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Minae A. Mure - Publications

Affiliations: 
Chemistry University of Kansas, Lawrence, KS, United States 
Area:
Analytical Chemistry
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25 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
2022 Meier AA, Moon HJ, Sabuncu S, Singh P, Ronnebaum TA, Ou S, Douglas JT, Jackson TA, Moënne-Loccoz P, Mure M. Insight into the Spatial Arrangement of the Lysine Tyrosylquinone and Cu in the Active Site of Lysyl Oxidase-like 2. International Journal of Molecular Sciences. 23. PMID 36430446 DOI: 10.3390/ijms232213966  0.324
2018 Okada K, Moon HJ, Finney J, Meier A, Mure M. Extracellular processing of lysyl oxidase-like 2 and its effect on amine oxidase activity. Biochemistry. PMID 30499665 DOI: 10.1021/Acs.Biochem.8B01008  0.359
2018 Go EP, Moon HJ, Mure M, Desaire H. A recombinant human LOXL2 secreted from HEK cells displays complex, acidic glycans at all three N-linked glycosylation sites. Journal of Proteome Research. PMID 29619832 DOI: 10.1021/Acs.Jproteome.7B00849  0.338
2017 Okada K, Moon HJ, Finney J, Couture F, Day R, Mure M. PACE4 Proteolytically Processes LOXL2 with little impact on its catalytic activity. The Journal of Biological Chemistry. PMID 29184001 DOI: 10.1074/Jbc.C117.810978  0.338
2014 Finney J, Moon HJ, Ronnebaum T, Lantz M, Mure M. Human copper-dependent amine oxidases. Archives of Biochemistry and Biophysics. 546: 19-32. PMID 24407025 DOI: 10.1016/J.Abb.2013.12.022  0.371
2013 Moon HJ, Finney J, Xu L, Moore D, Welch DR, Mure M. MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro. The Journal of Biological Chemistry. 288: 30000-8. PMID 24014025 DOI: 10.1074/Jbc.C113.502310  0.308
2013 Xu L, Go EP, Finney J, Moon H, Lantz M, Rebecchi K, Desaire H, Mure M. Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells. The Journal of Biological Chemistry. 288: 5357-63. PMID 23319596 DOI: 10.1074/Jbc.C112.421768  0.359
2010 Reed T, Lushington GH, Xia Y, Hirakawa H, Travis DM, Mure M, Scott EE, Limburg J. Crystal structure of histamine dehydrogenase from Nocardioides simplex. The Journal of Biological Chemistry. 285: 25782-91. PMID 20538584 DOI: 10.1074/Jbc.M109.084301  0.568
2010 Chang CM, Klema VJ, Johnson BJ, Mure M, Klinman JP, Wilmot CM. Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha Biochemistry. 49: 2540-2550. PMID 20155950 DOI: 10.1021/Bi901933D  0.365
2008 Reed TM, Hirakawa H, Mure M, Scott EE, Limburg J. Expression, purification, crystallization and preliminary X-ray studies of histamine dehydrogenase from Nocardioides simplex. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 64: 785-7. PMID 18765904 DOI: 10.1107/S1744309108023336  0.56
2007 Moore RH, Spies MA, Culpepper MB, Murakawa T, Hirota S, Okajima T, Tanizawa K, Mure M. Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis. Journal of the American Chemical Society. 129: 11524-34. PMID 17715921 DOI: 10.1021/ja0731165  0.605
2007 Moore RH, Spies, Culpepper MB, Murakawa T, Hirota S, Okajima T, Tanizawa K, Mure M. Trapping of a dopaquinone intermediate in the TPQ cofactor biogenesis in a copper-containing amine oxidase from Arthrobacter globiformis Journal of the American Chemical Society. 129: 11524-11534. DOI: 10.2210/Pdb2Yx9/Pdb  0.611
2005 Mure M, Kurtis CR, Brown DE, Rogers MS, Tambyrajah WS, Saysell C, Wilmot CM, Phillips SE, Knowles PF, Dooley DM, McPherson MJ. Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct. Biochemistry. 44: 1583-94. PMID 15683242 DOI: 10.1021/Bi0479860  0.436
2005 Mure M, Brown DE, Saysell C, Rogers MS, Wilmot CM, Kurtis CR, McPherson MJ, Phillips SE, Knowles PF, Dooley DM. Role of the interactions between the active site base and the substrate Schiff base in amine oxidase catalysis. Evidence from structural and spectroscopic studies of the 2-hydrazinopyridine adduct of Escherichia coli amine oxidase. Biochemistry. 44: 1568-82. PMID 15683241 DOI: 10.1021/Bi047988K  0.457
2004 Mure M. Tyrosine-derived quinone cofactors Accounts of Chemical Research. 37: 131-139. PMID 14967060 DOI: 10.1021/Ar9703342  0.395
2003 Mure M, Wang SX, Klinman JP. Synthesis and characterization of model compounds of the lysine tyrosyl quinone cofactor of lysyl oxidase. Journal of the American Chemical Society. 125: 6113-25. PMID 12785842 DOI: 10.1021/Ja0214274  0.376
2003 Kishishita S, Okajima T, Kim M, Yamaguchi H, Hirota S, Suzuki S, Kuroda S, Tanizawa K, Mure M. Role of copper ion in bacterial copper amine oxidase: spectroscopic and crystallographic studies of metal-substituted enzymes. Journal of the American Chemical Society. 125: 1041-55. PMID 12537504 DOI: 10.1021/Ja017899K  0.433
2002 Mure M, Mills SA, Klinman JP. Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry. 41: 9269-78. PMID 12135347 DOI: 10.1021/Bi020246B  0.379
1997 Wang SX, Nakamura N, Mure M, Klinman JP, Sanders-Loehr J. Characterization of the native lysine tyrosylquinone cofactor in lysyl oxidase by Raman spectroscopy. The Journal of Biological Chemistry. 272: 28841-4. PMID 9360949 DOI: 10.1074/Jbc.272.46.28841  0.425
1996 Wang SX, Mure M, Medzihradszky KF, Burlingame AL, Brown DE, Dooley DM, Smith AJ, Kagan HM, Klinman JP. A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. Science (New York, N.Y.). 273: 1078-84. PMID 8688089 DOI: 10.1126/Science.273.5278.1078  0.372
1995 Moënne-Loccoz P, Nakamura N, Steinebach V, Duine JA, Mure M, Klinman JP, Sanders-Loehr J. Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy. Biochemistry. 34: 7020-6. PMID 7766611 DOI: 10.1021/Bi00021A013  0.387
1995 Mure M, Klinman JP. Model studies of topaquinone-dependent amine oxidases. 2. Characterization of reaction intermediates and mechanism Journal of the American Chemical Society. 117: 8707-8718. DOI: 10.1021/Ja00139A003  0.302
1995 Mure M, Klinman JP. Model studies of topaquinone-dependent amine oxidases. 1. Oxidation of benzylamine by topaquinone analogs Journal of the American Chemical Society. 117: 8698-8706. DOI: 10.1021/Ja00139A002  0.322
1993 Mure M, Klinman JP. Synthesis and spectroscopic characterization of model compounds for the active site cofactor in copper amine oxidases Journal of the American Chemical Society. 115: 7117-7127. DOI: 10.1021/Ja00069A008  0.345
1992 Janes SM, Palcic MM, Scaman CH, Smith AJ, Brown DE, Dooley DM, Mure M, Klinman JP. Identification of topaquinone and its consensus sequence in copper amine oxidases Biochemistry. 31: 12147-12154. DOI: 10.1021/Bi00163A025  0.394
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