Bak
“Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity”. Proceedings of the National Academy of Sciences of the United States of America 97 (2): 577–82. (January 2000). Bibcode: 2000PNAS...97..577S. doi:10.1073/pnas.97.2.577. PMC 15372. PMID 10639121. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC15372/.
“MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain”. The Journal of Biological Chemistry 275 (33): 25255–61. (August 2000). doi:10.1074/jbc.M909826199. PMID 10837489.
“tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c”.
“Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis”. Science 275 (5302): 983–6. (February 1997). doi:10.1126/science.275.5302.983. PMID 9020082.
“A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members”. The Journal of Biological Chemistry 272 (17): 11350–5. (April 1997). doi:10.1074/jbc.272.17.11350. PMID 9111042.
“The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4”. The EMBO Journal 17 (4): 1029–39. (February 1998). doi:10.1093/emboj/17.4.1029. PMC 1170452. PMID 9463381. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170452/.