203060 DOI: 10.3390/Ijms131114219 |
0.436 |
|
2012 |
Dhatwalia R, Singh H, Solano LM, Oppenheimer M, Robinson RM, Ellerbrock JF, Sobrado P, Tanner JJ. Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase. Journal of the American Chemical Society. 134: 18132-8. PMID 23036087 DOI: 10.1021/Ja308188Z |
0.786 |
|
2012 |
Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A. Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases. Biochemistry. 51: 7043-5. PMID 22928747 DOI: 10.1021/Bi301072W |
0.488 |
|
2012 |
Dhatwalia R, Singh H, Oppenheimer M, Sobrado P, Tanner JJ. Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation. Biochemistry. 51: 4968-79. PMID 22646091 DOI: 10.1021/Bi300498C |
0.479 |
|
2012 |
Romero E, Fedkenheuer M, Chocklett SW, Qi J, Oppenheimer M, Sobrado P. Dual role of NADP(H) in the reaction of a flavin dependent N-hydroxylating monooxygenase. Biochimica Et Biophysica Acta. 1824: 850-7. PMID 22465572 DOI: 10.1016/J.Bbapap.2012.03.004 |
0.52 |
|
2012 |
Romero E, Robinson R, Sobrado P. Monitoring the reductive and oxidative half-reactions of a flavin-dependent monooxygenase using stopped-flow spectrophotometry. Journal of Visualized Experiments : Jove. PMID 22453826 DOI: 10.3791/3803 |
0.785 |
|
2012 |
Oppenheimer M, Valenciano AL, Kizjakina K, Qi J, Sobrado P. Chemical mechanism of UDP-galactopyranose mutase from Trypanosoma cruzi: a potential drug target against Chagas' disease. Plos One. 7: e32918. PMID 22448231 DOI: 10.1371/Journal.Pone.0032918 |
0.815 |
|
2012 |
Qi J, Kizjakina K, Robinson R, Tolani K, Sobrado P. A fluorescence polarization binding assay to identify inhibitors of flavin-dependent monooxygenases. Analytical Biochemistry. 425: 80-7. PMID 22410281 DOI: 10.1016/J.Ab.2012.03.002 |
0.774 |
|
2012 |
Dhatwalia R, Singh H, Oppenheimer M, Karr DB, Nix JC, Sobrado P, Tanner JJ. Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. The Journal of Biological Chemistry. 287: 9041-51. PMID 22294687 DOI: 10.1074/Jbc.M111.327536 |
0.414 |
|
2011 |
Qi J, Oppenheimer M, Sobrado P. Fluorescence Polarization Binding Assay for Aspergillus fumigatus Virulence Factor UDP-Galactopyranose Mutase. Enzyme Research. 2011: 513905. PMID 21876791 DOI: 10.4061/2011/513905 |
0.358 |
|
2011 |
Robinson R, Sobrado P. Substrate binding modulates the activity of Mycobacterium smegmatis G, a flavin-dependent monooxygenase involved in the biosynthesis of hydroxamate-containing siderophores. Biochemistry. 50: 8489-96. PMID 21870809 DOI: 10.1021/Bi200933H |
0.804 |
|
2011 |
Oppenheimer M, Valenciano AL, Sobrado P. Biosynthesis of galactofuranose in kinetoplastids: novel therapeutic targets for treating leishmaniasis and chagas' disease. Enzyme Research. 2011: 415976. PMID 21687654 DOI: 10.4061/2011/415976 |
0.353 |
|
2011 |
Oppenheimer M, Valenciano AL, Sobrado P. Isolation and characterization of functional Leishmania major virulence factor UDP-galactopyranose mutase. Biochemical and Biophysical Research Communications. 407: 552-6. PMID 21419104 DOI: 10.1016/J.Bbrc.2011.03.057 |
0.437 |
|
2010 |
Oppenheimer M, Poulin MB, Lowary TL, Helm RF, Sobrado P. Characterization of recombinant UDP-galactopyranose mutase from Aspergillus fumigatus. Archives of Biochemistry and Biophysics. 502: 31-8. PMID 20615386 DOI: 10.1016/J.Abb.2010.06.035 |
0.446 |
|
2010 |
Chocklett SW, Sobrado P. Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor. Biochemistry. 49: 6777-83. PMID 20614882 DOI: 10.1021/Bi100291N |
0.471 |
|
2010 |
Oppenheimer M, Pierce BS, Crawford JA, Ray K, Helm RF, Sobrado P. Recombinant expression, purification, and characterization of ThmD, the oxidoreductase component of tetrahydrofuran monooxygenase. Archives of Biochemistry and Biophysics. 496: 123-31. PMID 20159007 DOI: 10.1016/J.Abb.2010.02.006 |
0.447 |
|
2008 |
Sobrado P, Goren MA, James D, Amundson CK, Fox BG. A Protein Structure Initiative approach to expression, purification, and in situ delivery of human cytochrome b5 to membrane vesicles. Protein Expression and Purification. 58: 229-41. PMID 18226920 DOI: 10.1016/J.Pep.2007.11.018 |
0.52 |
|
2007 |
Tsai CL, Gokulan K, Sobrado P, Sacchettini JC, Fitzpatrick PF. Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base. Biochemistry. 46: 7844-51. PMID 17563122 DOI: 10.1021/Bi7005543 |
0.661 |
|
2006 |
Sobrado P, Lyle KS, Kaul SP, Turco MM, Arabshahi I, Marwah A, Fox BG. Identification of the binding region of the [2Fe-2S] ferredoxin in stearoyl-acyl carrier protein desaturase: insight into the catalytic complex and mechanism of action. Biochemistry. 45: 4848-58. PMID 16605252 DOI: 10.1021/Bi0600547 |
0.56 |
|
2005 |
Sobrado P, Jedlicki A, Bustos VH, Allende CC, Allende JE. Basic region of residues 228-231 of protein kinase CK1alpha is involved in its interaction with axin: binding to axin does not affect the kinase activity. Journal of Cellular Biochemistry. 94: 217-24. PMID 15565646 DOI: 10.1002/Jcb.20350 |
0.578 |
|
2003 |
Sobrado P, Fitzpatrick PF. Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism. Biochemistry. 42: 15208-14. PMID 14690431 DOI: 10.1021/Bi035546N |
0.63 |
|
2003 |
Sobrado P, Fitzpatrick PF. Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysis. Biochemistry. 42: 13833-8. PMID 14636050 DOI: 10.1021/Bi035300I |
0.669 |
|
2003 |
Sobrado P, Fitzpatrick PF. Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase family. Biochemistry. 42: 13826-32. PMID 14636049 DOI: 10.1021/Bi035299N |
0.646 |
|
2002 |
Sobrado P, Fitzpatrick PF. Analysis of the roles of amino acid residues in the flavoprotein tryptophan 2-monooxygenase modified by 2-oxo-3-pentynoate: characterization of His338, Cys339, and Cys511 mutant enzymes. Archives of Biochemistry and Biophysics. 402: 24-30. PMID 12051679 DOI: 10.1016/S0003-9861(02)00063-2 |
0.657 |
|
2001 |
Sobrado P, Daubner SC, Fitzpatrick PF. Probing the relative timing of hydrogen abstraction steps in the flavocytochrome b2 reaction with primary and solvent deuterium isotope effects and mutant enzymes. Biochemistry. 40: 994-1001. PMID 11170421 DOI: 10.1021/Bi002283D |
0.641 |
|
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