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Max O. Funk

Affiliations: 
The University of Toledo 
Area:
Biochemistry
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"Max Funk"
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Priya S. Shah research assistant 1999-2001 (Cell & Gene Therapy Tree)

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Xu S, Mueser TC, Marnett LJ, et al. (2012) Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis. Structure (London, England : 1993). 20: 1490-7
Arif W, Xu S, Isailovic D, et al. (2011) Complexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfate. Biochemistry. 50: 5806-11
Rapp J, Xu S, Sharp AM, et al. (2009) EPR spectroscopy and electrospray ionization mass spectrometry reveal distinctive features of the iron site in leukocyte 12-lipoxygenase. Archives of Biochemistry and Biophysics. 490: 50-6
Waller TM, Decker I, Frisch JP, et al. (2008) Secondary alkyl hydroperoxides as inhibitors and alternate substrates for lipoxygenase. Biochemistry. 47: 331-338
Peariso AM, Nicholson KM, Benjamin Jones R, et al. (2008) Electrospray ionization mass spectrometry of soybean lipoxygenases: N-terminal acetylation, chemical modification, and solution conformation. Proteins. 70: 650-8
Vahedi-Faridi A, Brault PA, Shah P, et al. (2004) Interaction between Non-Heme Iron of Lipoxygenases and Cumene Hydroperoxide: Basis for Enzyme Activation, Inactivation, and Inhibition Journal of the American Chemical Society. 126: 2006-2015
Brault PA, Kariapper MS, Pham CV, et al. (2002) Protein micelles from lipoxygenase 3. Biomacromolecules. 3: 649-54
Skrzypczak-Jankun E, Bross RA, Carroll RT, et al. (2001) Three-dimensional structure of a purple lipoxygenase. Journal of the American Chemical Society. 123: 10814-20
Kariapper MST, Dunham WR, Funk MO. (2001) Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme. Biochemical and Biophysical Research Communications. 284: 563-567
Pham C, Jankun J, Skrzypczak-Jankun E, et al. (1998) Structural and thermochemical characterization of lipoxygenase-catechol complexes. Biochemistry. 37: 17952-7
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