pubmed-article:14990734 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C1176457 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C1136102 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C1427831 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
pubmed-article:14990734 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:14990734 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:14990734 | pubmed:dateCreated | 2004-3-1 | lld:pubmed |
pubmed-article:14990734 | pubmed:abstractText | The core protein P3 of Rice dwarf virus constructs asymmetric dimers, one of which is inserted by the amino-terminal region of another P3 protein. The P3 proteins with serial amino-terminal deletions, expressed in a baculovirus system, formed particles with gradually decreasing stability. The capacity for self-assembly disappeared when 52 of the amino-terminal amino acids had been deleted. These results demonstrated that insertion of the amino-terminal arm of one P3 protein into another appears to play an important role in stabilizing the core particles. | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:language | eng | lld:pubmed |
pubmed-article:14990734 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:14990734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:14990734 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:14990734 | pubmed:month | Mar | lld:pubmed |
pubmed-article:14990734 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:MizunoHiroshi... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:TsukiharaTomi... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:NakagawaAtsus... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:MiyazakiNaoyu... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:HagiwaraKyoji... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:ChengR... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:NaitowHisashi... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:HigashiTakahi... | lld:pubmed |
pubmed-article:14990734 | pubmed:author | pubmed-author:OmuraToshihir... | lld:pubmed |
pubmed-article:14990734 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:14990734 | pubmed:volume | 78 | lld:pubmed |
pubmed-article:14990734 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:14990734 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:14990734 | pubmed:pagination | 3145-8 | lld:pubmed |
pubmed-article:14990734 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:14990734 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:14990734 | pubmed:articleTitle | The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus. | lld:pubmed |
pubmed-article:14990734 | pubmed:affiliation | Laboratory of Virology, National Agricultural Research Center, Tsukuba, Ibaraki 305-8666, Japan. | lld:pubmed |
pubmed-article:14990734 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:14990734 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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