| pubmed-article:8139035 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C0017279 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:8139035 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:8139035 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8139035 | pubmed:dateCreated | 1994-4-25 | lld:pubmed |
| pubmed-article:8139035 | pubmed:abstractText | Retroviral Gag proteins are targeted to the plasma membrane, where they play the central role in virion formation. Several studies have suggested that the membrane-binding signal is contained within the amino-terminal matrix sequence; however, the precise location has never been determined for the Gag protein of any retrovirus. In this report, we show that the first 31 residues of human immunodeficiency virus type 1 Gag protein can function independently as a membrane-targeting domain when fused to heterologous proteins. A bipartite membrane-targeting motif was identified, consisting of the myristylated N-terminal 14 amino acids and a highly basic region that binds acidic phospholipids. Replacement of the N-terminal membrane-targeting domain of pp60v-src with that of human immunodeficiency virus type 1 Gag elicits efficient membrane binding and a transforming phenotype. Removal of myristate or the basic region results in decreased membrane binding of Gag-Src chimeras in vitro and impaired virion formation by Pr55gag in vivo. We propose that the N-terminal Gag sequence functions as a targeting signal to direct interaction with acidic phospholipids on the cytoplasmic leaflet of the plasma membrane. | lld:pubmed |
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| pubmed-article:8139035 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8139035 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8139035 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8139035 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8139035 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8139035 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8139035 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:8139035 | pubmed:author | pubmed-author:ReshM DMD | lld:pubmed |
| pubmed-article:8139035 | pubmed:author | pubmed-author:ZhouWW | lld:pubmed |
| pubmed-article:8139035 | pubmed:author | pubmed-author:WillsJ WJW | lld:pubmed |
| pubmed-article:8139035 | pubmed:author | pubmed-author:ParentL JLJ | lld:pubmed |
| pubmed-article:8139035 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8139035 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:8139035 | pubmed:geneSymbol | gag | lld:pubmed |
| pubmed-article:8139035 | pubmed:owner | NLM | lld:pubmed |
