Selected Publications for David Chan

Chen, H., and Chan, D. C. (2005). Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 14 Spec No. 2, R283-289.

Griffin, E. E., Graumann, J., and Chan, D. C. (2005). The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J Cell Biol 170, 237-248.

Chen, H., Chomyn, A., and Chan, D. C. (2005). Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280, 26185-26192.

Suntoke, T. R., and Chan, D. C. (2005). The fusion activity of HIV-1 gp41 depends on interhelical interactions. J Biol Chem 280, 19852-19857.

Koshiba, T., Detmer, S. A., Kaiser, J. T., Chen, H., McCaffery, J. M., and Chan, D. C. (2004). Structural basis of mitochondrial tethering by mitofusin complexes. Science 305, 858-862.

Karbowski, M., Arnoult, D., Chen, H., Chan, D. C., Smith, C. L., and Youle, R. J. (2004). Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J Cell Biol 164, 493-499.

Chen, H., and Chan, D. C. (2004). Mitochondrial dynamics in mammals. Curr Top Dev Biol 59, 119-144.

Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., and Chan, D. C. (2003). Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J Cell Biol 160, 189-200.

Koshiba, T., and Chan, D. C. (2003). The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J Biol Chem 278, 7573-7579.

Chan, D. C., and Kim, P. S. (1998). HIV entry and its inhibition. Cell 93, 681-684.

Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998). Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc Natl Acad Sci U S A 95, 15613-15617.

Malashkevich, V. N., Chan, D. C., Chutkowski, C. T., and Kim, P. S. (1998). Crystal structure of the simian immunodeficiency virus (SIV) gp41 core: conserved helical interactions underlie the broad inhibitory activity of gp41 peptides. Proc Natl Acad Sci U S A 95, 9134-9139.

Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997). Core structure of gp41 from the HIV envelope glycoprotein. Cell 89, 263-273.