{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T14:39:18Z","timestamp":1759588758997},"reference-count":140,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2000,6,1]],"date-time":"2000-06-01T00:00:00Z","timestamp":959817600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Advances in Enzyme Regulation"],"published-print":{"date-parts":[[2000,6]]},"DOI":"10.1016\/s0065-2571(99)00030-8","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T02:38:44Z","timestamp":1027651124000},"page":"441-470","source":"Crossref","is-referenced-by-count":18,"title":["Interactions between protein kinases and proteases in cellular signaling and regulation"],"prefix":"10.1016","volume":"40","author":[{"given":"Edwin G","family":"Krebs","sequence":"first","affiliation":[]},{"given":"Jonathan D","family":"Graves","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0065-2571(99)00030-8_BIB1","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/S0021-9258(18)71184-8","article-title":"The enzymatic phosphorylation of protein","volume":"211","author":"Burnett","year":"1954","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB2","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1016\/S0021-9258(18)65911-3","article-title":"The relationship of epinephrine and glucagon to liver phosphorylation","volume":"218","author":"Rall","year":"1956","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB3","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/0006-3002(56)90273-6","article-title":"The phosphorylase b to a converting enzyme of rabbit skeletal muscle","volume":"20","author":"Krebs","year":"1956","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB4","doi-asserted-by":"crossref","first-page":"20745","DOI":"10.1074\/jbc.274.30.20745","article-title":"Proteolytic processing in the secretory pathway","volume":"274","author":"Zhou","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB5","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/S0021-9258(18)43139-0","article-title":"The enzymatic conversion of phosphorylase a to b","volume":"158","author":"Cori","year":"1945","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB6","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0021-9258(19)52289-X","article-title":"Conversion of phosphorylase b to phosphorylase a in muscle extracts","volume":"216","author":"Fischer","year":"1955","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB7","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1021\/bi00846a014","article-title":"Activation of skeletal muscle phosphorylase kinase by Ca2+, II: Identification of the kinase activating factor as a proteolytic enzyme","volume":"7","author":"Huston","year":"1968","journal-title":"Biochemistry"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB8","first-page":"51","article-title":"The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle","volume":"39","author":"Cohen","year":"1974","journal-title":"Biochem. Soc. Symp."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1093\/oxfordjournals.jbchem.a124302","article-title":"Identification of a latent Ca2+\/calmodulin dependent protein kinase II phosphorylation site in vascular calpain II","volume":"115","author":"McClelland","year":"1994","journal-title":"J. Biochem. (Tokyo)"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB10","first-page":"317","article-title":"Modulation of the activity of calpain II by phosphorylation\u2013changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE)","volume":"3","author":"Kuo","year":"1993","journal-title":"Appl. Theor. Electrophor."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB11","first-page":"41","article-title":"Regulation of the phosphorylation of histones and glycogen synthase","volume":"76","author":"Kuo","year":"1993","journal-title":"Cytobios."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB12","doi-asserted-by":"crossref","first-page":"3968","DOI":"10.1016\/S0021-9258(19)67888-9","article-title":"Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells","volume":"266","author":"Adachi","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB13","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1016\/S0955-0674(97)80079-8","article-title":"Roles of ubiquitin-mediated proteolysis in cell cycle control","volume":"9","author":"Hershko","year":"1997","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB14","doi-asserted-by":"crossref","first-page":"4547","DOI":"10.1128\/MCB.19.7.4547","article-title":"Bridging the gap: composition, regulation, and physiological function of the IkappaB kinase complex","volume":"19","author":"Zandi","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB15","doi-asserted-by":"crossref","first-page":"2527","DOI":"10.1101\/gad.10.20.2527","article-title":"Signal transduction through beta-catenin and specification of cell fate during embryogenesis","volume":"10","author":"Miller","year":"1996","journal-title":"Genes Dev."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB16","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1038\/374617a0","article-title":"Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos","volume":"374","author":"He","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB17","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1242\/dev.121.3.755","article-title":"Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3","volume":"121","author":"Pierce","year":"1995","journal-title":"Development."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB18","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1002\/(SICI)1097-4547(19980715)53:2<153::AID-JNR4>3.0.CO;2-6","article-title":"Calcineurin inhibition prevents calpain-mediated proteolysis of tau in differentiated PC12 cells","volume":"53","author":"Xie","year":"1998","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB19","doi-asserted-by":"crossref","first-page":"14282","DOI":"10.1016\/S0021-9258(18)71675-X","article-title":"In situ phosphorylation of platelet actin-binding protein by cAMP- dependent protein kinase stabilizes it against proteolysis by calpain","volume":"264","author":"Chen","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB20","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1002\/(SICI)1097-4547(19960601)44:5<438::AID-JNR4>3.0.CO;2-G","article-title":"Mutual protection of microtubule-associated protein 2 (MAP2) and cyclic AMP-dependent protein kinase II against mu-calpain","volume":"44","author":"Alexa","year":"1996","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB21","doi-asserted-by":"crossref","first-page":"7610","DOI":"10.1016\/S0021-9258(17)41010-6","article-title":"Studies on a cyclic nucleotide-independent protein kinase and its proenzyme in mammalian tissues. II. Proenzyme and its activation by calcium-dependent protease from rat brain","volume":"252","author":"Inoue","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB22","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1016\/S0021-9258(19)85886-6","article-title":"Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover","volume":"255","author":"Kishimoto","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB23","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1126\/science.3014651","article-title":"Studies and perspectives of protein kinase C","volume":"233","author":"Nishizuka","year":"1986","journal-title":"Science."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB24","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1096\/fasebj.1.2.2886390","article-title":"Calcium-dependent proteases: an enzyme system active at cellular membranes?","volume":"1","author":"Mellgren","year":"1987","journal-title":"FASEB J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB25","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1161\/01.HYP.20.5.585","article-title":"Protein kinase C of smooth muscle","volume":"20","author":"Andrea","year":"1992","journal-title":"Hypertension"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB26","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1016\/S0021-9258(18)33173-9","article-title":"Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease","volume":"258","author":"Kishimoto","year":"1983","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB27","doi-asserted-by":"crossref","first-page":"8309","DOI":"10.1016\/S0021-9258(19)83913-3","article-title":"Biochemical responses in activated human neutrophils mediated by protein kinase C and a Ca2\u00b1requiring proteinase","volume":"261","author":"Pontremoli","year":"1986","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB28","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1016\/0006-291X(84)91470-0","article-title":"Platelet Ca2\u00b1activated, phospholipid-dependent protein kinase: evidence for proteolytic activation of the enzyme in cells treated with phospholipase C1","volume":"118","author":"Tapley","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB29","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/0167-4889(95)00127-3","article-title":"Antibodies specific for proteolyzed forms of protein kinase C alpha","volume":"1269","author":"Kikuchi","year":"1995","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB30","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1046\/j.1471-4159.1996.66041539.x","article-title":"Calcium influx into human neuroblastoma cells induces ALZ-50 immunoreactivity: involvement of calpain-mediated hydrolysis of protein kinase C","volume":"66","author":"Shea","year":"1996","journal-title":"J. Neurochem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB31","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/S0008-6363(97)00099-0","article-title":"MDL-28170, a membrane-permeant calpain inhibitor, attenuates stunning and PKC epsilon proteolysis in reperfused ferret hearts","volume":"35","author":"Urthaler","year":"1997","journal-title":"Cardiovasc. Res."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB32","doi-asserted-by":"crossref","first-page":"2556","DOI":"10.1046\/j.1471-4159.1999.0722556.x","article-title":"Translocation and down-regulation of protein kinase C-alpha, -beta, and -gamma isoforms during ischemia-reperfusion in rat brain","volume":"72","author":"Harada","year":"1999","journal-title":"J. Neurochem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB33","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/0065-2571(70)90017-8","article-title":"A cyclic 3\u2032,5\u2032-AMP-stimulated protein kinase from cardiac muscle","volume":"8","author":"Brostrom","year":"1970","journal-title":"Advan. Enzyme Regul."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB34","doi-asserted-by":"crossref","first-page":"7592","DOI":"10.1523\/JNEUROSCI.15-11-07592.1995","article-title":"Persistent activation of cAMP-dependent protein kinase by regulated proteolysis suggests a neuron-specific function of the ubiquitin system in Aplysia","volume":"15","author":"Chain","year":"1995","journal-title":"J. Neurosci."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB35","doi-asserted-by":"crossref","first-page":"1441","DOI":"10.1016\/S0021-9258(17)40676-4","article-title":"Concentrations of cyclic AMP-dependent protein kinase subunits in various tissues","volume":"252","author":"Hofmann","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB36","doi-asserted-by":"crossref","first-page":"113","DOI":"10.3109\/10799899809047740","article-title":"PEST sequences in proteins involved in cyclic nucleotide signalling pathways","volume":"18","author":"Sekhar","year":"1998","journal-title":"J. Recept. Signal Transduct. Res."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB37","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1016\/S0896-6273(00)80686-8","article-title":"Mechanisms for generating the autonomous cAMP-dependent protein kinase required for long-term facilitation in Aplysia","volume":"22","author":"Chain","year":"1999","journal-title":"Neuron"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB38","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/S0896-6273(00)80747-3","article-title":"Making new connections: role of ERK\/MAP kinase signaling in neuronal plasticity","volume":"23","author":"Impey","year":"1999","journal-title":"Neuron."},{"issue":"150","key":"10.1016\/S0065-2571(99)00030-8_BIB39","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/BF01076559","article-title":"PEST sequences in calmodulin-binding proteins","volume":"149","author":"Barnes","year":"1995","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB40","doi-asserted-by":"crossref","first-page":"5380","DOI":"10.1021\/bi00439a010","article-title":"Autophosphorylation of the type II calmodulin-dependent protein kinase is essential for formation of a proteolytic fragment with catalytic activity. Implications for long-term synaptic potentiation","volume":"28","author":"Kwiatkowski","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB41","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/342505a0","article-title":"Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs [see comments]","volume":"342","author":"Watanabe","year":"1989","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB42","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1042\/bj3100657","article-title":"Purification and characterization of a fatty acid-activated protein kinase (PKN) from rat testis","volume":"310","author":"Kitagawa","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB43","doi-asserted-by":"crossref","first-page":"15538","DOI":"10.1016\/S0021-9258(18)47759-9","article-title":"Autophosphorylation of the protein kinase dependent on double-stranded RNA","volume":"262","author":"Galabru","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB44","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1042\/bj3090315","article-title":"Expression, purification and characterization of the ubiquitous protein kinase C-related kinase 1","volume":"309","author":"Palmer","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB45","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0014-5793(89)80430-2","article-title":"Activation of an insulin-stimulated S6 kinase in 3T3 L1 cell-free extracts by proteolysis","volume":"248","year":"1989","journal-title":"FEBS Lett."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB46","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1074\/jbc.273.3.1357","article-title":"Autoinhibition of casein kinase I epsilon (CKI epsilon) is relieved by protein phosphatases and limited proteolysis","volume":"273","author":"Cegielska","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB47","first-page":"65","article-title":"Protein phosphatases are pest containing proteins","volume":"41","author":"Gomes","year":"1997","journal-title":"Biochem. Mol. Biol. Int."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB48","doi-asserted-by":"crossref","first-page":"13251","DOI":"10.1016\/S0021-9258(18)98831-9","article-title":"Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit","volume":"266","author":"Kamibayashi","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB49","doi-asserted-by":"crossref","first-page":"13119","DOI":"10.1074\/jbc.273.21.13119","article-title":"Regulation of protein phosphatase 2A activity by caspase-3 during apoptosis","volume":"273","author":"Santoro","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB50","doi-asserted-by":"crossref","first-page":"2205","DOI":"10.1021\/bi00406a059","article-title":"Activation of a calmodulin-dependent phosphatase by a Ca2\u00b1dependent protease","volume":"27","author":"Tallant","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB51","doi-asserted-by":"crossref","first-page":"32731","DOI":"10.1074\/jbc.272.52.32731","article-title":"Phosphorylation of human CDC25B phosphatase by CDK1-cyclin A triggers its proteasome-dependent degradation","volume":"272","author":"Baldin","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB52","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/S0014-5793(96)01427-5","article-title":"Activation of protein phosphatase 5 by limited proteolysis or the binding of polyunsaturated fatty acids to the TPR domain","volume":"400","author":"Chen","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB53","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1083\/jcb.138.3.681","article-title":"Cellular redistribution of protein tyrosine phosphatases LAR and PTPsigma by inducible proteolytic processing","volume":"138","author":"Aicher","year":"1997","journal-title":"J. Cell Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB54","doi-asserted-by":"crossref","first-page":"20589","DOI":"10.1074\/jbc.273.32.20589","article-title":"Tyrosine phosphorylation and proteolysis. Pervanadate-induced, metalloprotease-dependent cleavage of the ErbB-4 receptor and amphiregulin","volume":"273","author":"Vecchi","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB55","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1111\/j.1432-1033.1994.tb19013.x","article-title":"The calpain cleavage sites in the epidermal growth factor receptor kinase domain","volume":"223","author":"Gregoriou","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB56","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1042\/bj3180041","article-title":"Focal adhesion kinase (pp125FAK) cleavage and regulation by calpain","volume":"318","author":"Cooray","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB57","doi-asserted-by":"crossref","first-page":"21847","DOI":"10.1074\/jbc.272.35.21847","article-title":"Calpain regulation of cytoskeletal signaling complexes in von Willebrand factor-stimulated platelets. Distinct roles for glycoprotein Ib-V-IX and glycoprotein IIb-IIIa (integrin alphaIIbbeta3) in von Willebrand factor-induced signal transduction","volume":"272","author":"Yuan","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB58","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1111\/j.1432-1033.1996.0400h.x","article-title":"The spleen protein-tyrosine kinase TPK-IIB is highly similar to the catalytic domain of p72syk","volume":"240","author":"Brunati","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB59","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1972.33","article-title":"Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics","volume":"26","author":"Kerr","year":"1972","journal-title":"Brit. J. Cancer."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB60","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S0074-7696(08)62312-8","article-title":"Cell death: the significance of apoptosis","volume":"68","author":"Wyllie","year":"1980","journal-title":"Int. Rev. Cytol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB61","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1126\/science.7878464","article-title":"Apoptosis in the pathogenesis and treatment of human disease","volume":"267","author":"Thompson","year":"1995","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB62","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0092-8674(00)81873-5","article-title":"Programmed cell death in animal development","volume":"88","author":"Jacobson","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB63","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1126\/science.281.5381.1317","article-title":"A matter of life and cell death","volume":"281","author":"Evan","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB64","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1126\/science.281.5381.1305","article-title":"Death receptors: signaling and modulation","volume":"281","author":"Ashkenazi","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB65","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1038\/sj.onc.1202183","article-title":"Anti-apoptotic vs pro-apoptotic signal transduction: Checkpoints and stop signs along the road to death","volume":"17","author":"Jarbe","year":"1998","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB66","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1101\/SQB.1994.059.01.042","article-title":"The genetics of programmed cell death in the nematode Caenorhabditis elegans","volume":"59","author":"Horvitz","year":"1994","journal-title":"Cold Spring Harbor Symp. Quant. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB67","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/385653a0","article-title":"Interaction between the C. elegans cell-death regulators CED-9 and CED-4","volume":"385","author":"Spector","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB68","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1126\/science.275.5303.1122","article-title":"Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death","volume":"275","author":"Chinnaiyan","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB69","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1126\/science.275.5303.1126","article-title":"Interaction and regulation of subcellular localization of CED-4 by CED-9","volume":"275","author":"Wu","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB70","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/S0960-9822(06)00120-5","article-title":"CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9","volume":"7","author":"James","year":"1997","journal-title":"Curr. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB71","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/0092-8674(94)90506-1","article-title":"C. elegans cell survival gene ced-9 encodes a functional homolog of the mammalian proto-oncogene bcl-2","volume":"76","author":"Hangartner","year":"1994","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB72","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1126\/science.281.5381.1322","article-title":"The Bcl-2 protein family: arbiters of cell survival","volume":"281","author":"Adams","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB73","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/S0092-8674(00)80501-2","article-title":"Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3","volume":"90","author":"Zou","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB74","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/S0092-8674(00)80434-1","article-title":"Cytochrome c and dATP-dependent formation of Apaf-1\/caspase-9 complex initiates an apoptotic protease cascade","volume":"91","author":"Li","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB75","doi-asserted-by":"crossref","first-page":"4386","DOI":"10.1073\/pnas.95.8.4386","article-title":"Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation","volume":"95","author":"Hu","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB76","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/S1097-2765(00)80095-7","article-title":"Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization","volume":"1","author":"Srinivasula","year":"1998","journal-title":"Mol. Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB77","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1101\/gad.10.9.1073","article-title":"The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease","volume":"10","author":"Xue","year":"1996","journal-title":"Genes Dev."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB78","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(00)81334-3","article-title":"Human ICE\/CED-3 protease nomenclature","volume":"87","author":"Alnemri","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB79","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/S1074-7613(00)80428-8","article-title":"ICE family proteases: Mediators of all apoptotic cell death?","volume":"4","author":"Henkart","year":"1996","journal-title":"Immunity"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB80","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1126\/science.281.5381.1312","article-title":"Caspases: enemies within","volume":"281","author":"Thornberry","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB81","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/375078a0","article-title":"Involvement of an ICE-like protease in Fas-mediated apoptosis","volume":"375","author":"Enari","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB82","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1038\/380723a0","article-title":"Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis","volume":"380","author":"Enari","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB83","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/375081a0","article-title":"Requirement of an ICE\/CED-3 protease for Fas\/APO-1-mediated apoptosis","volume":"375","author":"Los","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB84","doi-asserted-by":"crossref","first-page":"22705","DOI":"10.1074\/jbc.270.39.22705","article-title":"CrmA, a poxvirus-encoded serpin, inhibits cytotoxic T-lymphocyte-mediated apoptosis","volume":"270","author":"Tewari","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB85","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":"10.1016\/S0065-2571(99)00030-8_BIB86","doi-asserted-by":"crossref","first-page":"7795","DOI":"10.1074\/jbc.270.14.7795","article-title":"A novel protein that interacts with the death domain of Fas\/APO1 contains a sequence motif related to the death domain","volume":"270","author":"Boldin","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB87","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S0092-8674(00)81266-0","article-title":"FLICE, a novel FADD-homologous ICE\/CED-3-like protease, is recruited to the CD95 (Fas\/APO-1) death\u2013inducing signaling complex","volume":"85","author":"Muzio","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB88","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0092-8674(00)81265-9","article-title":"Involvement of MACH, a novel MORT1\/FADD-interacting protease, in Fas\/APO-1- and TNF receptor-induced cell death","volume":"85","author":"Boldin","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB89","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1126\/science.281.5381.1355","article-title":"Essential role of CED-4 oligomerization in CED-3 activation and apoptosis","volume":"281","author":"Yang","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB90","doi-asserted-by":"crossref","first-page":"1309","DOI":"10.1126\/science.281.5381.1309","article-title":"Mitochondria and apoptosis","volume":"281","author":"Green","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB91","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/371346a0","article-title":"Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE","volume":"371","author":"Lazebnik","year":"1994","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB92","doi-asserted-by":"crossref","first-page":"1185","DOI":"10.1006\/bbrc.1995.2894","article-title":"Identification of actin as a substrate of ICE and an ICE-like protease and involvement of an ICE-like protease but not ICE in VP-16-induced U937 apoptosis","volume":"217","author":"Mashima","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB93","doi-asserted-by":"crossref","first-page":"31277","DOI":"10.1074\/jbc.271.49.31277","article-title":"Specific cleavage of alpha-fodrin during Fas- and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1beta-converting enzyme\/Ced-3 protease distinct from the poly(ADP-ribose) polymerase protease","volume":"271","author":"Cryns","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB94","doi-asserted-by":"crossref","first-page":"16443","DOI":"10.1074\/jbc.271.28.16443","article-title":"The CED-3\/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A","volume":"271","author":"Orth","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB95","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1126\/science.278.5336.294","article-title":"Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis","volume":"278","author":"Kothakota","year":"1997","journal-title":"Science."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB96","doi-asserted-by":"crossref","first-page":"29419","DOI":"10.1074\/jbc.272.47.29419","article-title":"Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro","volume":"272","author":"Barkett","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB97","doi-asserted-by":"crossref","first-page":"11209","DOI":"10.1074\/jbc.271.19.11209","article-title":"D4-GDI, a substrate of CPP32, is proteolyzed during Fas-induced apoptosis","volume":"271","author":"Na","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB98","doi-asserted-by":"crossref","first-page":"1625","DOI":"10.1084\/jem.182.6.1625","article-title":"DNA-dependent protein kinase is one of a subset of autoantigens specifically cleaved early during apoptosis","volume":"182","author":"Casciola Rosen","year":"1995","journal-title":"J. Exp. Med."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB99","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1182\/blood.V87.5.1990.1990","article-title":"Activation of protein kinase Cdelta in human myeloid leukemia cells treated with 1-beta-D-arabinofuranosylcytosine","volume":"87","author":"Emoto","year":"1996","journal-title":"Blood"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB100","doi-asserted-by":"crossref","first-page":"20317","DOI":"10.1074\/jbc.272.33.20317","article-title":"Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis","volume":"272","author":"Datta","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB101","doi-asserted-by":"crossref","first-page":"10765","DOI":"10.1074\/jbc.274.16.10765","article-title":"Cleavage of zetaPKC but not lambda\/iotaPKC by caspase-3 during UV-induced apoptosis","volume":"274","author":"Frutos","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB102","doi-asserted-by":"crossref","first-page":"29449","DOI":"10.1074\/jbc.272.47.29449","article-title":"Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy","volume":"272","author":"Cryns","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB103","doi-asserted-by":"crossref","first-page":"11566","DOI":"10.1073\/pnas.95.20.11566","article-title":"Proteolytic activation of PKN by caspase-3 or related protease during apoptosis","volume":"95","author":"Takahashi","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB104","doi-asserted-by":"crossref","first-page":"1571","DOI":"10.1126\/science.276.5318.1571","article-title":"Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2","volume":"276","author":"Rudel","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB105","doi-asserted-by":"crossref","first-page":"28733","DOI":"10.1074\/jbc.273.44.28733","article-title":"Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity","volume":"273","author":"Walter","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB106","doi-asserted-by":"crossref","first-page":"2224","DOI":"10.1093\/emboj\/17.8.2224","article-title":"Caspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1","volume":"17","author":"Graves","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB107","doi-asserted-by":"crossref","first-page":"3029","DOI":"10.1038\/sj.onc.1201840","article-title":"Proteolytic activation of MST\/Krs, STE20-related protein kinase, by caspase during apoptosis","volume":"16","author":"Lee","year":"1998","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB108","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/S0092-8674(00)80339-6","article-title":"The regulation of anoikis: MEKK-1 activation requires cleavage by caspases","volume":"90","author":"Cardone","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB109","doi-asserted-by":"crossref","first-page":"11694","DOI":"10.1074\/jbc.272.18.11694","article-title":"Cleavage of PITSLRE kinases by ICE\/CASP-1 and CPP32\/CASP-3 during apoptosis induced by tumor necrosis factor","volume":"272","author":"Beyaert","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB110","first-page":"2689","article-title":"Targeted proteolysis of the focal adhesion kinase pp125 FAK during c-MYC-induced apoptosis is suppressed by integrin signalling","volume":"12","author":"Crouch","year":"1996","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB111","doi-asserted-by":"crossref","first-page":"26056","DOI":"10.1074\/jbc.272.41.26056","article-title":"Cleavage of focal adhesion kinase by caspases during apoptosis","volume":"272","author":"Wen","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB112","doi-asserted-by":"crossref","first-page":"17102","DOI":"10.1074\/jbc.273.27.17102","article-title":"Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide","volume":"273","author":"Gervais","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB113","doi-asserted-by":"crossref","first-page":"7141","DOI":"10.1074\/jbc.273.12.7141","article-title":"Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals","volume":"273","author":"Widmann","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB114","doi-asserted-by":"crossref","first-page":"19993","DOI":"10.1074\/jbc.273.32.19993","article-title":"Calcium\/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis","volume":"273","author":"McGinnis","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB115","doi-asserted-by":"crossref","first-page":"19207","DOI":"10.1074\/jbc.273.30.19207","article-title":"Cleavage of CDK inhibitor p21(Cip1\/Waf1) by caspases is an early event during DNA damage-induced apoptosis","volume":"273","author":"Gervais","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB116","doi-asserted-by":"crossref","first-page":"3324","DOI":"10.1038\/sj.onc.1202668","article-title":"Evidence for a p23 caspase-cleaved form of p27[KIP1] involved in G1 growth arrest","volume":"18","author":"Loubat","year":"1999","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB117","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1126\/science.7701324","article-title":"Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor","volume":"267","author":"Yao","year":"1995","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB118","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1101\/gad.11.6.701","article-title":"The PI 3-kinase\/Akt signaling pathway delivers an anti-apoptotic signal","volume":"11","author":"Kennedy","year":"1997","journal-title":"Genes Dev."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB119","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1038\/36442","article-title":"Apoptosis. A BAD kinase makes good","volume":"390","author":"Franke","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB120","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0092-8674(00)80405-5","article-title":"Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery","volume":"91","author":"Datta","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB121","doi-asserted-by":"crossref","first-page":"1318","DOI":"10.1126\/science.282.5392.1318","article-title":"Regulation of cell death protease caspase-9 by phosphorylation","volume":"282","author":"Cardone","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB122","doi-asserted-by":"crossref","first-page":"20664","DOI":"10.1074\/jbc.274.29.20664","article-title":"Apoptosis promotes a caspase-induced amino-terminal truncation of IkappaBalpha that functions as a stable inhibitor of NF-kappaB","volume":"274","author":"Reuther","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB123","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1146\/annurev.physiol.60.1.533","article-title":"Proteolytic activities that mediate apoptosis","volume":"60","author":"Kidd","year":"1998","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB124","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/MCB.15.1.1","article-title":"PITSLRE protein kinase activity is associated with apoptosis","volume":"15","author":"Lahti","year":"1995","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB125","doi-asserted-by":"crossref","first-page":"16601","DOI":"10.1074\/jbc.273.26.16601","article-title":"Phosphorylation of PITSLRE p110 isoforms accompanies their processing by caspases during Fas-mediated cell death","volume":"273","author":"Tang","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB126","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1126\/science.270.5240.1326","article-title":"Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis","volume":"270","author":"Xia","year":"1995","journal-title":"Science"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB127","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1002\/bies.950180708","article-title":"Protein kinase cascades activated by stress and inflammatory cytokines","volume":"18","author":"Kyriakis","year":"1996","journal-title":"Bioessays"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB128","first-page":"2087","article-title":"CD95 (APO-1\/Fas) induces activation of SAP kinases downstream of ICE-like proteases","volume":"13","author":"Cahill","year":"1996","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB129","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1128\/MCB.17.1.24","article-title":"Fas activation of the p38 mitogen-activated protein kinase signalling pathway requires ICE\/CED-3 family proteases","volume":"17","author":"Juo","year":"1997","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB130","doi-asserted-by":"crossref","first-page":"13814","DOI":"10.1073\/pnas.93.24.13814","article-title":"Involvement of stress-activated protein kinase and p38 mitogen-activated protein kinase in mIgM-induced apoptosis of human B lymphocytes","volume":"93","author":"Graves","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB131","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/S0962-8924(97)01003-9","article-title":"Emerging from the PAK: The p21-activated protein kinase family","volume":"7","author":"Sells","year":"1997","journal-title":"Trends Cell Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB132","doi-asserted-by":"crossref","first-page":"750","DOI":"10.1038\/377750a0","article-title":"Activation of the SAPK pathway by the human STE20 homologue germinal centre kinase","volume":"377","author":"Pombo","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB133","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1093\/emboj\/16.6.1279","article-title":"NIK is a new Ste20-related kinase that binds NCK and MEKK1 and activates the SAPK\/JNK cascade via a conserved regulatory domain","volume":"16","author":"Su","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB134","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1038\/sj.onc.1200877","article-title":"A novel human SPS1\/STE20 homologue, KHS, activates Jun N-terminal kinase","volume":"14","author":"Tung","year":"1997","journal-title":"Oncogene"},{"key":"10.1016\/S0065-2571(99)00030-8_BIB135","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/S0959-437X(97)80111-6","article-title":"MEKKs, GCKs, MLKs, PAKs, TAKs, and tpls: upstream regulators of the c-Jun amino-terminal kinases?","volume":"7","author":"Fanger","year":"1997","journal-title":"Curr. Opin. Genet. Dev."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB136","doi-asserted-by":"crossref","first-page":"7026","DOI":"10.1002\/j.1460-2075.1996.tb01094.x","article-title":"MLK-3 activates the SAPK\/JNK and p38\/RK pathways via SEK1 and MKK3\/6","volume":"15","author":"Tibbles","year":"1996","journal-title":"EMBO J."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB137","doi-asserted-by":"crossref","first-page":"15167","DOI":"10.1074\/jbc.272.24.15167","article-title":"MST\/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase\/stress-activated protein kinase","volume":"272","author":"Hirai","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB138","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1128\/MCB.18.4.2416","article-title":"MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis","volume":"18","author":"Widmann","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB139","doi-asserted-by":"crossref","first-page":"7","DOI":"10.4049\/jimmunol.160.1.7","article-title":"p21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells","volume":"160","author":"Rudel","year":"1998","journal-title":"J. Immunol."},{"key":"10.1016\/S0065-2571(99)00030-8_BIB140","doi-asserted-by":"crossref","first-page":"10916","DOI":"10.1074\/jbc.274.16.10916","article-title":"Differential involvement of MEK kinase 1 (MEKK1) in the induction of apoptosis in response to microtubule-targeted drugs vs DNA damaging agents","volume":"274","author":"Gibson","year":"1999","journal-title":"J. Biol. Chem."}],"container-title":["Advances in Enzyme Regulation"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0065257199000308?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0065257199000308?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,17]],"date-time":"2023-04-17T04:24:47Z","timestamp":1681705487000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0065257199000308"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,6]]},"references-count":140,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2000,6]]}},"alternative-id":["S0065257199000308"],"URL":"https:\/\/doi.org\/10.1016\/s0065-2571(99)00030-8","relation":{},"ISSN":["0065-2571"],"issn-type":[{"value":"0065-2571","type":"print"}],"subject":[],"published":{"date-parts":[[2000,6]]}}}