{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,26]],"date-time":"2026-02-26T16:03:28Z","timestamp":1772121808245,"version":"3.50.1"},"reference-count":55,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2001,9,1]],"date-time":"2001-09-01T00:00:00Z","timestamp":999302400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,17]],"date-time":"2013-07-17T00:00:00Z","timestamp":1374019200000},"content-version":"vor","delay-in-days":4337,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cell"],"published-print":{"date-parts":[[2001,9]]},"DOI":"10.1016\/s0092-8674(01)00496-2","type":"journal-article","created":{"date-parts":[[2004,4,15]],"date-time":"2004-04-15T05:36:43Z","timestamp":1082007403000},"page":"745-757","source":"Crossref","is-referenced-by-count":274,"title":["Structural Basis for Autoinhibition of the EphB2 Receptor Tyrosine Kinase by the Unphosphorylated Juxtamembrane Region"],"prefix":"10.1016","volume":"106","author":[{"given":"Leanne E.","family":"Wybenga-Groot","sequence":"first","affiliation":[]},{"given":"Berivan","family":"Baskin","sequence":"additional","affiliation":[]},{"given":"Siew Hwa","family":"Ong","sequence":"additional","affiliation":[]},{"given":"Jiefei","family":"Tong","sequence":"additional","affiliation":[]},{"given":"Tony","family":"Pawson","sequence":"additional","affiliation":[]},{"given":"Frank","family":"Sicheri","sequence":"additional","affiliation":[]}],"member":"78","reference":[{"key":"10.1016\/S0092-8674(01)00496-2_BIB1","first-page":"30","article-title":"Methods used in the structure determination of bovine mitochondrial F1 ATPase","volume":"D52","author":"Abrahams","year":"1996","journal-title":"Acta Cryst."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB2","first-page":"1","article-title":"c-kit gain-of-function mutations and human tumors","volume":"89","author":"Andersson","year":"1998","journal-title":"Japn. J. of Cancer Res."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB3","doi-asserted-by":"crossref","first-page":"14843","DOI":"10.1021\/bi00045a027","article-title":"Characterization of pp60c-src tyrosine kinase activities using a continuous assay","volume":"34","author":"Barker","year":"1995","journal-title":"Biochem."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB4","doi-asserted-by":"crossref","first-page":"17050","DOI":"10.1074\/jbc.273.27.17050","article-title":"Full activation of the platelet-derived growth factor beta-receptor kinase involves multiple events","volume":"273","author":"Baxter","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB5","doi-asserted-by":"crossref","first-page":"4791","DOI":"10.1128\/MCB.20.13.4791-4805.2000","article-title":"Phosphorylation of tyrosine residues in the kinase domain and juxtamembrane region regulates the biological and catalytic activities of Eph receptors","volume":"20","author":"Binns","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB6","doi-asserted-by":"crossref","first-page":"1640","DOI":"10.1126\/science.275.5306.1640","article-title":"Tyrosine phosphorylation of transmembrane ligands for Eph receptors","volume":"275","author":"Bruckner","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB7","first-page":"905","article-title":"Crystallography and NMR system","volume":"D54","author":"Brunger","year":"1998","journal-title":"Acta Crystallogr."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB8","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1107\/S0021889891007240","article-title":"Ribbons 2.0","volume":"24","author":"Carson","year":"1991","journal-title":"J. Appl. Crystallgr."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB9","first-page":"760","article-title":"The CCP4 suite","volume":"D50","year":"1994","journal-title":"Acta Crystallogr."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB10","first-page":"2429","article-title":"Genomic organization and alternatively processed forms of Cek5, a receptor protein-tyrosine kinase of the Eph family","volume":"11","author":"Connor","year":"1995","journal-title":"Oncogene"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB11","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1016\/S0076-6879(97)76073-7","article-title":"Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods","volume":"276","author":"de La Fortelle","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB12","doi-asserted-by":"crossref","first-page":"5614","DOI":"10.1038\/sj.onc.1203856","article-title":"Eph receptors and ephrin ligands","volume":"19","author":"Dodelet","year":"2000","journal-title":"Oncogene"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB13","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/0092-8674(95)90425-5","article-title":"In vitro guidance of retinal ganglion cell exons by RAGS, a 25 kDa tectal protein related to ligands for Eph receptor tyrosine kinases","volume":"82","author":"Drescher","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB14","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0092-8674(00)80500-0","article-title":"Unified nomenclature for Eph family receptors and their ligands, the ephrins","volume":"90","year":"1997","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB15","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/S0896-6273(00)80276-7","article-title":"Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis","volume":"17","author":"Gale","year":"1996","journal-title":"Neuron"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB16","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1038\/sj.onc.1203354","article-title":"Tandem-duplicated Flt3 constitutively activates STAT5 and MAP kinase and introduces autonomous cell growth in IL-3-dependent cell lines","volume":"19","author":"Hayakawa","year":"2000","journal-title":"Oncogene"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB17","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/0092-8674(95)90404-2","article-title":"Dimerization of cell surface receptors in signal transduction","volume":"80","author":"Heldin","year":"1995","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB18","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1126\/science.279.5350.577","article-title":"Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors","volume":"279","author":"Hirota","year":"1998","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB19","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1242\/dev.126.10.2033","article-title":"Eph receptors and ephrins","volume":"126","author":"Holder","year":"1999","journal-title":"Development"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB20","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1038\/383722a0","article-title":"Bi-directional signalling through the Eph family receptor Nuk and its transmembrane ligands","volume":"383","author":"Holland","year":"1996","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB21","doi-asserted-by":"crossref","first-page":"3877","DOI":"10.1093\/emboj\/16.13.3877","article-title":"Juxtamembrane tyrosine residues couple the Eph family receptor Eph B2\/Nuk to specific SH2 domain proteins in neuronal cells","volume":"16","author":"Holland","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB22","doi-asserted-by":"crossref","first-page":"5572","DOI":"10.1093\/emboj\/16.18.5572","article-title":"Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog","volume":"16","author":"Hubbard","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB23","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1146\/annurev.biochem.69.1.373","article-title":"Protein tyrosine kinase structure and function","volume":"69","author":"Hubbard","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB24","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1038\/372746a0","article-title":"Crystal structure of the tyrosine kinase domain of the human insulin receptor","volume":"372","author":"Hubbard","year":"1994","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB25","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/S0092-8674(00)80555-3","article-title":"Crystal structure of the cytoplasmic domain of the type I TGF\u03b2 receptor in complex with FKBP12","volume":"96","author":"Huse","year":"1999","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB26","doi-asserted-by":"crossref","first-page":"6912","DOI":"10.1093\/emboj\/17.23.6912","article-title":"A single amino acid substitution in a WW-like domain of diverse members of the PDGF receptor subfamily of tyrosine kinases causes constitutive receptor activation","volume":"17","author":"Irusta","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB27","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0092-8674(00)81092-2","article-title":"Active and inactive protein kinases","volume":"85","author":"Johnson","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB28","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1107\/S0108767390010224","article-title":"Improved methods for binding protein models in electron density maps and the localization of errors in these models","volume":"A47","author":"Jones","year":"1991","journal-title":"Acta Cryst."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB29","doi-asserted-by":"crossref","first-page":"14396","DOI":"10.1021\/bi991628t","article-title":"Multiple in vivo tyrosine phosphorylation sites in EphB receptors","volume":"38","author":"Kalo","year":"1999","journal-title":"Biochem."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB30","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1182\/blood.V85.3.790.bloodjournal853790","article-title":"Constitutively activating mutations of c-kit receptor tyrosine kinase confer factor-independent growth and tumorigenicity of factor-dependent hematopoietic cell lines","volume":"85","author":"Kitayama","year":"1995","journal-title":"Blood"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB31","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1126\/science.1862342","article-title":"Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase","volume":"253","author":"Knighton","year":"1991","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB32","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1146\/annurev.biophys.26.1.259","article-title":"Modular peptide recognition domains in eukaryotic signaling","volume":"26","author":"Kuriyan","year":"1997","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB33","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1016\/S0092-8674(00)81817-6","article-title":"MADR2 is a substrate of the TGF\u03b2 receptor and its phosphorylation is required for nuclear accumulation and signaling","volume":"87","author":"Macias-Silva","year":"1996","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB34","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/21907","article-title":"Eph receptors and ephrins restrict cell intermingling and communication","volume":"400","author":"Mellitzer","year":"1999","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB35","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1107\/S0021889894000191","article-title":"SnB","volume":"27","author":"Miller","year":"1994","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB36","doi-asserted-by":"crossref","first-page":"4843","DOI":"10.1128\/MCB.14.7.4843","article-title":"Tyrosine 569 in the c-Fms juxtamembrane domain is essential for kinase activity and macrophage colony-stimulating factor-dependent internalization","volume":"14","author":"Myles","year":"1994","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB37","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.1016\/S0016-5085(98)70079-4","article-title":"A novel gain-of-function mutation of c-kit in gastrointestinal stromal tumors","volume":"115","author":"Nakahara","year":"1998","journal-title":"Gastroenterology"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB38","first-page":"1911","article-title":"Internal tandem duplication of the flt3 gene found in acute myeloid leukemia","volume":"10","author":"Nakao","year":"1996","journal-title":"Leukemia"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB39","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1107\/S0108767393007597","article-title":"AMoRe","volume":"A50","author":"Navaza","year":"1994","journal-title":"Acta Cryst."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB40","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/prot.340110407","article-title":"Protein folding and association","volume":"11","author":"Nicholls","year":"1991","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB41","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB42","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1126\/science.278.5346.2075","article-title":"Signaling through scaffold, anchoring, and adaptor proteins","volume":"278","author":"Pawson","year":"1997","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB43","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1126\/science.289.5486.1938","article-title":"Structural mechanism for STI-571 inhibition of abelson tyrosine kinase","volume":"289","author":"Schindler","year":"2000","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB44","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0092-8674(00)00114-8","article-title":"Cell signaling by receptor tyrosine kinases","volume":"103","author":"Schlessinger","year":"2000","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB45","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1016\/S0969-2126(00)00516-5","article-title":"Structure of the Tie2 RTK domain","volume":"8","author":"Shewchuk","year":"2000","journal-title":"Structure Fold. Des."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB46","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1038\/385602a0","article-title":"Crystal structure of the Src family tyrosine kinase Hck","volume":"385","author":"Sicheri","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB47","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1038\/4917","article-title":"The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization","volume":"6","author":"Stapleton","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB48","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1126\/science.283.5403.833","article-title":"Oligomeric structure of the human EphB2 receptor SAM domain","volume":"283","author":"Thanos","year":"1999","journal-title":"Science"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB49","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1182\/blood.V87.1.273.273","article-title":"Constitutive activation of c-kit in FMA3 murine mastocytoma cells caused by deletion of seven amino acids at the juxtamembrane domain","volume":"87","author":"Tsujimura","year":"1996","journal-title":"Blood"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB50","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1146\/annurev.cellbio.10.1.251","article-title":"Receptor protein-tyrosine kinases and their signal transduction pathways","volume":"10","author":"van der Geer","year":"1994","journal-title":"Annu. Rev. Cell Biol."},{"key":"10.1016\/S0092-8674(01)00496-2_BIB51","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/0092-8674(84)90386-6","article-title":"Mutagenesis of fujinami sarcoma virus","volume":"37","author":"Weinnmaster","year":"1984","journal-title":"Cell"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB52","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1038\/385595a0","article-title":"Three-dimensional structure of the tyrosine kinase c-Src","volume":"385","author":"Xu","year":"1997","journal-title":"Nature"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB53","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1038\/sj.leu.2400812","article-title":"Internal tandem duplication of the FLT3 gene is preferentially seen in acute myeloid leukemia and myelodysplastic syndrome among various hematological malignancies. A study on a large series of patients and cell lines","volume":"11","author":"Yokota","year":"1997","journal-title":"Leukemia"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB54","doi-asserted-by":"crossref","first-page":"2657","DOI":"10.1038\/sj.onc.1201823","article-title":"Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region","volume":"16","author":"Zisch","year":"1998","journal-title":"Oncogene"},{"key":"10.1016\/S0092-8674(01)00496-2_BIB55","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/sj.onc.1203304","article-title":"Replacing two conserved tyrosines of the EphB2 receptors with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses","volume":"19","author":"Zisch","year":"2000","journal-title":"Oncogene"}],"container-title":["Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867401004962?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0092867401004962?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,15]],"date-time":"2021-06-15T12:29:53Z","timestamp":1623760193000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0092867401004962"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,9]]},"references-count":55,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2001,9]]}},"alternative-id":["S0092867401004962"],"URL":"https:\/\/doi.org\/10.1016\/s0092-8674(01)00496-2","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.1004168.12505","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1004168.11906","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1004168.10252","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.1004168.13110","asserted-by":"object"}]},"ISSN":["0092-8674"],"issn-type":[{"value":"0092-8674","type":"print"}],"subject":[],"published":{"date-parts":[[2001,9]]}}}