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APAF1
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<h2 id="function">Function</h2> <p>The protein was identified in the laboratory of <a href="/facts/Xiaodong_Wang_(biochemist)/djuW8wXB">Xiaodong Wang</a> as an activator of caspase-3 in the presence of cytochromeC and dATP.<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> This gene encodes a cytoplasmic protein that forms one of the central hubs in the <a href="/facts/Apoptosis/8dVzSm4y">apoptosis</a> regulatory network. This protein contains (from the N terminal) a caspase recruitment domain (<a href="/facts/CARD_domain/ySJupuCo">CARD</a>), an <a href="/facts/ATPase/8aEJlNgl">ATPase</a> domain (NB-ARC), few short helical domains and then several copies of the <a href="/facts/WD40_repeat/0DxvU1fg">WD40 repeat</a> domain. Upon binding <a href="/facts/Cytochrome_c/8gXbxw9z">cytochrome c</a> and <a href="/facts/Deoxyadenosine_triphosphate/mn1qjUy9">dATP</a>, this protein forms an oligomeric <a href="/facts/Apoptosome/LgvlRKQg">apoptosome</a>. The apoptosome binds and cleaves Procaspase-9 protein, releasing its mature, activated form. The precise mechanism for this reaction is still debated though work published by <a href="/facts/Guy_Salvesen/QY16gYbp">Guy Salvesen</a> suggests that the apoptosome may induce <a href="/facts/Caspase-9/faVbBt1M">caspase-9</a> dimerization and subsequent <a href="/facts/Autocatalysis/2eGCpunY">autocatalysis</a>.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> Activated caspase-9 stimulates the subsequent caspase cascade that commits the cell to apoptosis. </p><p><a href="/facts/Alternative_splicing/nNRwPVNK">Alternative splicing</a> results in several transcript variants encoding different isoforms.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p> <h2 id="structure">Structure</h2> <p>APAF1 contains a <a href="/facts/CARD_domain/ySJupuCo">CARD domain</a> with a <a href="/facts/Beta_sheet/B6mwwR6H">Greek key</a> motif composed of six helices, a Rossman fold nucleotide binding domains, a short helical motif and a winged-helix domain.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>APAF1 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/APIP/0o2eIQQx">APIP</a>,<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a></li> <li><a href="/facts/BCL2-like_1_(gene)/frra0AA2">BCL2-like 1</a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a></li> <li><a href="/facts/Caspase-9/faVbBt1M">Caspase-9</a>,<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a></li> <li><a href="/facts/HSPA4/R1Gjs8Nn">HSPA4</a>,<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> and</li> <li><a href="/facts/NLRP1/4Vvn7IGe">NLRP1</a>.<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Smith TF, Gaitatzes C, Saxena K, Neer EJ (May 1999). <a href="https://doi.org/10.1016%2FS0968-0004%2899%2901384-5">"The WD repeat: a common architecture for diverse functions"</a>. <i>Trends in Biochemical Sciences</i>. 24 (5): 181–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0968-0004%2899%2901384-5">10.1016/S0968-0004(99)01384-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10322433">10322433</a>.</li> <li>van Oirschot JT (Aug 1999). "Diva vaccines that reduce virus transmission". <i>Journal of Biotechnology</i>. 73 (2–3): 195–205. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0168-1656%2899%2900121-2">10.1016/S0168-1656(99)00121-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10486928">10486928</a>.</li> <li>Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (Jun 2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". <i>DNA Research</i>. 9 (3): 99–106. <a href="/facts/CiteSeerX_(identifier)/SceDmd3c">CiteSeerX</a> <a href="https://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.500.923">10.1.1.500.923</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fdnares%2F9.3.99">10.1093/dnares/9.3.99</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12168954">12168954</a>.</li> <li>Campioni M, Santini D, Tonini G, Murace R, Dragonetti E, Spugnini EP, Baldi A (Nov 2005). <a href="https://doi.org/10.1111%2Fj.1600-0625.2005.00360.x">"Role of Apaf-1, a key regulator of apoptosis, in melanoma progression and chemoresistance"</a>. <i>Experimental Dermatology</i>. 14 (11): 811–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1111%2Fj.1600-0625.2005.00360.x">10.1111/j.1600-0625.2005.00360.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16232302">16232302</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:45588573">45588573</a>.</li> <li>Zou H, Henzel WJ, Liu X, Lutschg A, Wang X (Aug 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980501-2">"Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3"</a>. <i>Cell</i>. 90 (3): 405–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980501-2">10.1016/S0092-8674(00)80501-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9267021">9267021</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:18105320">18105320</a>.</li> <li>Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (Nov 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980434-1">"Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade"</a>. <i>Cell</i>. 91 (4): 479–89. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980434-1">10.1016/S0092-8674(00)80434-1</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9390557">9390557</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:14321446">14321446</a>.</li> <li>Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Oct 1997). <a href="https://doi.org/10.1093%2Fdnares%2F4.5.307">"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro"</a>. <i>DNA Research</i>. 4 (5): 307–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fdnares%2F4.5.307">10.1093/dnares/4.5.307</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9455477">9455477</a>.</li> <li>Pan G, O'Rourke K, Dixit VM (Mar 1998). <a href="https://doi.org/10.1074%2Fjbc.273.10.5841">"Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex"</a>. <i>The Journal of Biological Chemistry</i>. 273 (10): 5841–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.10.5841">10.1074/jbc.273.10.5841</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9488720">9488720</a>.</li> <li>Hu Y, Benedict MA, Wu D, Inohara N, Núñez G (Apr 1998). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22498">"Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation"</a>. <i>Proceedings of the National Academy of Sciences of the United States of America</i>. 95 (8): 4386–91. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998PNAS...95.4386H">1998PNAS...95.4386H</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.95.8.4386">10.1073/pnas.95.8.4386</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22498">22498</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9539746">9539746</a>.</li> <li>Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES (Jun 1998). <a href="https://doi.org/10.1016%2FS1097-2765%2800%2980095-7">"Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization"</a>. <i>Molecular Cell</i>. 1 (7): 949–57. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1097-2765%2800%2980095-7">10.1016/S1097-2765(00)80095-7</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9651578">9651578</a>.</li> <li>Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P (Sep 1998). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981732-8">"Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development"</a>. <i>Cell</i>. 94 (6): 727–37. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2981732-8">10.1016/S0092-8674(00)81732-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9753320">9753320</a>.</li> <li>Inohara N, Gourley TS, Carrio R, Muñiz M, Merino J, Garcia I, Koseki T, Hu Y, Chen S, Núñez G (Dec 1998). <a href="https://doi.org/10.1074%2Fjbc.273.49.32479">"Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-independent cell death"</a>. <i>The Journal of Biological Chemistry</i>. 273 (49): 32479–86. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.49.32479">10.1074/jbc.273.49.32479</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9829980">9829980</a>.</li> <li>Hu Y, Ding L, Spencer DM, Núñez G (Dec 1998). <a href="https://doi.org/10.1074%2Fjbc.273.50.33489">"WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation"</a>. <i>The Journal of Biological Chemistry</i>. 273 (50): 33489–94. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.50.33489">10.1074/jbc.273.50.33489</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9837928">9837928</a>.</li> <li>Song Q, Kuang Y, Dixit VM, Vincenz C (Jan 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171112">"Boo, a novel negative regulator of cell death, interacts with Apaf-1"</a>. <i>The EMBO Journal</i>. 18 (1): 167–78. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F18.1.167">10.1093/emboj/18.1.167</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171112">1171112</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9878060">9878060</a>.</li> <li>Slee EA, Harte MT, Kluck RM, Wolf BB, Casiano CA, Newmeyer DD, Wang HG, Reed JC, Nicholson DW, Alnemri ES, Green DR, Martin SJ (Jan 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132895">"Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner"</a>. <i>The Journal of Cell Biology</i>. 144 (2): 281–92. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.144.2.281">10.1083/jcb.144.2.281</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132895">2132895</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9922454">9922454</a>.</li> <li>Zou H, Li Y, Liu X, Wang X (Apr 1999). <a href="https://doi.org/10.1074%2Fjbc.274.17.11549">"An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9"</a>. <i>The Journal of Biological Chemistry</i>. 274 (17): 11549–56. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.274.17.11549">10.1074/jbc.274.17.11549</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10206961">10206961</a>.</li> <li>Saleh A, Srinivasula SM, Acharya S, Fishel R, Alnemri ES (Jun 1999). <a href="https://doi.org/10.1074%2Fjbc.274.25.17941">"Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation"</a>. <i>The Journal of Biological Chemistry</i>. 274 (25): 17941–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.274.25.17941">10.1074/jbc.274.25.17941</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10364241">10364241</a>.</li> <li>Qin H, Srinivasula SM, Wu G, Fernandes-Alnemri T, Alnemri ES, Shi Y (Jun 1999). "Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1". <i>Nature</i>. 399 (6736): 549–57. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1999Natur.399..549Q">1999Natur.399..549Q</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F21124">10.1038/21124</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10376594">10376594</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4403525">4403525</a>.</li> <li>Drosopoulos NE, Walsh FS, Doherty P (Jun 1999). "A soluble version of the receptor-like protein tyrosine phosphatase kappa stimulates neurite outgrowth via a Grb2/MEK1-dependent signaling cascade". <i>Molecular and Cellular Neurosciences</i>. 13 (6): 441–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fmcne.1999.0758">10.1006/mcne.1999.0758</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10383829">10383829</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:35458154">35458154</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>"Entrez Gene: APAF1 apoptotic peptidase activating factor 1". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Zou H, Henzel WJ, Liu X, Lutschg A, Wang X (Aug 1997). "Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3". Cell. 90 (3): 405–13. doi:10.1016/S0092-8674(00)80501-2. PMID 9267021. S2CID 18105320. <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980501-2" target="_blank">https://doi.org/10.1016%2FS0092-8674%2800%2980501-2</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Kim H, Jung YK, Kwon YK, Park SH (1999). "Assignment of apoptotic protease activating factor-1 gene (APAF1) to human chromosome band 12q23 by fluorescence in situ hybridization". Cytogenetics and Cell Genetics. 87 (3–4): 252–3. doi:10.1159/000015436. PMID 10702682. S2CID 10377371. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X (Nov 1997). "Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade". Cell. 91 (4): 479–89. doi:10.1016/s0092-8674(00)80434-1. PMID 9390557. S2CID 14321446. <a href="https://doi.org/10.1016%2Fs0092-8674%2800%2980434-1" target="_blank">https://doi.org/10.1016%2Fs0092-8674%2800%2980434-1</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Pop C, Timmer J, Sperandio S, Salvesen GS (Apr 2006). "The apoptosome activates caspase-9 by dimerization". Molecular Cell. 22 (2): 269–75. doi:10.1016/j.molcel.2006.03.009. PMID 16630894. <a href="https://doi.org/10.1016%2Fj.molcel.2006.03.009" target="_blank">https://doi.org/10.1016%2Fj.molcel.2006.03.009</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>"Entrez Gene: APAF1 apoptotic peptidase activating factor 1". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Riedl SJ, Li W, Chao Y, Schwarzenbacher R, Shi Y (Apr 2005). "Structure of the apoptotic protease-activating factor 1 bound to ADP". Nature. 434 (7035): 926–33. Bibcode:2005Natur.434..926R. doi:10.1038/nature03465. PMID 15829969. S2CID 4355459. <a href="/wiki/Bibcode_(identifier)" target="_blank">/wiki/Bibcode_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Cho DH, Hong YM, Lee HJ, Woo HN, Pyo JO, Mak TW, Jung YK (Sep 2004). "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein". The Journal of Biological Chemistry. 279 (38): 39942–50. doi:10.1074/jbc.M405747200. PMID 15262985. <a href="https://doi.org/10.1074%2Fjbc.M405747200" target="_blank">https://doi.org/10.1074%2Fjbc.M405747200</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Hu Y, Benedict MA, Wu D, Inohara N, Núñez G (Apr 1998). "Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation". Proceedings of the National Academy of Sciences of the United States of America. 95 (8): 4386–91. Bibcode:1998PNAS...95.4386H. doi:10.1073/pnas.95.8.4386. PMC 22498. PMID 9539746. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22498" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC22498</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Pan G, O'Rourke K, Dixit VM (Mar 1998). "Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex". The Journal of Biological Chemistry. 273 (10): 5841–5. doi:10.1074/jbc.273.10.5841. PMID 9488720. <a href="https://doi.org/10.1074%2Fjbc.273.10.5841" target="_blank">https://doi.org/10.1074%2Fjbc.273.10.5841</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Chu ZL, Pio F, Xie Z, Welsh K, Krajewska M, Krajewski S, Godzik A, Reed JC (Mar 2001). "A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis". The Journal of Biological Chemistry. 276 (12): 9239–45. doi:10.1074/jbc.M006309200. 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