Megan M. McEvoy - Publications

Affiliations: 
Biochemistry & Molecular Biophysics University of Arizona, Tucson, AZ 
Area:
Biochemistry, General Biophysics

39 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
2021 Gomez-Lugo JJ, Santos BD, Perez-Perez DA, Montfort-Gardeazabal JM, McEvoy MM, Zarate X. Expression and Purification of Recombinant Proteins in Escherichia coli Tagged with the Metal-Binding Proteins SmbP and CusF3H. Methods in Molecular Biology (Clifton, N.J.). 2178: 329-344. PMID 33128759 DOI: 10.1007/978-1-0716-0775-6_22  1
2020 Hausrath AC, Ramirez NA, Ly AT, McEvoy MM. The bacterial copper-resistance protein CopG contains a cysteine-bridged tetranuclear copper cluster. The Journal of Biological Chemistry. PMID 32571874 DOI: 10.1074/jbc.RA120.013907  1
2020 Bazzi W, Abou Fayad AG, Nasser A, Haraoui LP, Dewachi O, Abou-Sitta G, Nguyen VK, Abara A, Karah N, Landecker H, Knapp C, McEvoy MM, Zaman MH, Higgins PG, Matar GM. Heavy Metal Toxicity in Armed Conflicts Potentiates AMR in by Selecting for Antibiotic and Heavy Metal Co-resistance Mechanisms. Frontiers in Microbiology. 11: 68. PMID 32117111 DOI: 10.3389/Fmicb.2020.00068  0.01
2020 Górecki K, McEvoy MM. Phylogenetic analysis reveals an ancient gene duplication as the origin of the MdtABC efflux pump. Plos One. 15: e0228877. PMID 32050009 DOI: 10.1371/journal.pone.0228877  0.01
2019 Affandi T, McEvoy MM. Mechanism of metal ion-induced activation of a two-component sensor kinase. The Biochemical Journal. 476: 115-135. PMID 30530842 DOI: 10.1042/BCJ20180577  1
2017 Santiago AG, Chen TY, Genova LA, Jung W, George Thompson AM, McEvoy MM, Chen P. Adaptor protein mediates dynamic pump assembly for bacterial metal efflux. Proceedings of the National Academy of Sciences of the United States of America. PMID 28607072 DOI: 10.1073/Pnas.1704729114  0.01
2016 Affandi T, Issaian AV, McEvoy MM. The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface. Biochemistry. PMID 27583660 DOI: 10.1021/Acs.Biochem.6B00707  1
2016 Cantu-Bustos JE, Vargas-Cortez T, Morones-Ramirez JR, Balderas-Renteria I, Galbraith DW, McEvoy MM, Zarate X. Expression and purification of recombinant proteins in Escherichia coli tagged with the metal-binding protein CusF. Protein Expression and Purification. 121: 61-5. PMID 26805756 DOI: 10.1016/J.Pep.2016.01.007  1
2014 Chacón KN, Mealman TD, McEvoy MM, Blackburn NJ. Tracking metal ions through a Cu/Ag efflux pump assigns the functional roles of the periplasmic proteins. Proceedings of the National Academy of Sciences of the United States of America. 111: 15373-8. PMID 25313055 DOI: 10.1073/Pnas.1411475111  1
2014 Gudipaty SA, McEvoy MM. The histidine kinase CusS senses silver ions through direct binding by its sensor domain. Biochimica Et Biophysica Acta. 1844: 1656-61. PMID 24948475 DOI: 10.1016/J.Bbapap.2014.06.001  1
2014 Padilla-Benavides T, George Thompson AM, McEvoy MM, Argüello JM. Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic chaperones: the interaction of Escherichia coli CopA and CusF. The Journal of Biological Chemistry. 289: 20492-501. PMID 24917681 DOI: 10.1074/Jbc.M114.577668  1
2012 Mealman TD, Blackburn NJ, McEvoy MM. Metal export by CusCFBA, the periplasmic Cu(I)/Ag(I) transport system of Escherichia coli. Current Topics in Membranes. 69: 163-96. PMID 23046651 DOI: 10.1016/B978-0-12-394390-3.00007-0  1
2012 Mealman TD, Zhou M, Affandi T, Chacón KN, Aranguren ME, Blackburn NJ, Wysocki VH, McEvoy MM. N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF. Biochemistry. 51: 6767-75. PMID 22812620 DOI: 10.1021/Bi300596A  1
2012 Jayakanthan S, Roberts SA, Weichsel A, Argüello JM, McEvoy MM. Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Bioscience Reports. 32: 443-53. PMID 22663904 DOI: 10.1042/Bsr20120048  1
2012 Gudipaty SA, Larsen AS, Rensing C, McEvoy MM. Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor kinase CusS. Fems Microbiology Letters. 330: 30-7. PMID 22348296 DOI: 10.1111/J.1574-6968.2012.02529.X  1
2011 Kim EH, Nies DH, McEvoy MM, Rensing C. Switch or funnel: how RND-type transport systems control periplasmic metal homeostasis. Journal of Bacteriology. 193: 2381-7. PMID 21398536 DOI: 10.1128/Jb.01323-10  1
2011 McEvoy MM, Rensing C. Biometals 2010 (Tucson, Arizona, USA). Biometals : An International Journal On the Role of Metal Ions in Biology, Biochemistry, and Medicine. 24: 377-8. PMID 21387113 DOI: 10.1007/S10534-011-9432-7  1
2011 Mealman TD, Bagai I, Singh P, Goodlett DR, Rensing C, Zhou H, Wysocki VH, McEvoy MM. Interactions between CusF and CusB identified by NMR spectroscopy and chemical cross-linking coupled to mass spectrometry. Biochemistry. 50: 2559-66. PMID 21323389 DOI: 10.1021/Bi102012J  1
2010 Conroy O, Kim EH, McEvoy MM, Rensing C. Differing ability to transport nonmetal substrates by two RND-type metal exporters. Fems Microbiology Letters. 308: 115-22. PMID 20497225 DOI: 10.1111/J.1574-6968.2010.02006.X  1
2010 Kim EH, Rensing C, McEvoy MM. Chaperone-mediated copper handling in the periplasm. Natural Product Reports. 27: 711-9. PMID 20442961 DOI: 10.1039/B906681K  1
2009 Kim EH, Charpentier X, Torres-Urquidy O, McEvoy MM, Rensing C. The metal efflux island of Legionella pneumophila is not required for survival in macrophages and amoebas. Fems Microbiology Letters. 301: 164-70. PMID 19895645 DOI: 10.1111/J.1574-6968.2009.01813.X  1
2009 Quaranta D, McEvoy MM, Rensing C. Site-directed mutagenesis identifies a molecular switch involved in copper sensing by the histidine kinase CinS in Pseudomonas putida KT2440. Journal of Bacteriology. 191: 5304-11. PMID 19542288 DOI: 10.1128/Jb.00551-09  1
2009 Loftin IR, Blackburn NJ, McEvoy MM. Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 14: 905-12. PMID 19381697 DOI: 10.1007/S00775-009-0503-Y  1
2008 Bagai I, Rensing C, Blackburn NJ, McEvoy MM. Direct metal transfer between periplasmic proteins identifies a bacterial copper chaperone. Biochemistry. 47: 11408-14. PMID 18847219 DOI: 10.1021/Bi801638M  1
2007 Loftin IR, Franke S, Blackburn NJ, McEvoy MM. Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Science : a Publication of the Protein Society. 16: 2287-93. PMID 17893365 DOI: 10.1110/Ps.073021307  1
2007 Bagai I, Liu W, Rensing C, Blackburn NJ, McEvoy MM. Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system. The Journal of Biological Chemistry. 282: 35695-702. PMID 17893146 DOI: 10.1074/Jbc.M703937200  1
2006 Kittleson JT, Loftin IR, Hausrath AC, Engelhardt KP, Rensing C, McEvoy MM. Periplasmic metal-resistance protein CusF exhibits high affinity and specificity for both CuI and AgI. Biochemistry. 45: 11096-102. PMID 16964970 DOI: 10.1021/Bi0612622  1
2005 Loftin IR, Franke S, Roberts SA, Weichsel A, Héroux A, Montfort WR, Rensing C, McEvoy MM. A novel copper-binding fold for the periplasmic copper resistance protein CusF. Biochemistry. 44: 10533-40. PMID 16060662 DOI: 10.1021/Bi050827B  1
2005 Astashkin AV, Raitsimring AM, Walker FA, Rensing C, McEvoy MM. Characterization of the copper(II) binding site in the pink copper binding protein CusF by electron paramagnetic resonance spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 10: 221-30. PMID 15770503 DOI: 10.1007/S00775-005-0631-Y  1
2004 Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW. Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide. Journal of Molecular Biology. 342: 1325-35. PMID 15351654 DOI: 10.1016/J.Jmb.2004.07.084  1
2000 Halkides CJ, McEvoy MM, Casper E, Matsumura P, Volz K, Dahlquist FW. The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Biochemistry. 39: 5280-6. PMID 10819997 DOI: 10.1021/Bi9925524  1
1999 McEvoy MM, Bren A, Eisenbach M, Dahlquist FW. Identification of the binding interfaces on CheY for two of its targets, the phosphatase CheZ and the flagellar switch protein fliM. Journal of Molecular Biology. 289: 1423-33. PMID 10373376 DOI: 10.1006/Jmbi.1999.2830  1
1998 McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway. Proceedings of the National Academy of Sciences of the United States of America. 95: 7333-8. PMID 9636149 DOI: 10.1073/Pnas.95.13.7333  1
1997 McEvoy MM, Dahlquist FW. Phosphohistidines in bacterial signaling. Current Opinion in Structural Biology. 7: 793-7. PMID 9434897 DOI: 10.1016/S0959-440X(97)80148-0  1
1997 McEvoy MM, de la Cruz AF, Dahlquist FW. Large modular proteins by NMR. Nature Structural Biology. 4: 9. PMID 8989314 DOI: 10.1038/Nsb0197-9  1
1996 McEvoy MM, Muhandiram DR, Kay LE, Dahlquist FW. Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy. Biochemistry. 35: 5633-40. PMID 8639521 DOI: 10.1021/Bi952707H  1
1996 Zhou H, McEvoy MM, Lowry DF, Swanson RV, Simon MI, Dahlquist FW. Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker. Biochemistry. 35: 433-43. PMID 8555213 DOI: 10.1021/Bi951960E  1
1995 McEvoy MM, Zhou H, Roth AF, Lowry DF, Morrison TB, Kay LE, Dahlquist FW. Nuclear magnetic resonance assignments and global fold of a CheY-binding domain in CheA, the chemotaxis-specific kinase of Escherichia coli. Biochemistry. 34: 13871-80. PMID 7577981 DOI: 10.1021/Bi00042A019  1
1995 Swanson RV, Lowry DF, Matsumura P, McEvoy MM, Simon MI, Dahlquist FW. Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface. Nature Structural Biology. 2: 906-10. PMID 7552716 DOI: 10.1038/Nsb1095-906  1
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