@article{widlak_dff40cad_2000,
	title = {The {DFF40}/{CAD} endonuclease and its role in apoptosis.},
	volume = {47},
	copyright = {Copyright (c)},
	issn = {1734-154X},
	url = {https://ojs.ptbioch.edu.pl/index.php/abp/article/view/3957},
	doi = {10.18388/abp.2000_3957},
	abstract = {The sequential generation of large-scale DNA fragments followed by internucleosomal chromatin fragmentation is a biochemical hallmark of apoptosis. One of the nucleases primarily responsible for genomic DNA fragmentation during apoptosis is called DNA Fragmentation Factor 40 (DFF40) or Caspase-activated DNase (CAD). DFF40/CAD is a magnesium-dependent endonuclease specific for double stranded DNA that generates double strand breaks with 3'-hydroxyl ends. DFF40/CAD is activated by caspase-3 that cuts the nuclease's inhibitor DFF45/ICAD. The nuclease preferentially attacks chromatin in the internucleosomal linker DNA. However, the nuclease hypersensitive sites can be detected and DFF40/CAD is potentially involved in large-scale DNA fragmentation as well. DFF40/CAD-mediated DNA fragmentation triggers chromatin condensation that is another hallmark of apoptosis.},
	language = {en},
	number = {4},
	urldate = {2022-04-11},
	journal = {Acta Biochimica Polonica},
	author = {Widłak, P.},
	month = dec,
	year = {2000},
	note = {Number: 4},
	pages = {1037--1044},
}

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