Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly
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Veröffentlicht in: | Journal of Virology 1993-05, Vol.67 (5), p.2486-2495 |
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container_title | Journal of Virology |
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creator | Haynes, J. I. 2nd Chang, D. Consigli, R. A. Spooner, B. S. |
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doi_str_mv | 10.1128/JVI.67.5.2486-2495.1993 |
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</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/JVI.67.5.2486-2495.1993</identifier><identifier>PMID: 8386264</identifier><language>eng</language><publisher>Legacy CDMS: American Society for Microbiology</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Biological and medical sciences ; Calcium - metabolism ; Capsid - metabolism ; Capsid - ultrastructure ; Capsid Proteins ; Cells, Cultured ; Fundamental and applied biological sciences. Psychology ; Immunohistochemistry ; Life Sciences (General) ; Mice ; Microbiology ; Microscopy, Electron ; Molecular Sequence Data ; Morphology, structure, chemical composition, physicochemical properties ; Mutagenesis, Site-Directed ; polyomavirus ; Polyomavirus - genetics ; Polyomavirus - growth & development ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Recombinant Proteins - ultrastructure ; Sequence Deletion ; Sequence Homology, Amino Acid ; Structure-Activity Relationship ; Transfection ; Virology</subject><ispartof>Journal of Virology, 1993-05, Vol.67 (5), p.2486-2495</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c572t-cf0f4f83418bcb6970941bbe310fef39dd941bafd677402c65001de45a94add53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC237567/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC237567/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4748899$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8386264$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haynes, J. I. 2nd</creatorcontrib><creatorcontrib>Chang, D.</creatorcontrib><creatorcontrib>Consigli, R. A.</creatorcontrib><creatorcontrib>Spooner, B. S.</creatorcontrib><title>Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>Article Usage Stats
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</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Capsid - metabolism</subject><subject>Capsid - ultrastructure</subject><subject>Capsid Proteins</subject><subject>Cells, Cultured</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunohistochemistry</subject><subject>Life Sciences (General)</subject><subject>Mice</subject><subject>Microbiology</subject><subject>Microscopy, Electron</subject><subject>Molecular Sequence Data</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Mutagenesis, Site-Directed</subject><subject>polyomavirus</subject><subject>Polyomavirus - genetics</subject><subject>Polyomavirus - growth & development</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Recombinant Proteins - ultrastructure</subject><subject>Sequence Deletion</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-Activity Relationship</subject><subject>Transfection</subject><subject>Virology</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>CYI</sourceid><sourceid>EIF</sourceid><recordid>eNpVUU1v1DAUtBBVWRb-AYggIW4J_rZz6AFVQIuK4AAVEgfL8ceuqyQOcbJo_z1Od7VqT9bzzLw37w0AbxCsEMLyw9fb64qLilWYSl5iWrMK1TV5AlYI1rJkDNGnYAUhxiUj8vcz8DylOwgRpZyeg3NJJMecrsCfb_OkpxD7VIS-mLauGO4_dq4wujVh7som9Db0m8LGTmdO9MUQ230udmGcU3H7AxXae2emrBhSsIVOyXVNu38Bzrxuk3t5fNfg1-dPPy-vypvvX64vP96Uhgk8lcZDT70kFMnGNLwWsKaoaRxB0DtPamuXWnvLhaAQG87yHtZRpmuqrWVkDS4OfYe56Zw1rp9G3aphDJ0e9yrqoB4jfdiqTdwpTATjIuvfH_Vj_Du7NKkuJOPaVvcuzkkhTgWhhGeiOBDNGFManT_NQFAtsai7XVBcKKaWWNQSi1piycrXDy2edMccMv7uiOuU7-5H3ZuQTjQqqJS5zxq8OtB6nbTKyySFIcz3gJCKxd_bA7wNm-2_MDqlU_fYE_kP_lesyA</recordid><startdate>19930501</startdate><enddate>19930501</enddate><creator>Haynes, J. 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S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c572t-cf0f4f83418bcb6970941bbe310fef39dd941bafd677402c65001de45a94add53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Capsid - metabolism</topic><topic>Capsid - ultrastructure</topic><topic>Capsid Proteins</topic><topic>Cells, Cultured</topic><topic>Fundamental and applied biological sciences. 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</abstract><cop>Legacy CDMS</cop><pub>American Society for Microbiology</pub><pmid>8386264</pmid><doi>10.1128/JVI.67.5.2486-2495.1993</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Base Sequence Biological and medical sciences Calcium - metabolism Capsid - metabolism Capsid - ultrastructure Capsid Proteins Cells, Cultured Fundamental and applied biological sciences. Psychology Immunohistochemistry Life Sciences (General) Mice Microbiology Microscopy, Electron Molecular Sequence Data Morphology, structure, chemical composition, physicochemical properties Mutagenesis, Site-Directed polyomavirus Polyomavirus - genetics Polyomavirus - growth & development Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Recombinant Proteins - ultrastructure Sequence Deletion Sequence Homology, Amino Acid Structure-Activity Relationship Transfection Virology |
title | Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly |
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