pubmed-article:19400954 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0042216 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C1167395 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0887882 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C1853155 | lld:lifeskim |
pubmed-article:19400954 | lifeskim:mentions | umls-concept:C0005495 | lld:lifeskim |
pubmed-article:19400954 | pubmed:dateCreated | 2009-5-25 | lld:pubmed |
pubmed-article:19400954 | pubmed:abstractText | Proteins associated with the late endosome (LE) appear to play a central role in the envelopment of a number of taxonomically diverse viruses. How viral proteins interact with LE-associated proteins to facilitate envelopment is not well understood. LE-derived transport vesicles form through the interaction of Rab9 GTPase with cargo proteins, and TIP47, a Rab9-specific effector protein. Vaccinia virus (VV) induces a wrapping complex derived from intracellular host membranes to envelope intracellular mature virus particles producing egress-competent forms of virus. | lld:pubmed |
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pubmed-article:19400954 | pubmed:language | eng | lld:pubmed |
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pubmed-article:19400954 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:19400954 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19400954 | pubmed:issn | 1743-422X | lld:pubmed |
pubmed-article:19400954 | pubmed:author | pubmed-author:JordanRobertR | lld:pubmed |
pubmed-article:19400954 | pubmed:author | pubmed-author:GuangYangY | lld:pubmed |
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pubmed-article:19400954 | pubmed:author | pubmed-author:ChenYaliY | lld:pubmed |
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pubmed-article:19400954 | pubmed:author | pubmed-author:HarverChrisC | lld:pubmed |
pubmed-article:19400954 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19400954 | pubmed:volume | 6 | lld:pubmed |
pubmed-article:19400954 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19400954 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19400954 | pubmed:pagination | 44 | lld:pubmed |
pubmed-article:19400954 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:19400954 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19400954 | pubmed:articleTitle | Vaccinia virus p37 interacts with host proteins associated with LE-derived transport vesicle biogenesis. | lld:pubmed |
pubmed-article:19400954 | pubmed:affiliation | SIGA Technologies Inc, Corvallis, Oregon 97333, USA. ychen@siga.com | lld:pubmed |
pubmed-article:19400954 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19400954 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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