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	1.	[2Fe-2S]-ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin. [electronic resource] by Kim, Jin Hae Frederick, Ronnie O Reinen, Nichole M Troupis, Andrew T Markley, John L Producer: 20140930 In: Journal of the American Chemical Society vol. 135 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	2.	Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). [electronic resource] by Cai, Kai Frederick, Ronnie O Kim, Jin Hae Reinen, Nichole M Tonelli, Marco Markley, John L Producer: 20131203 In: The Journal of biological chemistry vol. 288 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	3.	Solution structure of the 2A protease from a common cold agent, human rhinovirus C2, strain W12. [electronic resource] by Lee, Woonghee Watters, Kelly E Troupis, Andrew T Reinen, Nichole M Suchy, Fabian P Moyer, Kylie L Frederick, Ronnie O Tonelli, Marco Aceti, David J Palmenberg, Ann C Markley, John L Producer: 20151020 In: PloS one vol. 9 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)