This gene encodes a pro-survival (anti-
apoptotic) member of the
bcl-2 protein family, and is most similar to
Bcl-xL.[7] The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under
cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of
NGF- and
BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult
spermatogenesis.[6][9][7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA,
Sutherland GR, Baker E, Adams JM, Cory S (October 1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75.
PMID8761287.
^Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75.
PMID8761287.
^Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (October 2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30.
doi:
10.1023/A:1011319901057.
PMID11483855.
S2CID23119757.
Bae J, Hsu SY, Leo CP, et al. (2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30.
doi:
10.1023/A:1011319901057.
PMID11483855.
S2CID23119757.
Denisov AY, Chen G, Sprules T, et al. (2006). "Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles". Biochemistry. 45 (7): 2250–6.
doi:
10.1021/bi052332s.
PMID16475813.
This gene encodes a pro-survival (anti-
apoptotic) member of the
bcl-2 protein family, and is most similar to
Bcl-xL.[7] The proteins of this family form hetero- or homodimers and act as anti- and pro-apoptotic regulators. Expression of this gene in cells has been shown to contribute to reduced cell apoptosis under
cytotoxic conditions. Studies of the related gene in mice indicated a role in the survival of
NGF- and
BDNF-dependent neurons. Mutation and knockout studies of the mouse gene demonstrated an essential role in adult
spermatogenesis.[6][9][7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Gibson L, Holmgreen SP, Huang DC, Bernard O, Copeland NG, Jenkins NA,
Sutherland GR, Baker E, Adams JM, Cory S (October 1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75.
PMID8761287.
^Gibson L, Holmgreen SP, Huang DC, et al. (1996). "bcl-w, a novel member of the bcl-2 family, promotes cell survival". Oncogene. 13 (4): 665–75.
PMID8761287.
^Bae J, Hsu SY, Leo CP, Zell K, Hsueh AJ (October 2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30.
doi:
10.1023/A:1011319901057.
PMID11483855.
S2CID23119757.
Bae J, Hsu SY, Leo CP, et al. (2001). "Underphosphorylated BAD interacts with diverse antiapoptotic Bcl-2 family proteins to regulate apoptosis". Apoptosis. 6 (5): 319–30.
doi:
10.1023/A:1011319901057.
PMID11483855.
S2CID23119757.
Denisov AY, Chen G, Sprules T, et al. (2006). "Structural model of the BCL-w-BID peptide complex and its interactions with phospholipid micelles". Biochemistry. 45 (7): 2250–6.
doi:
10.1021/bi052332s.
PMID16475813.