{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T03:49:51Z","timestamp":1791258591724,"version":"4.1.0"},"reference-count":68,"publisher":"Elsevier BV","issue":"30","license":[{"start":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T00:00:00Z","timestamp":1372636800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,7]],"date-time":"2020-09-07T00:00:00Z","timestamp":1599436800000},"content-version":"vor","delay-in-days":2625,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,7]]},"DOI":"10.1074\/jbc.m113.471821","type":"journal-article","created":{"date-parts":[[2013,6,12]],"date-time":"2013-06-12T01:18:02Z","timestamp":1370999882000},"page":"21898-21908","source":"Crossref","is-referenced-by-count":20,"title":["Structural and Biophysical Characterization of the Interactions between the Death Domain of Fas Receptor and Calmodulin"],"prefix":"10.1016","volume":"288","author":[{"given":"Timothy F.","family":"Fernandez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandra B.","family":"Samal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory J.","family":"Bedwell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yabing","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jamil S.","family":"Saad","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.471821_bib1","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1080\/01926230701320337","article-title":"Apoptosis. A review of programmed cell death","volume":"35","author":"Elmore","year":"2007","journal-title":"Toxicol Pathol"},{"key":"10.1074\/jbc.M113.471821_bib2","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1016\/S0002-9440(10)65649-0","article-title":"Histopathological evaluation of apoptosis in cancer","volume":"153","author":"Soini","year":"1998","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.M113.471821_bib3","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0092-8674(91)90614-5","article-title":"The polypeptide encoded by the cDNA for human cell surface antigen Fas can mediate apoptosis","volume":"66","author":"Itoh","year":"1991","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.471821_bib4","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1007\/978-3-540-69184-6_3","article-title":"The death receptors","volume":"23","author":"Peter","year":"1999","journal-title":"Results Probl. Cell Differ"},{"key":"10.1074\/jbc.M113.471821_bib5","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1038\/sj.leu.2402169","article-title":"The kiss of death. Promises and failures of death receptors and ligands in cancer therapy","volume":"15","author":"Daniel","year":"2001","journal-title":"Leukemia"},{"key":"10.1074\/jbc.M113.471821_bib6","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1016\/S0960-9822(02)70791-4","article-title":"Apo-3, a new member of the tumor necrosis factor receptor family, contains a death domain and activates apoptosis and NF-\u03baB","volume":"6","author":"Marsters","year":"1996","journal-title":"Curr. Biol"},{"key":"10.1074\/jbc.M113.471821_bib7","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/0092-8674(95)90071-3","article-title":"FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis","volume":"81","author":"Chinnaiyan","year":"1995","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.471821_bib8","doi-asserted-by":"crossref","first-page":"1019","DOI":"10.1038\/nature07606","article-title":"The Fas-FADD death domain complex structure unravels signalling by receptor clustering","volume":"457","author":"Scott","year":"2009","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.471821_bib9","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1038\/nri2570","article-title":"CD95, BIM, and T cell homeostasis","volume":"9","author":"Bouillet","year":"2009","journal-title":"Nat. Rev. Immunol"},{"key":"10.1074\/jbc.M113.471821_bib10","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1038\/nsmb.1920","article-title":"The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations","volume":"17","author":"Wang","year":"2010","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.471821_bib11","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1002\/jcb.21447","article-title":"Calmodulin binding to the Fas-mediated death-inducing signaling complex in cholangiocarcinoma cells","volume":"103","author":"Chen","year":"2008","journal-title":"J. Cell. Biochem"},{"key":"10.1074\/jbc.M113.471821_bib12","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/S0002-9440(10)63563-8","article-title":"The combination of calmodulin antagonists and interferon-\u03b3 induces apoptosis through caspase-dependent and -independent pathways in cholangiocarcinoma cells","volume":"163","author":"Ahn","year":"2003","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.M113.471821_bib13","doi-asserted-by":"crossref","first-page":"5661","DOI":"10.1074\/jbc.M311040200","article-title":"Calmodulin binding to the Fas death domain. Regulation by Fas activation","volume":"279","author":"Ahn","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib14","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1158\/1078-0432.CCR-08-1150","article-title":"Molecular mechanisms of tamoxifen therapy for cholangiocarcinoma. Role of calmodulin","volume":"15","author":"Pawar","year":"2009","journal-title":"Clin. Cancer res"},{"key":"10.1074\/jbc.M113.471821_bib15","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1042\/BJ20071507","article-title":"Calmodulin binding to cellular FLICE-like inhibitory protein modulates Fas-induced signalling","volume":"412","author":"Pawar","year":"2008","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M113.471821_bib16","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1002\/hep.510300618","article-title":"Cholangiocarcinomas express Fas ligand and disable the Fas receptor","volume":"30","author":"Que","year":"1999","journal-title":"Hepatology"},{"key":"10.1074\/jbc.M113.471821_bib17","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/S0002-9440(10)65113-9","article-title":"Apoptosis and tumorigenesis in human cholangiocarcinoma cells. Involvement of Fas\/APO-1 (CD95) and calmodulin","volume":"155","author":"Pan","year":"1999","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.M113.471821_bib18","doi-asserted-by":"crossref","first-page":"24776","DOI":"10.1074\/jbc.M110.202804","article-title":"Calmodulin mediates Fas-induced FADD-independent survival signaling in pancreatic cancer cells via activation of Src-extracellular signal-regulated kinase (ERK)","volume":"286","author":"Yuan","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib19","first-page":"2571","article-title":"Positive correlation between calmodulin content and hepatoma growth rates","volume":"42","author":"Wei","year":"1982","journal-title":"Cancer Res"},{"key":"10.1074\/jbc.M113.471821_bib20","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1016\/S0962-8924(00)01800-6","article-title":"Calmodulin. A prototypical calcium sensor","volume":"10","author":"Chin","year":"2000","journal-title":"Trends Cell Biol"},{"key":"10.1074\/jbc.M113.471821_bib21","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1016\/S0092-8674(02)00682-7","article-title":"Calmodulin in action. Diversity in target recognition and activation mechanisms","volume":"108","author":"Hoeflich","year":"2002","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.471821_bib22","doi-asserted-by":"crossref","first-page":"455","DOI":"10.2174\/092986606776819600","article-title":"Protein-peptide interaction studies demonstrate the versatility of calmodulin target protein binding","volume":"13","author":"Ishida","year":"2006","journal-title":"Protein Pept. Lett"},{"key":"10.1074\/jbc.M113.471821_bib23","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1038\/12271","article-title":"A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase","volume":"6","author":"Osawa","year":"1999","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.M113.471821_bib24","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1046\/j.1432-1033.2003.03414.x","article-title":"Novel aspects of calmodulin target recognition and activation","volume":"270","author":"Vetter","year":"2003","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M113.471821_bib25","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1385\/MB:27:1:33","article-title":"Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides","volume":"27","author":"Yamniuk","year":"2004","journal-title":"Mol. Biotechnol"},{"key":"10.1074\/jbc.M113.471821_bib26","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1038\/nsb0196-12","article-title":"EF-hands reach out","volume":"3","author":"Kretsinger","year":"1996","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.M113.471821_bib27","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1080\/07391102.2001.10506719","article-title":"Conformation and structural transitions in the EF-hands of calmodulin","volume":"19","author":"Moorthy","year":"2001","journal-title":"J. Biomol. Struct. Dyn"},{"key":"10.1074\/jbc.M113.471821_bib28","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1002\/(SICI)1097-0134(19991115)37:3<499::AID-PROT17>3.0.CO;2-Y","article-title":"Diversity of conformational states and changes within the EF-hand protein superfamily","volume":"37","author":"Yap","year":"1999","journal-title":"Proteins"},{"key":"10.1074\/jbc.M113.471821_bib29","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1038\/384638a0","article-title":"NMR structure and mutagenesis of the Fas (APO-1\/CD95) death domain","volume":"384","author":"Huang","year":"1996","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.471821_bib30","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1002\/1096-9896(2000)9999:9999<::AID-PATH759>3.0.CO;2-A","article-title":"Somatic mutations in the death domain of the Fas (apo-1\/CD95) gene in gastric cancer","volume":"193","author":"Park","year":"2001","journal-title":"J. Pathol"},{"key":"10.1074\/jbc.M113.471821_bib31","first-page":"1382","article-title":"Frequent mutations of Fas gene in thyroid lymphoma","volume":"61","author":"Takakuwa","year":"2001","journal-title":"Cancer Res"},{"key":"10.1074\/jbc.M113.471821_bib32","doi-asserted-by":"crossref","first-page":"5913","DOI":"10.1529\/biophysj.108.130542","article-title":"Conformation and free energy analyses of the complex of calcium-bound calmodulin and the Fas death domain","volume":"95","author":"Suever","year":"2008","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M113.471821_bib33","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1038\/356314a0","article-title":"Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis","volume":"356","author":"Watanabe-Fukunaga","year":"1992","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.471821_bib34","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1097\/00000658-200206000-00016","article-title":"Tamoxifen (TMX)\/Fas induced growth inhibition of human cholangiocarcinoma (HCC) by \u03b3 interferon (IFN-\u03b3)","volume":"235","author":"Vickers","year":"2002","journal-title":"Ann. Surg"},{"key":"10.1074\/jbc.M113.471821_bib35","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/bjc.1997.153","article-title":"Tamoxifen, 17\u03b2-oestradiol and the calmodulin antagonist J8 inhibit human melanoma cell invasion through fibronectin","volume":"75","author":"Dewhurst","year":"1997","journal-title":"Br. J. Cancer"},{"key":"10.1074\/jbc.M113.471821_bib36","first-page":"249","article-title":"Inhibition of lung metastasis by a calmodulin antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), in mice bearing Lewis lung carcinoma","volume":"11","author":"Ito","year":"1991","journal-title":"Anticancer Res"},{"key":"10.1074\/jbc.M113.471821_bib37","doi-asserted-by":"crossref","first-page":"33533","DOI":"10.1074\/jbc.M111.273623","article-title":"NMR, biophysical, and biochemical studies reveal the minimal calmodulin-binding domain of the HIV-1 matrix protein","volume":"286","author":"Samal","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib38","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1110\/ps.0207702","article-title":"Modern analytical ultracentrifugation in protein science. A tutorial review","volume":"11","author":"Lebowitz","year":"2002","journal-title":"Protein. Sci"},{"key":"10.1074\/jbc.M113.471821_bib39","doi-asserted-by":"crossref","first-page":"1606","DOI":"10.1016\/S0006-3495(00)76713-0","article-title":"Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling","volume":"78","author":"Schuck","year":"2000","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M113.471821_bib40","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/S0003-2697(03)00289-6","article-title":"On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation","volume":"320","author":"Schuck","year":"2003","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.M113.471821_bib41","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1016\/S0006-3495(02)75469-6","article-title":"Size-distribution analysis of proteins by analytical ultracentrifugation. Strategies and application to model systems","volume":"82","author":"Schuck","year":"2002","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M113.471821_bib42","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe. A multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.M113.471821_bib43","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1007\/BF00404272","article-title":"NMRview. A computer program for the visualization and analysis of NMR data","volume":"4","author":"Johnson","year":"1994","journal-title":"J. Biomol. NMR"},{"key":"10.1074\/jbc.M113.471821_bib44","doi-asserted-by":"crossref","first-page":"4659","DOI":"10.1021\/bi00471a022","article-title":"A novel approach for sequential assignment of 1H, 13C, and 15N spectra of larger proteins. Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin","volume":"29","author":"Ikura","year":"1990","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.471821_bib45","doi-asserted-by":"crossref","first-page":"41911","DOI":"10.1074\/jbc.M110.179093","article-title":"Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure","volume":"285","author":"Ghanam","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib46","series-title":"NMR of Proteins and Nucleic Acids","author":"W\u00fcthrich","year":"1986"},{"key":"10.1074\/jbc.M113.471821_bib47","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1126\/science.2377896","article-title":"Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1\u03b2 in solution","volume":"249","author":"Kay","year":"1990","journal-title":"Science"},{"key":"10.1074\/jbc.M113.471821_bib48","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1016\/j.str.2010.08.006","article-title":"Solution NMR investigation of the CD95\/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus","volume":"18","author":"Esposito","year":"2010","journal-title":"Structure"},{"key":"10.1074\/jbc.M113.471821_bib49","doi-asserted-by":"crossref","first-page":"1717","DOI":"10.1038\/sj.cdd.4402191","article-title":"Biophysical and cell-based evidence for differential interactions between the death domains of CD95\/Fas and FADD","volume":"14","author":"Ferguson","year":"2007","journal-title":"Cell Death Differ"},{"key":"10.1074\/jbc.M113.471821_bib50","doi-asserted-by":"crossref","first-page":"e5402","DOI":"10.1371\/journal.pone.0005402","article-title":"Domain swapping and different oligomeric states for the complex between calmodulin and the calmodulin-binding domain of calcineurin A","volume":"4","author":"Majava","year":"2009","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M113.471821_bib51","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1126\/science.1585175","article-title":"Solution structure of a calmodulin-target peptide complex by multidimensional NMR","volume":"256","author":"Ikura","year":"1992","journal-title":"Science"},{"key":"10.1074\/jbc.M113.471821_bib52","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1126\/science.1519061","article-title":"Target enzyme recognition by calmodulin. 2.4 \u00c5 structure of a calmodulin-peptide complex","volume":"257","author":"Meador","year":"1992","journal-title":"Science"},{"key":"10.1074\/jbc.M113.471821_bib53","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1006\/jmbi.1997.1524","article-title":"Solution structure of calmodulin-W-7 complex. The basis of diversity in molecular recognition","volume":"276","author":"Osawa","year":"1998","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M113.471821_bib54","doi-asserted-by":"crossref","first-page":"15259","DOI":"10.1021\/bi00255a006","article-title":"Drug binding by calmodulin. Crystal structure of a calmodulin-trifluoperazine complex","volume":"33","author":"Cook","year":"1994","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.471821_bib55","doi-asserted-by":"crossref","first-page":"15300","DOI":"10.1021\/bi980795a","article-title":"Simultaneous binding of drugs with different chemical structures to Ca2+-calmodulin. Crystallographic and spectroscopic studies","volume":"37","author":"Vertessy","year":"1998","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.471821_bib56","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1038\/nsb1194-795","article-title":"Trifluoperazine-induced conformational change in Ca2+-calmodulin","volume":"1","author":"Vandonselaar","year":"1994","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.M113.471821_bib57","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1002\/prot.22739","article-title":"Allosteric effects of the antipsychotic drug trifluoperazine on the energetics of calcium binding by calmodulin","volume":"78","author":"Feldkamp","year":"2010","journal-title":"Proteins"},{"key":"10.1074\/jbc.M113.471821_bib58","doi-asserted-by":"crossref","first-page":"16045","DOI":"10.1074\/jbc.270.27.16045","article-title":"Ligand binding analysis of soluble interleukin-2 receptor complexes by surface plasmon resonance","volume":"270","author":"Wu","year":"1995","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib59","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1023\/A:1011320027914","article-title":"Calmodulin target database","volume":"1","author":"Yap","year":"2000","journal-title":"J. Struct. Funct. Genomics"},{"key":"10.1074\/jbc.M113.471821_bib60","doi-asserted-by":"crossref","first-page":"1833","DOI":"10.2353\/ajpath.2006.060234","article-title":"Fas-mediated apoptosis in cholangiocarcinoma cells is enhanced by 3,3\u2032-diindolylmethane through inhibition of AKT signaling and FLICE-like inhibitory protein","volume":"169","author":"Chen","year":"2006","journal-title":"Am. J. Pathol"},{"key":"10.1074\/jbc.M113.471821_bib61","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1529\/biophysj.104.055780","article-title":"Backbone dynamics of a symmetric calmodulin dimer in complex with the calmodulin-binding domain of the basic-helix-loop-helix transcription factor SEF2\u20131\/E2\u20132. A highly dynamic complex","volume":"89","author":"Larsson","year":"2005","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.M113.471821_bib62","doi-asserted-by":"crossref","first-page":"30328","DOI":"10.1074\/jbc.273.46.30328","article-title":"Calcium-calmodulin-induced dimerization of the carboxyl-terminal domain from petunia glutamate decarboxylase. A novel calmodulin-peptide interaction motif","volume":"273","author":"Yuan","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.471821_bib63","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1046\/j.1432-1327.1999.00284.x","article-title":"Evidence of noncovalent dimerization of calmodulin","volume":"261","author":"Lafitte","year":"1999","journal-title":"Eur. J. Biochem"},{"key":"10.1074\/jbc.M113.471821_bib64","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1016\/j.jmb.2010.05.022","article-title":"Calmodulin disrupts the structure of the HIV-1 MA protein","volume":"400","author":"Chow","year":"2010","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M113.471821_bib65","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1042\/bj2070541","article-title":"A model for the regulation of the calmodulin-dependent enzymes erythrocyte Ca2+-transport ATPase and brain phosphodiesterase by activators and inhibitors","volume":"207","author":"Gietzen","year":"1982","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.M113.471821_bib66","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1016\/j.febslet.2012.04.026","article-title":"Hinge sequences as signaling agents?","volume":"586","author":"Stec","year":"2012","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M113.471821_bib67","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0928-4257(05)80011-7","article-title":"Calmodulin and cell cycle control","volume":"86","author":"Rasmussen","year":"1992","journal-title":"J. Physiol. Paris"},{"key":"10.1074\/jbc.M113.471821_bib68","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1038\/labinvest.2011.131","article-title":"Reduced CaM\/FLIP binding by a single point mutation in c-FLIP(L) modulates Fas-mediated apoptosis and decreases tumorigenesis","volume":"92","author":"Jing","year":"2012","journal-title":"Lab. Invest"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820454869?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820454869?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.471821","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T14:30:03Z","timestamp":1641306603000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820454869"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,7]]},"references-count":68,"journal-issue":{"issue":"30","published-print":{"date-parts":[[2013,7]]}},"alternative-id":["S0021925820454869"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.471821","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,7]]}}}