The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant

By J. Goldstein, N. Waterhouse, P. Juin, G. Evan, Douglas R. Green. Nature Cell Biology, 2000

1,085 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/66423169626dd41371c6694f3a5f42338c11954b

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Citations in the corpus

Mitochondrial membrane permeabilization in cell death. (2007, background): “Using GFP-tagged Cyt c, Green and co-workers (256) found that the release of Cyt c is almost invariably completed in 5 min and precedes the exposure of phosphatidylserine and the loss of plasma membrane integrity.”
Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis (2002, background): “…alternative model, supported by results obtained with artificial membranes, is that Bax directly forms pores (Antonsson et al., 1997; Schlesinger et al., 1997; Basanez et al., 1999) that allow proteins to escape from the mitochondria (Goldstein et al., 2000) into the cytosol to initiate apoptosis.”
Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. (2002, methodology): “Apoptosis mediated by mitochondria Department of Biochemistry requires the release of cytochrome c into the cytosol University of Texas (Liu et al., 1996; Goldstein et al., 2000) through a process Southwestern Medical Center at Dallas that may involve the formation of specific pores or rupDallas, Te”
Bcl-2-family proteins and the role of mitochondria in apoptosis. (2003, result): “The importance of ER Ca2þ release in apoptosis may be both cell-type- and stimulusspecific; if so, this might help explain why some researchers observed evidence of PT in mitochondria before cytochrome c release in dying cells [76,77] while others did not [78–80].”