Heregulin induces tyrosine phosphorylation of HER4/p180erbB4
THE HER4/ERBB4 gene encodes a 180K transmembrane protein (HER4/pl80 erbB4 that is structurally related to the 185K product (HERl/pl85 erbB2 of the HER2/ERBB2 proto-oncogene 1 . A 45K heparin-binding glycoprotein (p45) has been characterized that specifically activates the intrinsic tyrosine kinase a...
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| Veröffentlicht in: | Nature (London) 1993-12, Vol.366 (6454), p.473-475 |
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| creator | Plowman, Gregory D. Green, Janell M. Culouscou, Jean-Michel Carlton, Gary W. Rothwell, Victoria M. Buckley, Sharon |
| description | THE
HER4/ERBB4
gene encodes a 180K transmembrane protein (HER4/pl80
erbB4
that is structurally related to the 185K product (HERl/pl85
erbB2
of the
HER2/ERBB2
proto-oncogene
1
. A 45K heparin-binding glycoprotein (p45) has been characterized that specifically activates the intrinsic tyrosine kinase activity of HER4 (ref. 2). This HER4 ligand shares several features with the heregulin family of proteins, including molecular mass, ability to induce differentiation of breast cancer cells, activation of tyrosine phosphorylation in MDA-MB453 cells, and amino-terminal protein sequence. Heregulin exists as multiple isoforms and all are presumed to interact directly with HER2 (refs 3–6). We have used binding and phosphorylation studies with recombinant ligand on cell lines expressing recombinant receptors, and report here that heregulin, like p45, is a specific ligand for HER4. Furthermore, heregulin fails to induce phosphorylation of HER2 in the absence of HER4. These findings suggest that activation of the HER4 receptor is involved in signal transduction by heregulin. |
| doi_str_mv | 10.1038/366473a0 |
| format | Article |
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HER4/ERBB4
gene encodes a 180K transmembrane protein (HER4/pl80
erbB4
that is structurally related to the 185K product (HERl/pl85
erbB2
of the
HER2/ERBB2
proto-oncogene
1
. A 45K heparin-binding glycoprotein (p45) has been characterized that specifically activates the intrinsic tyrosine kinase activity of HER4 (ref. 2). This HER4 ligand shares several features with the heregulin family of proteins, including molecular mass, ability to induce differentiation of breast cancer cells, activation of tyrosine phosphorylation in MDA-MB453 cells, and amino-terminal protein sequence. Heregulin exists as multiple isoforms and all are presumed to interact directly with HER2 (refs 3–6). We have used binding and phosphorylation studies with recombinant ligand on cell lines expressing recombinant receptors, and report here that heregulin, like p45, is a specific ligand for HER4. Furthermore, heregulin fails to induce phosphorylation of HER2 in the absence of HER4. These findings suggest that activation of the HER4 receptor is involved in signal transduction by heregulin.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/366473a0</identifier><identifier>PMID: 7902537</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Blotting, Western ; Cell Line ; Cell physiology ; CHO Cells ; Cricetinae ; Fundamental and applied biological sciences. Psychology ; Glycoproteins - metabolism ; Glycoproteins - pharmacology ; Humanities and Social Sciences ; Humans ; letter ; Medical research ; Molecular and cellular biology ; Molecular Sequence Data ; multidisciplinary ; Neuregulins ; Oncogene Proteins, Viral - metabolism ; Pharmacology ; Phosphorylation ; Proteins ; Receptor, Epidermal Growth Factor - metabolism ; Receptor, ErbB-2 ; Receptor, ErbB-4 ; Recombinant Proteins - pharmacology ; Science ; Science (multidisciplinary) ; Signal Transduction ; Transfection ; Tyrosine - metabolism</subject><ispartof>Nature (London), 1993-12, Vol.366 (6454), p.473-475</ispartof><rights>Springer Nature Limited 1993</rights><rights>1994 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Dec 2, 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2150-db7c4ab58011eda865c3a47aedd17dbc6795486df3728358ba5b473e044c95143</citedby><cites>FETCH-LOGICAL-c2150-db7c4ab58011eda865c3a47aedd17dbc6795486df3728358ba5b473e044c95143</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/366473a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/366473a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=3803881$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7902537$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Plowman, Gregory D.</creatorcontrib><creatorcontrib>Green, Janell M.</creatorcontrib><creatorcontrib>Culouscou, Jean-Michel</creatorcontrib><creatorcontrib>Carlton, Gary W.</creatorcontrib><creatorcontrib>Rothwell, Victoria M.</creatorcontrib><creatorcontrib>Buckley, Sharon</creatorcontrib><title>Heregulin induces tyrosine phosphorylation of HER4/p180erbB4</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>THE
HER4/ERBB4
gene encodes a 180K transmembrane protein (HER4/pl80
erbB4
that is structurally related to the 185K product (HERl/pl85
erbB2
of the
HER2/ERBB2
proto-oncogene
1
. A 45K heparin-binding glycoprotein (p45) has been characterized that specifically activates the intrinsic tyrosine kinase activity of HER4 (ref. 2). This HER4 ligand shares several features with the heregulin family of proteins, including molecular mass, ability to induce differentiation of breast cancer cells, activation of tyrosine phosphorylation in MDA-MB453 cells, and amino-terminal protein sequence. Heregulin exists as multiple isoforms and all are presumed to interact directly with HER2 (refs 3–6). We have used binding and phosphorylation studies with recombinant ligand on cell lines expressing recombinant receptors, and report here that heregulin, like p45, is a specific ligand for HER4. Furthermore, heregulin fails to induce phosphorylation of HER2 in the absence of HER4. These findings suggest that activation of the HER4 receptor is involved in signal transduction by heregulin.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoproteins - pharmacology</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>letter</subject><subject>Medical research</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Neuregulins</subject><subject>Oncogene Proteins, Viral - metabolism</subject><subject>Pharmacology</subject><subject>Phosphorylation</subject><subject>Proteins</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Receptor, ErbB-2</subject><subject>Receptor, ErbB-4</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Signal Transduction</subject><subject>Transfection</subject><subject>Tyrosine - metabolism</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNplkEtLw0AUhQdRan2Af0AIIqKL2DuZZ8GNlmqFgiC6DpOZSU1JJ3GmWfTfO9JYQReXuzgf595zEDrDcIuByBHhnAqiYA8NMRU8pVyKfTQEyGQKkvBDdBTCEgAYFnSABmIMGSNiiO5m1ttFV1cuqZzptA3JeuObUDmbtB9NiOM3tVpXjUuaMplNX-moxRKsLx7oCTooVR3sab-P0fvj9G0yS-cvT8-T-3mqM8wgNYXQVBVMAsbWKMmZJooKZY3BwhSaizGjkpuSiEwSJgvFipjGAqV6zDAlx-hq69v65rOzYZ2vqqBtXStnmy7kgoOQlGURvPgDLpvOu_hbnkU3iiVjEbreQjrmDN6WeeurlfKbHEP-3Wb-02ZEz3u_rlhZswP7-qJ-2esqaFWXXjldhR1GZHSTOGI3WyxExS2s_33r38kvsRmGIg</recordid><startdate>19931202</startdate><enddate>19931202</enddate><creator>Plowman, Gregory D.</creator><creator>Green, Janell M.</creator><creator>Culouscou, Jean-Michel</creator><creator>Carlton, Gary W.</creator><creator>Rothwell, Victoria M.</creator><creator>Buckley, Sharon</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>19931202</creationdate><title>Heregulin induces tyrosine phosphorylation of HER4/p180erbB4</title><author>Plowman, Gregory D. ; Green, Janell M. ; Culouscou, Jean-Michel ; Carlton, Gary W. ; Rothwell, Victoria M. ; Buckley, Sharon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c2150-db7c4ab58011eda865c3a47aedd17dbc6795486df3728358ba5b473e044c95143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoproteins - pharmacology</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>letter</topic><topic>Medical research</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Neuregulins</topic><topic>Oncogene Proteins, Viral - metabolism</topic><topic>Pharmacology</topic><topic>Phosphorylation</topic><topic>Proteins</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>Receptor, ErbB-2</topic><topic>Receptor, ErbB-4</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Signal Transduction</topic><topic>Transfection</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Plowman, Gregory D.</creatorcontrib><creatorcontrib>Green, Janell M.</creatorcontrib><creatorcontrib>Culouscou, Jean-Michel</creatorcontrib><creatorcontrib>Carlton, Gary W.</creatorcontrib><creatorcontrib>Rothwell, Victoria M.</creatorcontrib><creatorcontrib>Buckley, Sharon</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Proquest Nursing & Allied Health Source</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Plowman, Gregory D.</au><au>Green, Janell M.</au><au>Culouscou, Jean-Michel</au><au>Carlton, Gary W.</au><au>Rothwell, Victoria M.</au><au>Buckley, Sharon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heregulin induces tyrosine phosphorylation of HER4/p180erbB4</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1993-12-02</date><risdate>1993</risdate><volume>366</volume><issue>6454</issue><spage>473</spage><epage>475</epage><pages>473-475</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>THE
HER4/ERBB4
gene encodes a 180K transmembrane protein (HER4/pl80
erbB4
that is structurally related to the 185K product (HERl/pl85
erbB2
of the
HER2/ERBB2
proto-oncogene
1
. A 45K heparin-binding glycoprotein (p45) has been characterized that specifically activates the intrinsic tyrosine kinase activity of HER4 (ref. 2). This HER4 ligand shares several features with the heregulin family of proteins, including molecular mass, ability to induce differentiation of breast cancer cells, activation of tyrosine phosphorylation in MDA-MB453 cells, and amino-terminal protein sequence. Heregulin exists as multiple isoforms and all are presumed to interact directly with HER2 (refs 3–6). We have used binding and phosphorylation studies with recombinant ligand on cell lines expressing recombinant receptors, and report here that heregulin, like p45, is a specific ligand for HER4. Furthermore, heregulin fails to induce phosphorylation of HER2 in the absence of HER4. These findings suggest that activation of the HER4 receptor is involved in signal transduction by heregulin.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>7902537</pmid><doi>10.1038/366473a0</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1993-12, Vol.366 (6454), p.473-475 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76078452 |
| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Blotting, Western Cell Line Cell physiology CHO Cells Cricetinae Fundamental and applied biological sciences. Psychology Glycoproteins - metabolism Glycoproteins - pharmacology Humanities and Social Sciences Humans letter Medical research Molecular and cellular biology Molecular Sequence Data multidisciplinary Neuregulins Oncogene Proteins, Viral - metabolism Pharmacology Phosphorylation Proteins Receptor, Epidermal Growth Factor - metabolism Receptor, ErbB-2 Receptor, ErbB-4 Recombinant Proteins - pharmacology Science Science (multidisciplinary) Signal Transduction Transfection Tyrosine - metabolism |
| title | Heregulin induces tyrosine phosphorylation of HER4/p180erbB4 |
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