{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T15:24:44Z","timestamp":1771082684428,"version":"3.50.1"},"reference-count":84,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2001,4,1]],"date-time":"2001-04-01T00:00:00Z","timestamp":986083200000},"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":["Current Opinion in Cell Biology"],"published-print":{"date-parts":[[2001,4]]},"DOI":"10.1016\/s0955-0674(00)00189-7","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T19:58:13Z","timestamp":1027627093000},"page":"131-138","source":"Crossref","is-referenced-by-count":291,"title":["Phosphoserine\/threonine-binding domains"],"prefix":"10.1016","volume":"13","author":[{"given":"Michael B","family":"Yaffe","sequence":"first","affiliation":[]},{"given":"Andrew E.H","family":"Elia","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0955-0674(00)00189-7_BIB1","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1016\/S0092-8674(00)81067-3","article-title":"Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine","volume":"84","author":"Muslin","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB2","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1016\/S0092-8674(00)80487-0","article-title":"The structural basis for 14-3-3:phosphopeptide binding specificity","volume":"91","author":"Yaffe","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB3","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1146\/annurev.pharmtox.40.1.617","article-title":"14-3-3 proteins: structure, function and regulation","volume":"40","author":"Fu","year":"2000","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB4","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/S1360-1385(99)01462-4","article-title":"The 14-3-3 proteins: cellular regulators of plant metabolism","volume":"4","author":"Chung","year":"1999","journal-title":"Trends Plant Sci"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB5","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.8036497","article-title":"14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast","volume":"265","author":"Ford","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB6","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1126\/science.277.5331.1497","article-title":"Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25","volume":"277","author":"Sanchez","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB7","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1126\/science.277.5331.1501","article-title":"Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216","volume":"277","author":"Peng","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB8","doi-asserted-by":"crossref","first-page":"7410","DOI":"10.1128\/MCB.19.11.7410","article-title":"DNA damage and replication checkpoints in fission yeast require nuclear exclusion of the Cdc25 phosphatase via 14-3-3 binding","volume":"19","author":"Zeng","year":"1999","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB9","doi-asserted-by":"crossref","first-page":"2174","DOI":"10.1093\/emboj\/18.8.2174","article-title":"Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated inhibition of Cdc25 nuclear import","volume":"18","author":"Yang","year":"1999","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB10","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1101\/gad.13.9.1067","article-title":"Binding of 14-3-3 proteins and nuclear export control the intracellular localization of the mitotic inducer Cdc25","volume":"13","author":"Kumagai","year":"1999","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB11","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1038\/16488","article-title":"Nuclear localization of cdc25 is regulated by DNA damage and a 14-3-3 protein","volume":"397","author":"Lopez-Girona","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB12","doi-asserted-by":"crossref","first-page":"4465","DOI":"10.1128\/MCB.19.6.4465","article-title":"Cytoplasmic localization of human cdc25C during interphase requires an intact 14-3-3 binding site","volume":"19","author":"Dalal","year":"1999","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB13","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1091\/mbc.9.2.345","article-title":"14-3-3 proteins act as negative regulators of the mitotic inducer Cdc25 in Xenopus egg extracts","volume":"9","author":"Kumagai","year":"1998","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB14","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S1097-2765(00)80002-7","article-title":"14-3-3\u03c3 is a p53-regulated inhibitor of G2\/M progression","volume":"1","author":"Hermeking","year":"1997","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB15","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/44188","article-title":"14-3-3\u03c3 is required to prevent mitotic catastrophe after DNA damage","volume":"401","author":"Chan","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB16","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1073\/pnas.100566997","article-title":"High frequency of hypermethylation at the 14-3-3 sigma locus leads to gene silencing in breast cancer","volume":"97","author":"Ferguson","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB17","doi-asserted-by":"crossref","first-page":"3947","DOI":"10.1128\/MCB.18.7.3947","article-title":"14-3-3 facilitates Ras-dependent Raf-1 activation in vitro and in vivo","volume":"18","author":"Roy","year":"1998","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB18","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1038\/27938","article-title":"A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity","volume":"394","author":"Tzivion","year":"1998","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB19","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1042\/0264-6021:3450297","article-title":"14-3-3 isotypes facilitate coupling of protein kinase C-\u03b6 to Raf-1: negative regulation by 14-3-3 phosphorylation","volume":"345","author":"Van Der Hoeven","year":"2000","journal-title":"Biochem J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB20","first-page":"349","volume":"19","author":"Xing","year":"2000","journal-title":"14-3-3 proteins block apoptosis and differentially regulate MAPK cascades. EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB21","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S1097-2765(00)00006-X","article-title":"14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation","volume":"6","author":"Datta","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB22","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/S0092-8674(00)81382-3","article-title":"Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X","volume":"87","author":"Zha","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB23","doi-asserted-by":"crossref","first-page":"25046","DOI":"10.1074\/jbc.M002526200","article-title":"Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155","volume":"275","author":"Zhou","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB24","doi-asserted-by":"crossref","first-page":"25865","DOI":"10.1074\/jbc.M004199200","article-title":"BAD Ser155 phosphorylation regulates BAD\/Bcl-XL interaction and cell survival","volume":"275","author":"Tan","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB25","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1042\/0264-6021:3490547","article-title":"Regulation of BAD by cAMP dependent protein kinase is mediated via phosphorylation of a novel site, Ser155","volume":"349","author":"Lizcano","year":"2000","journal-title":"Biochem J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB26","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\/S0955-0674(00)00189-7_BIB27","doi-asserted-by":"crossref","first-page":"8511","DOI":"10.1073\/pnas.96.15.8511","article-title":"Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins","volume":"96","author":"Zhang","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB28","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1016\/S0092-8674(00)80595-4","article-title":"Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor","volume":"96","author":"Brunet","year":"1999","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB29","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1038\/45287","article-title":"The TOR signalling pathway controls nuclear localization of nutrient-regulated transcription factors","volume":"402","author":"Beck","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB30","doi-asserted-by":"crossref","first-page":"6778","DOI":"10.1093\/emboj\/19.24.6778","article-title":"TAZ; a novel transcriptional co-activator regulated by interactions with 14-3-3 and PDZ-domain proteins","volume":"19","author":"Kanai","year":"2000","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB31","doi-asserted-by":"crossref","first-page":"25356","DOI":"10.1074\/jbc.273.39.25356","article-title":"Association of the TLX-2 homeodomain and 14-3-3\u03b7 signaling proteins","volume":"273","author":"Tang","year":"1998","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB32","doi-asserted-by":"crossref","first-page":"13085","DOI":"10.1021\/bi9912490","article-title":"Purification and properties of the Xenopus Hat1 acetyltransferase: association with the 14-3-3 proteins in the oocyte nucleus","volume":"38","author":"Imhof","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB33","doi-asserted-by":"crossref","first-page":"7835","DOI":"10.1073\/pnas.140199597","article-title":"Regulation of histone deacetylase 4 and 5 and transcriptional activity by 14-3-3-dependent cellular localization","volume":"97","author":"Grozinger","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB34","doi-asserted-by":"crossref","first-page":"6904","DOI":"10.1128\/MCB.20.18.6904-6912.2000","article-title":"Regulation of histone deacetylase 4 by binding of 14-3-3 proteins","volume":"20","author":"Wang","year":"2000","journal-title":"Mol Cell Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB35","doi-asserted-by":"crossref","first-page":"13948","DOI":"10.1074\/jbc.275.18.13948","article-title":"Modulation of human DNA topoisomerase IIalpha function by interaction with 14-3-3epsilon","volume":"275","author":"Kurz","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB36","first-page":"2652","volume":"19","author":"Seimiya","year":"2000","journal-title":"Involvement of 14-3-3 proteins in nuclear localization of telomerase. EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB37","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1126\/science.283.5406.1325","article-title":"Function of WW domains as phosphoserine- or phosphothreonine-binding modules","volume":"283","author":"Lu","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB38","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/S1097-2765(05)00083-3","article-title":"Pin1-dependent prolyl isomerization regulates dephosphorylation of Cdc25C and Tau proteins","volume":"6","author":"Zhou","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB39","doi-asserted-by":"crossref","first-page":"31583","DOI":"10.1074\/jbc.274.44.31583","article-title":"Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3\u2032-End formation","volume":"274","author":"Morris","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB40","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1038\/77929","article-title":"Structural basis for phosphoserine-proline recognition by group IV WW domains","volume":"7","author":"Verdecia","year":"2000","journal-title":"Nat Struct Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB41","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/S0968-0004(00)89072-6","article-title":"The FHA domain: a putative nuclear signalling domain found in protein kinases and transcription factors","volume":"20","author":"Hofmann","year":"1995","journal-title":"Trends Biochem Sci"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB42","doi-asserted-by":"crossref","first-page":"7821","DOI":"10.1073\/pnas.96.14.7821","article-title":"Kinase interaction domain of kinase-associated protein phosphatase, a phosphoprotein-binding domain","volume":"96","author":"Li","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB43","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1006\/jmbi.1999.3313","article-title":"Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53","volume":"294","author":"Liao","year":"1999","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB44","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0014-5793(00)01392-2","article-title":"FHA domain boundaries of the dun1p and rad53p cell cycle checkpoint kinases","volume":"471","author":"Hammet","year":"2000","journal-title":"FEBS Lett"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB45","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1006\/jmbi.2000.4095","article-title":"II. Structure and specificity of the interaction between the FHA2 domain of rad53 and phosphotyrosyl peptides","volume":"302","author":"Wang","year":"2000","journal-title":"J Mol Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB46","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/S1097-2765(00)00114-3","article-title":"The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phosphodependent signaling mechanisms","volume":"6","author":"Durocher","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB47","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1126\/science.7973632","article-title":"Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase","volume":"266","author":"Stone","year":"1994","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB48","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1126\/science.281.5374.272","article-title":"Rad53 FHA domain associated with phosphorylated Rad9 in the DNA damage checkpoint","volume":"281","author":"Sun","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB49","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S1097-2765(00)80340-8","article-title":"The FHA domain is a modular phosphopeptide recognition motif","volume":"4","author":"Durocher","year":"1999","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB50","doi-asserted-by":"crossref","first-page":"2528","DOI":"10.1126\/science.286.5449.2528","article-title":"Heterozygous germ line hCHK2 mutations in Li-Fraumeni syndrome","volume":"286","author":"Bell","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB51","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/35019108","article-title":"Chfr defines a mitotic stress checkpoint that delays entry into metaphase","volume":"406","author":"Scolnick","year":"2000","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB52","doi-asserted-by":"crossref","first-page":"28888","DOI":"10.1074\/jbc.M003879200","article-title":"The forkhead-associated domain of Ki-67 antigen interacts with the novel kinesin-like protein Hklp2","volume":"275","author":"Sueishi","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB53","doi-asserted-by":"crossref","first-page":"25411","DOI":"10.1074\/jbc.M001676200","article-title":"NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry","volume":"275","author":"Boudrez","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB54","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1101\/gad.14.13.1605","article-title":"A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-\u03b2 signal transduction","volume":"14","author":"Kim","year":"2000","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB55","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.cellbio.15.1.435","article-title":"SCF and Cullin\/Ring H2-based ubiquitin ligases","volume":"15","author":"Deshaies","year":"1999","journal-title":"Annu Rev Cell Dev Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB56","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/S0092-8674(00)80753-9","article-title":"How the cyclin became a cyclin: regulated proteolysis in the cell cycle","volume":"97","author":"Koepp","year":"1999","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB57","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1093\/emboj\/19.9.2069","article-title":"Targeted disruption of Skp2 results in accumulation of cyclin E and p27(Kip1), polyploidy and centrosome overduplication","volume":"19","author":"Nakayama","year":"2000","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB58","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/S0092-8674(00)80404-3","article-title":"A complex of Cdc4p, Skp1p, and Cdc53p\/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p","volume":"91","author":"Feldman","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB59","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/S0092-8674(00)80403-1","article-title":"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex","volume":"91","author":"Skowyra","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB60","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/25159","article-title":"Identification of the receptor component of the I\u03baB\u03b1-ubiquitin ligase","volume":"396","author":"Yaron","year":"1998","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB61","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1101\/gad.13.3.284","article-title":"Signal-induced ubiquitination of I\u03baB\u03b1 by the F-box protein Slimb\/\u03b2-TrCP","volume":"13","author":"Spencer","year":"1999","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB62","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1038\/sj.onc.1202760","article-title":"HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of I\u03baB\u03b1 and beta-catenin","volume":"18","author":"Fuchs","year":"1999","journal-title":"Oncogene"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB63","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1016\/S1097-2765(00)80481-5","article-title":"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I\u03baB\u03b1","volume":"3","author":"Tan","year":"1999","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB64","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1093\/emboj\/19.11.2580","article-title":"SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-\u03baB p105 requires phosphorylation of its C-terminus by I\u03baB kinase","volume":"19","author":"Orian","year":"2000","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB65","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1016\/S0960-9822(99)80091-8","article-title":"The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell","volume":"9","author":"Hart","year":"1999","journal-title":"Curr Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB66","doi-asserted-by":"crossref","first-page":"6273","DOI":"10.1073\/pnas.96.11.6273","article-title":"\u03b2-Trcp couples beta-catenin phosphorylation-degradation and regulates Xenopus axis formation","volume":"96","author":"Liu","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB67","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/12013","article-title":"SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27","volume":"1","author":"Carrano","year":"1999","journal-title":"Nat Cell Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB68","doi-asserted-by":"crossref","first-page":"8159","DOI":"10.1073\/pnas.95.14.8159","article-title":"sud1(+) targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1 proteins for degradation and stops unwanted diploidization in fission yeast","volume":"95","author":"Jallepalli","year":"1998","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB69","doi-asserted-by":"crossref","first-page":"2767","DOI":"10.1101\/gad.11.21.2767","article-title":"Regulation of the replication initiator protein p65cdc18 by CDK phosphorylation","volume":"11","author":"Jallepalli","year":"1997","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB70","doi-asserted-by":"crossref","first-page":"2401","DOI":"10.1093\/emboj\/18.9.2401","article-title":"An F-box protein, FWD1, mediates ubiquitin-dependent proteolysis of \u03b2-catenin","volume":"18","author":"Kitagawa","year":"1999","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB71","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/S1097-2765(00)80056-8","article-title":"A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif","volume":"1","author":"Margottin","year":"1998","journal-title":"Mol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB72","doi-asserted-by":"crossref","first-page":"3655","DOI":"10.1242\/jcs.111.24.3655","article-title":"An essential function of Grr1 for the degradation of Cln2 is to act as a binding core that links Cln2 to Skp1","volume":"111","author":"Kishi","year":"1998","journal-title":"J Cell Sci"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB73","doi-asserted-by":"crossref","first-page":"6486","DOI":"10.1093\/emboj\/16.21.6486","article-title":"Inhibition of NF-\u03ba-B cellular function via specific targeting of the I-\u03ba-B-ubiquitin ligase","volume":"16","author":"Yaron","year":"1997","journal-title":"EMBO J"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB74","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1101\/gad.13.3.270","article-title":"The SCFbeta-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in I\u03baB\u03b1 and \u03b2-catenin and stimulates I\u03baB\u03b1 ubiquitination in vitro","volume":"13","author":"Winston","year":"1999","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB75","doi-asserted-by":"crossref","first-page":"28169","DOI":"10.1074\/jbc.274.40.28169","article-title":"Common pathway for the ubiquitination of I\u03baB\u03b1, I\u03baB\u03b1, and I\u03baB\u03b1 mediated by the F-box protein FWD1","volume":"274","author":"Shirane","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB76","doi-asserted-by":"crossref","first-page":"29641","DOI":"10.1074\/jbc.274.42.29641","article-title":"Molecular dissection of the interactions among I\u03baB\u03b1, FWD1, and Skp1 required for ubiquitin-mediated proteolysis of I\u03baB\u03b1","volume":"274","author":"Hattori","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB77","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/S0960-9822(99)80290-5","article-title":"p27(Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27","volume":"9","author":"Tsvetkov","year":"1999","journal-title":"Curr Biol"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB78","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1126\/science.278.5337.455","article-title":"Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase","volume":"278","author":"Verma","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB79","doi-asserted-by":"crossref","first-page":"3263","DOI":"10.1091\/mbc.10.10.3263","article-title":"Phosphorylation controls timing of Cdc6p destruction: a biochemical analysis","volume":"10","author":"Elsasser","year":"1999","journal-title":"Mol Biol Cell"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB80","doi-asserted-by":"crossref","first-page":"1597","DOI":"10.1126\/science.271.5255.1597","article-title":"Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation","volume":"271","author":"Lanker","year":"1996","journal-title":"Science"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB81","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/374183a0","article-title":"A structural basis of the interactions between leucine-rich repeats and protein ligands","volume":"374","author":"Kobe","year":"1995","journal-title":"Nature"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB82","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1073\/pnas.97.3.1096","article-title":"Peptide-in-groove interactions link target proteins to the \u03b2-propeller of clathrin","volume":"97","author":"ter Haar","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB83","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1101\/gad.13.9.1181","article-title":"Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation","volume":"13","author":"Montagnoli","year":"1999","journal-title":"Genes Dev"},{"key":"10.1016\/S0955-0674(00)00189-7_BIB84","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1038\/35042620","article-title":"Insights into SCF ubiquitin ligase from the structure of the Skp1-Skp2 complex","volume":"408","author":"Schulman","year":"2000","journal-title":"Nature"}],"container-title":["Current Opinion in Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067400001897?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0955067400001897?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,12]],"date-time":"2023-04-12T22:42:45Z","timestamp":1681339365000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0955067400001897"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,4]]},"references-count":84,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2001,4]]}},"alternative-id":["S0955067400001897"],"URL":"https:\/\/doi.org\/10.1016\/s0955-0674(00)00189-7","relation":{},"ISSN":["0955-0674"],"issn-type":[{"value":"0955-0674","type":"print"}],"subject":[],"published":{"date-parts":[[2001,4]]}}}