{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,4]],"date-time":"2026-01-04T04:47:54Z","timestamp":1767502074262,"version":"3.48.0"},"reference-count":14,"publisher":"The Royal Society","issue":"1242","license":[{"start":{"date-parts":[[1985,10,22]],"date-time":"1985-10-22T00:00:00Z","timestamp":498787200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/royalsociety.org\/journals\/ethics-policies\/data-sharing-mining\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1985,10,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The human epidermal growth factor receptor has been purified and partial amino acid sequence obtained. A synthetic oligonucleotide was used to select complementary DNA clones from placental and A431 clone banks. The nucleotide sequence of a 5.8 kilobase transcript was determined and used to predict the total amino acid sequence of the receptor. We have predicted a model for the receptor which has an external ligand binding domain of 621 amino acids, a transmembrane region of 23 amino acids, and a cytoplasmic domain of 542 amino acids having protein tyrosine kinase activity. The kinase autophosphorylation sites have been mapped onto the primary amino acid sequence. Analysis of protein sequence databases have shown that the erb-B oncogene of avian erythroblastosis virus has acquired part of the avian EGF receptor gene. The hypothesis has been proposed that transformation by this virus is the result of expression of a truncated EGF receptor which lacks the majority of the EGF binding domain and delivers a continuous proliferation signal to transformed cells. We describe here the production of polyclonal and monoclonal antibodies to selected synthetic peptides from the EGF receptor and v-erb B sequences. Antisera to sequences encompassing the three major sites of autophosphorylation and the putative ATP binding site all recognize the native EGF receptor molecule. We have used these reagents to test our model of EGF receptor structure and v-erb B function.<\/jats:p>","DOI":"10.1098\/rspb.1985.0087","type":"journal-article","created":{"date-parts":[[2006,12,15]],"date-time":"2006-12-15T13:37:57Z","timestamp":1166189877000},"page":"127-134","source":"Crossref","is-referenced-by-count":24,"title":["The structure and function of the epidermal growth factor receptor studied by using antisynthetic peptide antibodies"],"prefix":"10.1098","volume":"226","author":[{"given":"W. J.","family":"Gullick","sequence":"first","affiliation":[{"name":"Protein Chemistry Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julian","family":"Downward","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P. J.","family":"Parker","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.","family":"Whittle","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.","family":"Kris","sequence":"additional","affiliation":[{"name":"Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.","family":"Schlessinger","sequence":"additional","affiliation":[{"name":"Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Ullrich","sequence":"additional","affiliation":[{"name":"Genentech Inc., 460 Point San Bruno Boulevard, South San Francisco, California 94080, U. S. A."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael Derek","family":"Waterfield","sequence":"additional","affiliation":[{"name":"Protein Chemistry Laboratory, Imperial Cancer Research Fund Laboratories, Lincoln's Inn Fields, London WC2A 3PX, U. K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"175","reference":[{"key":"p_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.48.070179.001205"},{"key":"p_2","doi-asserted-by":"publisher","DOI":"10.1038\/311483a0"},{"key":"p_3","doi-asserted-by":"publisher","DOI":"10.1038\/307521a0"},{"key":"p_4","unstructured":"Gullick W. J. Marsden J. J. & Waterfield M. D. 1985 a The production and use of antibodies to the epidermal growth factor receptor using natural and synthetic immunogens. Hormones Cell Regulation 9. (In the press.)"},{"key":"p_5","unstructured":"Gullick W. J. Marsden J. J. Whittle N. Ward B. Bobrow L. & Waterfield M. D. 19856 Expression of epidermal growth factors on cervical ovarian and vulval carcinomas. Cancer Res. (In the press.)"},{"key":"p_6","unstructured":"Guroff G. 1983 Growth and maturation factors. New York: Wiley."},{"key":"p_7","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.78.6.3824"},{"key":"p_8","doi-asserted-by":"publisher","DOI":"10.1038\/310589a0"},{"key":"p_9","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(85)90210-7"},{"key":"p_10","first-page":"2149","article-title":"Solid phase peptide synthesis. Paper I: the synthesis of tetrapeptide. J. Am. chem","volume":"85","author":"Merrifield R. B.","year":"1963","journal-title":"Soc."},{"key":"p_11","doi-asserted-by":"publisher","DOI":"10.1038\/312127a0"},{"key":"p_12","doi-asserted-by":"publisher","DOI":"10.1038\/309418a0"},{"key":"p_13","doi-asserted-by":"publisher","DOI":"10.1038\/311123a0"},{"key":"p_14","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(83)90209-X"}],"container-title":["Proceedings of the Royal Society of London. Series B. Biological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/royalsocietypublishing.org\/doi\/pdf\/10.1098\/rspb.1985.0087","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/royalsocietypublishing.org\/rspb\/article-pdf\/226\/1242\/127\/173534\/rspb.1985.0087.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/royalsocietypublishing.org\/rspb\/article-pdf\/226\/1242\/127\/173534\/rspb.1985.0087.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,1,4]],"date-time":"2026-01-04T04:47:24Z","timestamp":1767502044000},"score":1,"resource":{"primary":{"URL":"https:\/\/royalsocietypublishing.org\/rspb\/article\/226\/1242\/127\/33774\/The-structure-and-function-of-the-epidermal-growth"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1985,10,22]]},"references-count":14,"journal-issue":{"issue":"1242","published-print":{"date-parts":[[1985,10,22]]}},"URL":"https:\/\/doi.org\/10.1098\/rspb.1985.0087","relation":{},"ISSN":["0080-4649","2053-9193"],"issn-type":[{"type":"print","value":"0080-4649"},{"type":"electronic","value":"2053-9193"}],"subject":[],"published":{"date-parts":[[1985,10,22]]}}}