New insights into heparin-induced FGF oligomerization
Fibroblast growth factors (FGFs) play important roles in a variety of developmental processes in mammals. The dependence of their activity on heparin binding has been a puzzle that, in recent years, has been the subject of active investigation. Recent structural analyses on complexes of FGFs with he...
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| Veröffentlicht in: | Nature Structural Biology 1998-07, Vol.5 (7), p.527-530 |
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| container_title | Nature Structural Biology |
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| creator | Waksman, Gabriel Herr, Andrew B |
| description | Fibroblast growth factors (FGFs) play important roles in a variety of developmental processes in mammals. The dependence of their activity on heparin binding has been a puzzle that, in recent years, has been the subject of active investigation. Recent structural analyses on complexes of FGFs with heparin fragments or heparin analogs have unveiled the extreme complexity of these systems. |
| doi_str_mv | 10.1038/778 |
| format | Article |
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The dependence of their activity on heparin binding has been a puzzle that, in recent years, has been the subject of active investigation. Recent structural analyses on complexes of FGFs with heparin fragments or heparin analogs have unveiled the extreme complexity of these systems.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Dimerization</subject><subject>Fibroblast Growth Factors - chemistry</subject><subject>Heparin - chemistry</subject><subject>Life Sciences</subject><subject>Mammals</subject><subject>Membrane Biology</subject><subject>news-and-views</subject><subject>Protein Conformation</subject><subject>Protein Structure</subject><issn>1072-8368</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkNFKwzAUhoMoc04fQago3lWTnjRJL2W4KQy9UfAupG26ZbTJTFpEn95Ixy7kXJwD_8cH50doRvAdwSDuORdHaJoBkBRY_nGMpgTzLBXAxCk6C2GLMaEUFxM0KRjLCSNTlL_or8TYYNabPsSjd8lG75Q3NjW2HipdJ4vlInGtWbtOe_OjeuPsOTppVBv0xX7P0Pvi8W3-lK5el8_zh1VaQQZ9SqDItBAqz3gFdU6bEmicktYMGAPOgRQ5BZUxUpZlxQRogkWjKkoANG1ghm5H7867z0GHXnYmVLptldVuCJIXRcFzjiN4PYKVdyF43cidN53y35Jg-VeOjOVE6nKvG8pO1wdm30bMb8Y8xMSutZdbN3gbP_ynuRoxq_rB64PGhhLzQsj4LvwCaGdzjA</recordid><startdate>19980701</startdate><enddate>19980701</enddate><creator>Waksman, Gabriel</creator><creator>Herr, Andrew B</creator><general>Nature Publishing Group US</general><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>7X8</scope></search><sort><creationdate>19980701</creationdate><title>New insights into heparin-induced FGF oligomerization</title><author>Waksman, Gabriel ; Herr, Andrew B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c323t-1392e88a527c3d54fb34343b4d6366377319543a261bbbc683e108fac4133e4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Dimerization</topic><topic>Fibroblast Growth Factors - chemistry</topic><topic>Heparin - chemistry</topic><topic>Life Sciences</topic><topic>Mammals</topic><topic>Membrane Biology</topic><topic>news-and-views</topic><topic>Protein Conformation</topic><topic>Protein Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Waksman, Gabriel</creatorcontrib><creatorcontrib>Herr, Andrew B</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Waksman, Gabriel</au><au>Herr, Andrew B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New insights into heparin-induced FGF oligomerization</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>1998-07-01</date><risdate>1998</risdate><volume>5</volume><issue>7</issue><spage>527</spage><epage>530</epage><pages>527-530</pages><issn>1072-8368</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>Fibroblast growth factors (FGFs) play important roles in a variety of developmental processes in mammals. 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| fulltext | fulltext |
| identifier | ISSN: 1072-8368 |
| ispartof | Nature Structural Biology, 1998-07, Vol.5 (7), p.527-530 |
| issn | 1072-8368 2331-365X 1545-9985 |
| language | eng |
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| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Dimerization Fibroblast Growth Factors - chemistry Heparin - chemistry Life Sciences Mammals Membrane Biology news-and-views Protein Conformation Protein Structure |
| title | New insights into heparin-induced FGF oligomerization |
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