Structural organization of C-terminal parts of fibrinogen Aα-chains
Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1983-08, Vol.160 (1), p.291-295 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 295 |
|---|---|
| container_issue | 1 |
| container_start_page | 291 |
| container_title | FEBS letters |
| container_volume | 160 |
| creator | Medved', L.V. Gorkun, O.V. Privalov, P.L. |
| description | Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule. |
| doi_str_mv | 10.1016/0014-5793(83)80985-5 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80616801</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579383809855</els_id><sourcerecordid>13704569</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5265-1ee4197fa010325c4f04452edd2b2d7c7d7fbdd3bedfe1e7b79bca57952d7b373</originalsourceid><addsrcrecordid>eNqNkN9qFDEUxkNR2rX2DSrshYheTM3fSeZGqGtXhUIvtNchk5zUlNnMmswo9a18EZ_JxF32UoVAyPm-852cH0LnBF8QTNrXGBPeCNmxl4q9UrhTohFHaEGUZA3jrXqEFgfLCXqS8z0ub0W6Y3TcUsol5gv07tOUZjvNyQzLMd2ZGH6YKYxxOfrlqpkgbUIs0takKdeaD30KcbyDuLz89bOxX0yI-Sl67M2Q4Wx_n6Lb9dXn1Yfm-ub9x9XldWMFbUVDADjppDeYYEaF5R5zLig4R3vqpJVO-t451oPzQED2suutKd8XRe2ZZKfoxS53m8avM-RJb0K2MAwmwjhnrXBLWoXJP42EleVF2xUj3xltGnNO4PU2hY1JD5pgXSnrilBXhFqVUylrUdqe7fPnfgPu0LTHWvTne91kawafTLQhH2wda6kkNWa9s30PAzz812i9vnpLq1Driv2p1qA3uyAo9L8FSDrbANGCCwnspN0Y_r7QbyVmrFk</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>13704569</pqid></control><display><type>article</type><title>Structural organization of C-terminal parts of fibrinogen Aα-chains</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Medved', L.V. ; Gorkun, O.V. ; Privalov, P.L.</creator><creatorcontrib>Medved', L.V. ; Gorkun, O.V. ; Privalov, P.L.</creatorcontrib><description>Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(83)80985-5</identifier><identifier>PMID: 6224704</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Animals ; Aα-chain ; Biological and medical sciences ; Blood coagulation. Blood cells ; Calorimetry ; Cattle ; Coagulation factors ; Domain ; Fibrinogen ; Fibrinolysin ; Fibrinopeptide A ; Fundamental and applied biological sciences. Psychology ; Macromolecular Substances ; Molecular and cellular biology ; Peptide Fragments - analysis ; Protein Conformation ; Thermodynamics ; Unfolding ; X-fragment</subject><ispartof>FEBS letters, 1983-08, Vol.160 (1), p.291-295</ispartof><rights>1983</rights><rights>FEBS Letters 160 (1983) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1984 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5265-1ee4197fa010325c4f04452edd2b2d7c7d7fbdd3bedfe1e7b79bca57952d7b373</citedby><cites>FETCH-LOGICAL-c5265-1ee4197fa010325c4f04452edd2b2d7c7d7fbdd3bedfe1e7b79bca57952d7b373</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(83)80985-5$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=9362715$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6224704$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Medved', L.V.</creatorcontrib><creatorcontrib>Gorkun, O.V.</creatorcontrib><creatorcontrib>Privalov, P.L.</creatorcontrib><title>Structural organization of C-terminal parts of fibrinogen Aα-chains</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.</description><subject>Animals</subject><subject>Aα-chain</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Calorimetry</subject><subject>Cattle</subject><subject>Coagulation factors</subject><subject>Domain</subject><subject>Fibrinogen</subject><subject>Fibrinolysin</subject><subject>Fibrinopeptide A</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Macromolecular Substances</subject><subject>Molecular and cellular biology</subject><subject>Peptide Fragments - analysis</subject><subject>Protein Conformation</subject><subject>Thermodynamics</subject><subject>Unfolding</subject><subject>X-fragment</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkN9qFDEUxkNR2rX2DSrshYheTM3fSeZGqGtXhUIvtNchk5zUlNnMmswo9a18EZ_JxF32UoVAyPm-852cH0LnBF8QTNrXGBPeCNmxl4q9UrhTohFHaEGUZA3jrXqEFgfLCXqS8z0ub0W6Y3TcUsol5gv07tOUZjvNyQzLMd2ZGH6YKYxxOfrlqpkgbUIs0takKdeaD30KcbyDuLz89bOxX0yI-Sl67M2Q4Wx_n6Lb9dXn1Yfm-ub9x9XldWMFbUVDADjppDeYYEaF5R5zLig4R3vqpJVO-t451oPzQED2suutKd8XRe2ZZKfoxS53m8avM-RJb0K2MAwmwjhnrXBLWoXJP42EleVF2xUj3xltGnNO4PU2hY1JD5pgXSnrilBXhFqVUylrUdqe7fPnfgPu0LTHWvTne91kawafTLQhH2wda6kkNWa9s30PAzz812i9vnpLq1Driv2p1qA3uyAo9L8FSDrbANGCCwnspN0Y_r7QbyVmrFk</recordid><startdate>19830822</startdate><enddate>19830822</enddate><creator>Medved', L.V.</creator><creator>Gorkun, O.V.</creator><creator>Privalov, P.L.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830822</creationdate><title>Structural organization of C-terminal parts of fibrinogen Aα-chains</title><author>Medved', L.V. ; Gorkun, O.V. ; Privalov, P.L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5265-1ee4197fa010325c4f04452edd2b2d7c7d7fbdd3bedfe1e7b79bca57952d7b373</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Animals</topic><topic>Aα-chain</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Calorimetry</topic><topic>Cattle</topic><topic>Coagulation factors</topic><topic>Domain</topic><topic>Fibrinogen</topic><topic>Fibrinolysin</topic><topic>Fibrinopeptide A</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Macromolecular Substances</topic><topic>Molecular and cellular biology</topic><topic>Peptide Fragments - analysis</topic><topic>Protein Conformation</topic><topic>Thermodynamics</topic><topic>Unfolding</topic><topic>X-fragment</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Medved', L.V.</creatorcontrib><creatorcontrib>Gorkun, O.V.</creatorcontrib><creatorcontrib>Privalov, P.L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Medved', L.V.</au><au>Gorkun, O.V.</au><au>Privalov, P.L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural organization of C-terminal parts of fibrinogen Aα-chains</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1983-08-22</date><risdate>1983</risdate><volume>160</volume><issue>1</issue><spage>291</spage><epage>295</epage><pages>291-295</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>Calorimetric studies of fibrinogen melting and of its early degradation products have shown that the C-terminal parts of both the Aα-chains form structural domains which strongly interact with each other in the native fibrinogen molecule.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>6224704</pmid><doi>10.1016/0014-5793(83)80985-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1983-08, Vol.160 (1), p.291-295 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80616801 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Aα-chain Biological and medical sciences Blood coagulation. Blood cells Calorimetry Cattle Coagulation factors Domain Fibrinogen Fibrinolysin Fibrinopeptide A Fundamental and applied biological sciences. Psychology Macromolecular Substances Molecular and cellular biology Peptide Fragments - analysis Protein Conformation Thermodynamics Unfolding X-fragment |
| title | Structural organization of C-terminal parts of fibrinogen Aα-chains |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T07%3A22%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20organization%20of%20C-terminal%20parts%20of%20fibrinogen%20A%CE%B1-chains&rft.jtitle=FEBS%20letters&rft.au=Medved',%20L.V.&rft.date=1983-08-22&rft.volume=160&rft.issue=1&rft.spage=291&rft.epage=295&rft.pages=291-295&rft.issn=0014-5793&rft.eissn=1873-3468&rft.coden=FEBLAL&rft_id=info:doi/10.1016/0014-5793(83)80985-5&rft_dat=%3Cproquest_cross%3E13704569%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=13704569&rft_id=info:pmid/6224704&rft_els_id=0014579383809855&rfr_iscdi=true |