1Gupta, S., Chai, J., Cheng, J., D'Mello, R., Chance, MC, and Fu, D., Visualizing the kinetic power stroke that drives proton-coupled Zn(II) transport. Nature, 512(7512):101-4 (2014),
2Hoch E., Lin W., Chai J., Hershfinkel M., Fu D., Sekler I. Histidine pairing at the metal transport site of mammalian ZnT transporter controls Zn2+ over Cd2+ selectivity. Proc Natl Acad Sci U.S.A.,109(19):7202-7207 (2012).
3Fu, D. Zinc transporter YiiP from Escherichia coli., book chapter in Handbook of Metalloprotein, volume 4&5 (2011) (edited by Albrecht Messerschmidt, published by Wiley-Balchwell).
4Lin W., Chai J., Love J. and Fu D. Selective electrodiffusion of zinc ions in a Zrt-, Irt-like protein, ZIPB. J Biol Chem., 285(50):39013-20 (2010). This paper was selected as a paper-of-the-week and featured on the journal cover.
5Lu M., Chai J. and Fu D. Structural basis for autoregulation of the zinc transporter YiiP. Nat. Struct. Mol. Biol., 16(10):1063-1067 (2009).
6Lu M. and Fu D. Structure of the zinc transport YiiP. Science, 317:1746-8 (2007). This paper was selected as a Science highlight.
7Wei Y. and Fu D. Binding and transport of metal ions at the dimer interface of the Escherichia coli metal transporter YiiP. J Biol Chem., 281(33):23492-23502 (2006).
8Wei Y. and Fu D. Selective metal binding to a membrane-embedded aspartate in the Escherichia coli metal transporter YiiP (FieF). J Biol Chem., 280(40):33716-33724 (2005).
9Wei Y., Li H. and Fu D. Oligomeric state of the Escherichia coli metal transporter YiiP. J Biol Chem., 279(38):39251-39259 (2004).
10Chao Y. and Fu D. Thermodynamic studies of the mechanism of metal binding to the Escherichia coli zinc transporter YiiP. J Biol Chem., 279(17):17173-17180(2004).
11Chao Y and Fu D. Kinetic study of the antiport mechanism of an Escherichia coli zinc transporter, ZitB. J Biol Chem., 279(13):12043-12050 (2004).
aSladek, R. et al., A genome-wide association study identifies novel risk loci for type 2 diabetes. Nature. 445 (7130), 881 (2007)
bWenzlau, J.M. et al. The cation efflux transporter ZnT8 (Slc30A8) is a major autoantigen in human type 1 diabetes. Proc Natl Acad Sci U S A. 104, 17040-5. (2007)
cFlannick, J. et al., Loss-of-function mutations in SLC30A8 protect against type 2 diabetes. Nat Genet 46, 357-63 (2014)