| pubmed-article:9356340 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9356340 | lifeskim:mentions | umls-concept:C0206273 | lld:lifeskim |
| pubmed-article:9356340 | lifeskim:mentions | umls-concept:C0026649 | lld:lifeskim |
| pubmed-article:9356340 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9356340 | lifeskim:mentions | umls-concept:C1136102 | lld:lifeskim |
| pubmed-article:9356340 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9356340 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:9356340 | pubmed:dateCreated | 1997-12-2 | lld:pubmed |
| pubmed-article:9356340 | pubmed:abstractText | The role of bean common mosaic necrosis potyvirus (BCMNV) and lettuce mosaic potyvirus (LMV) proteins was investigated in terms of their capacity to function as viral movement proteins (MPs). Using Escherichia coli-expressed proteins and microinjection techniques, direct evidence was obtained that both the potyviral capsid protein (CP) and helper component- proteinase (HC-Pro) function in this capacity, in that both proteins (a) trafficked from cell to cell, (b) induced an increase in plasmodesmal size exclusion limit, and (c) facilitated cell-to-cell movement of viral RNA. CP and HC-Pro mutants were also produced and used in microinjection experiments. Mutations in the core region of the CP either impaired (single and double amino acid substitution mutants) or abolished (triple amino acid substitution mutant) cell-to-cell movement, as did C-terminal deletion mutants in HC-Pro. The BCMNV P1, CI, NIa, and NIb proteins did not exhibit viral MP properties, but NIa and NIb proteins were found to accumulate within the nuclei of injected cells. These results further establish the multifunctional nature of the potyvirus CP and HC-Pro. | lld:pubmed |
| pubmed-article:9356340 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9356340 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9356340 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9356340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9356340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9356340 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9356340 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9356340 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9356340 | pubmed:issn | 0042-6822 | lld:pubmed |
| pubmed-article:9356340 | pubmed:author | pubmed-author:LucasW JWJ | lld:pubmed |
| pubmed-article:9356340 | pubmed:author | pubmed-author:GilbertsonR... | lld:pubmed |
| pubmed-article:9356340 | pubmed:author | pubmed-author:AllisonR FRF | lld:pubmed |
| pubmed-article:9356340 | pubmed:author | pubmed-author:RojasM RMR | lld:pubmed |
| pubmed-article:9356340 | pubmed:author | pubmed-author:ZerbiniF MFM | lld:pubmed |
| pubmed-article:9356340 | pubmed:copyrightInfo | Copyright 1997 Academic Press. | lld:pubmed |
| pubmed-article:9356340 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9356340 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:9356340 | pubmed:volume | 237 | lld:pubmed |
| pubmed-article:9356340 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9356340 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9356340 | pubmed:pagination | 283-95 | lld:pubmed |
| pubmed-article:9356340 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:meshHeading | pubmed-meshheading:9356340-... | lld:pubmed |
| pubmed-article:9356340 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9356340 | pubmed:articleTitle | Capsid protein and helper component-proteinase function as potyvirus cell-to-cell movement proteins. | lld:pubmed |
| pubmed-article:9356340 | pubmed:affiliation | Division of Biological Sciences, University of California, Davis, California 95616, USA. | lld:pubmed |
| pubmed-article:9356340 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9356340 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9356340 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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