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For general information on mitochondrial dynamics:
Detmer, S.A., and Chan, D.C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8, 870-879. [PDF]
Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252. [PDF]
Chan, D. C. (2006). Mitochondrial fusion and fission in mammals. Annu Rev Cell Dev Biol 22, 79-99. [PDF]
Selected Publications
Detmer, S.A., Velde, C.V., Cleveland, D.W., and Chan, D.C. (2008). Hindlimb gait defects due to motor axon loss and reduced distal muscles in a transgenic mouse model of Charcot-Marie-Tooth type 2A. Hum Mol Genet 17, 367-375. [PDF]
Zhang, Y., and Chan, D.C. (2007). Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc Natl Acad Sci U S A 104, 18526-18530. [PDF]
Detmer, S.A., and Chan, D.C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8, 870-879. [PDF]
Chen, H., McCaffery, J.M., and Chan, D.C. (2007). Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130, 548-562. [PDF]
Song, Z., Chen, H., Fiket, M., Alexander, C., and Chan, D.C. (2007). OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J Cell Biol 178, 749-755. [PDF]
Chan, D.C. (2007). Mitochondrial dynamics in disease. The New England Journal of Medicine 356, 1707-1709. [PDF]
Detmer, S. A., and Chan, D. C. (2007). Complementation between mouse Mfn1 and Mfn2 protects mitochondrial fusion defects caused by CMT2A disease mutations. J Cell Biol 176, 405-414. [PDF]
Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252. [PDF]
Chan, D. C. (2006). Mitochondrial fusion and fission in mammals. Annu Rev Cell Dev Biol 22, 79-99. [PDF]
Griffin, E. E., Detmer, S. A., and Chan, D. C. (2006). Molecular mechanism of mitochondrial membrane fusion. Biochim Biophys Acta 1763, 482-489. [PDF]
Griffin, E. E., and Chan, D. C. (2006). Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion. J Biol Chem 281, 16599-16606. [PDF]
Chen, H., and Chan, D. C. (2005). Emerging functions of mammalian mitochondrial fusion and fission. Hum Mol Genet 14 Spec No. 2, R283-289. [PDF]
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. [PDF]
Chen, H., Chomyn, A., and Chan, D. C. (2005). Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280, 26185-26192. [PDF] [supplement]
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. [PDF]
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. [PDF]
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. [PDF]
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. [PDF]
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. [PDF]
Chan, D. C., and Kim, P. S. (1998). HIV entry and its inhibition. Cell 93, 681-684. [PDF]
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. [PDF]
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. [PDF]