| pubmed-article:8495750 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C1706204 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C1555721 | lld:lifeskim |
| pubmed-article:8495750 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:8495750 | pubmed:issue | 1-2 | lld:pubmed |
| pubmed-article:8495750 | pubmed:dateCreated | 1993-6-24 | lld:pubmed |
| pubmed-article:8495750 | pubmed:abstractText | A point mutation (Ala-589 to Thr) in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1) has been shown to decrease the sensitivity of the virus to the neutralizing effect of human HIV-1 specific antibodies [(1990) J. Virol. 64, 3240-3248]. Here 17-residue peptides with the parental and mutant sequences were compared: the parental peptide bound antibodies of sera from HIV-1 infected persons more frequently and with higher affinity than the mutant peptide. However, according to circular dichroism (CD), NMR spectroscopy and molecular modelling the peptides have indistinguishable backbone conformations under a variety of experimental conditions. These techniques showed for both peptides that no ordered helix was present in water solution. However, for both peptides in alcohol-water solutions approximately 60% alpha-helix could be induced. The three-dimensional structures of these peptides provide a basis for understanding how this mutation in the transmembrane protein may affect the interaction with both the outer envelope glycoprotein and with antibodies. | lld:pubmed |
| pubmed-article:8495750 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8495750 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8495750 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8495750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8495750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8495750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8495750 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8495750 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8495750 | pubmed:month | May | lld:pubmed |
| pubmed-article:8495750 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:BlombergJJ | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:FerrettiJ AJA | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:PipkornRR | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:RAOS SSS | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:HiltonBB | lld:pubmed |
| pubmed-article:8495750 | pubmed:author | pubmed-author:KlasseJJ | lld:pubmed |
| pubmed-article:8495750 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8495750 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:8495750 | pubmed:volume | 323 | lld:pubmed |
| pubmed-article:8495750 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8495750 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8495750 | pubmed:pagination | 68-72 | lld:pubmed |
| pubmed-article:8495750 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
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| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:meshHeading | pubmed-meshheading:8495750-... | lld:pubmed |
| pubmed-article:8495750 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8495750 | pubmed:articleTitle | Three-dimensional structure and antigenicity of transmembrane-protein peptides of the human immunodeficiency virus type 1. Effects of a neutralization-escape substitution. | lld:pubmed |
| pubmed-article:8495750 | pubmed:affiliation | Department of Medical Microbiology, University of Lund, Sweden. | lld:pubmed |
| pubmed-article:8495750 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8495750 | lld:pubmed |
