Relevant Publications

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 (2014), in press

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)