After Insulin Binds
Three recent advances pertinent to the mechanism of insulin action include (i) the discovery that the insulin receptor is an insulin-dependent protein tyrosine kinase, functionally related to certain growth factor receptors and oncogene-encoded proteins, (ii) the molecular cloning of the insulin pro...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 1987-09, Vol.237 (4821), p.1452-1458 |
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| container_title | Science (American Association for the Advancement of Science) |
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| creator | Rosen, Ora M. |
| description | Three recent advances pertinent to the mechanism of insulin action include (i) the discovery that the insulin receptor is an insulin-dependent protein tyrosine kinase, functionally related to certain growth factor receptors and oncogene-encoded proteins, (ii) the molecular cloning of the insulin proreceptor complementary DNA, and (iii) evidence that the protein tyrosine kinase activity of the receptor is essential for insulin action. Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose pphosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man. |
| doi_str_mv | 10.1126/science.2442814 |
| format | Article |
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Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose pphosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.2442814</identifier><identifier>PMID: 2442814</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: The American Association for the Advancement of Science</publisher><subject>Biochemistry ; Biological and medical sciences ; cDNA ; Cell lines ; Cell physiology ; CHO cells ; cloning ; Complementary DNA ; Diabetes mellitus ; DNA - analysis ; Drosophila ; Enzymes ; ErbB Receptors - physiology ; Fundamental and applied biological sciences. 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Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose pphosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man.</description><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>cDNA</subject><subject>Cell lines</subject><subject>Cell physiology</subject><subject>CHO cells</subject><subject>cloning</subject><subject>Complementary DNA</subject><subject>Diabetes mellitus</subject><subject>DNA - analysis</subject><subject>Drosophila</subject><subject>Enzymes</subject><subject>ErbB Receptors - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormonal regulation</subject><subject>Humans</subject><subject>Insulin</subject><subject>Insulin - metabolism</subject><subject>Insulin receptors</subject><subject>Medical research</subject><subject>Membrane proteins</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Oncogenes</subject><subject>Phosphorylation</subject><subject>Phosphoserine - metabolism</subject><subject>Phosphothreonine - metabolism</subject><subject>Phosphotyrosine</subject><subject>protein-tyrosine kinase</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Receptor, Insulin - genetics</subject><subject>Receptor, Insulin - physiology</subject><subject>Receptors</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>reviews</subject><subject>Substrate Specificity</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - metabolism</subject><subject>Vertebrata</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqN0s2LEzEYBvAgylpXTx68KCwielhn9813cuwWrYViD35cQ5p5p0yZzuwmM6D_vZEOu6sUtuQQyPNLQshDyCsKF5QydZlCjW3ACyYEM1Q8IhMKVhaWAX9MJgBcFQa0fEqepbQFyJnlJ-Rk5BPyclr1GM8WbRqauj27qtsyPSdPKt8kfDHOp-TH50_fZ1-K5Wq-mE2XRdBK9kWF1AjGVQhobcCSaqpUYJxKs65M4FCupWUeuS4ZUCZM5Y0UAswahBVrxk_J-_2517G7GTD1blengE3jW-yG5LTWoKmwD0IuqdFCmgchFVqCtTTDt__BbTfENr_WMcolB6VERud7tPENurqtuj76sMEWo2-6Fqs6L08VUGtBZ_3xgM6jxF0dDvAP__AsevzVb_yQklt8-3qsXP08Vl7Nj5Rmvrwvzw_J0DUNbtDlQsxW9_XlXofYpRSxctex3vn421FwfwvrxsK6sYF5x5vxJ4b1Dstbf5e_G3Ofgm-q6NtQp1umuWFaQWav92yb-i7e3aqsNRL4H_Og9Pg</recordid><startdate>19870918</startdate><enddate>19870918</enddate><creator>Rosen, Ora M.</creator><general>The American Association for the Advancement of Science</general><general>American Association for the Advancement of Science</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>8GL</scope><scope>IBG</scope><scope>IOV</scope><scope>ISN</scope><scope>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>M7Z</scope><scope>7X8</scope></search><sort><creationdate>19870918</creationdate><title>After Insulin Binds</title><author>Rosen, Ora M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c765t-fe184236cce99ced17166c23158bf8c30db592ae37d201248fa854408b0494b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>cDNA</topic><topic>Cell lines</topic><topic>Cell physiology</topic><topic>CHO cells</topic><topic>cloning</topic><topic>Complementary DNA</topic><topic>Diabetes mellitus</topic><topic>DNA - analysis</topic><topic>Drosophila</topic><topic>Enzymes</topic><topic>ErbB Receptors - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormonal regulation</topic><topic>Humans</topic><topic>Insulin</topic><topic>Insulin - metabolism</topic><topic>Insulin receptors</topic><topic>Medical research</topic><topic>Membrane proteins</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Oncogenes</topic><topic>Phosphorylation</topic><topic>Phosphoserine - metabolism</topic><topic>Phosphothreonine - metabolism</topic><topic>Phosphotyrosine</topic><topic>protein-tyrosine kinase</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proteins</topic><topic>Receptor, Insulin - genetics</topic><topic>Receptor, Insulin - physiology</topic><topic>Receptors</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>reviews</topic><topic>Substrate Specificity</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - metabolism</topic><topic>Vertebrata</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rosen, Ora M.</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>Gale In Context: High School</collection><collection>Gale In Context: Biography</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Canada</collection><collection>Aluminium Industry Abstracts</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Ecology Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Biochemistry Abstracts 1</collection><collection>MEDLINE - Academic</collection><jtitle>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rosen, Ora M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>After Insulin Binds</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1987-09-18</date><risdate>1987</risdate><volume>237</volume><issue>4821</issue><spage>1452</spage><epage>1458</epage><pages>1452-1458</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Three recent advances pertinent to the mechanism of insulin action include (i) the discovery that the insulin receptor is an insulin-dependent protein tyrosine kinase, functionally related to certain growth factor receptors and oncogene-encoded proteins, (ii) the molecular cloning of the insulin proreceptor complementary DNA, and (iii) evidence that the protein tyrosine kinase activity of the receptor is essential for insulin action. Efforts are now focusing on the physiological substrates for the receptor kinase. Experience to date suggests that they will be rare proteins whose pphosphorylation in intact cells may be transient. The advantages of attempting to dissect the initial biochemical pathway of insulin action include the wealth of information about the metabolic consequences of insulin action and the potential for genetic analysis in Drosophila and in man.</abstract><cop>Washington, DC</cop><pub>The American Association for the Advancement of Science</pub><pmid>2442814</pmid><doi>10.1126/science.2442814</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1987-09, Vol.237 (4821), p.1452-1458 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_77707149 |
| source | MEDLINE; Science Magazine; JSTOR Archive Collection A-Z Listing |
| subjects | Biochemistry Biological and medical sciences cDNA Cell lines Cell physiology CHO cells cloning Complementary DNA Diabetes mellitus DNA - analysis Drosophila Enzymes ErbB Receptors - physiology Fundamental and applied biological sciences. Psychology Hormonal regulation Humans Insulin Insulin - metabolism Insulin receptors Medical research Membrane proteins Molecular and cellular biology Molecular Weight Oncogenes Phosphorylation Phosphoserine - metabolism Phosphothreonine - metabolism Phosphotyrosine protein-tyrosine kinase Protein-Tyrosine Kinases - metabolism Proteins Receptor, Insulin - genetics Receptor, Insulin - physiology Receptors Receptors, Cell Surface - metabolism reviews Substrate Specificity Tyrosine - analogs & derivatives Tyrosine - metabolism Vertebrata |
| title | After Insulin Binds |
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