pubmed-article:12051774 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0328767 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0033382 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C1413246 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C1826471 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C1837441 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0872252 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0023089 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0013860 | lld:lifeskim |
pubmed-article:12051774 | lifeskim:mentions | umls-concept:C0205088 | lld:lifeskim |
pubmed-article:12051774 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:12051774 | pubmed:dateCreated | 2002-6-7 | lld:pubmed |
pubmed-article:12051774 | pubmed:abstractText | HIV-1(LAV-1) particles were collected by ultracentrifugation, treated with subtilisin, and then purified by Sepharose CL-4B column chromatography to remove microvesicles. The lysate of the purified human immunodeficiency virus type 1 (HIV-1) particles was subjected to two-dimensional (2D) gel electrophoresis and stained, and the stained spots were excised and digested with trypsin. The resulting peptide fragments were characterized by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). Twenty-five proteins were identified as the proteins inside the virion and the acid-labile formyl group of an amino terminal proline residue of HIV-1(LAV-1) p24(gag) was determined by MALDI-TOF MS before and after weak-acid treatments (0.6 N hydrochloric acid) and confirmed by post-source decay (PSD) of the N-formylated N-terminal tryptic peptide (N-formylated Pro(1)-Arg(18)). The role of formylation has been unclear so far, but it is surmised that the acid-labile formylation of HIV-1(LAV-1) p24(gag) may play a critical role in the formation of the HIV-1 core for conferring HIV-1 infectivity. | lld:pubmed |
pubmed-article:12051774 | pubmed:language | eng | lld:pubmed |
pubmed-article:12051774 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12051774 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12051774 | pubmed:month | May | lld:pubmed |
pubmed-article:12051774 | pubmed:issn | 0006-291X | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:AirE WEW | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:TakahashiIchi... | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:MisumiShogoS | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:FuchigamiTaka... | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:TakamuneNobut... | lld:pubmed |
pubmed-article:12051774 | pubmed:author | pubmed-author:TakamaMichiho... | lld:pubmed |
pubmed-article:12051774 | pubmed:copyrightInfo | (c) 2002 Elsevier Science (USA). | lld:pubmed |
pubmed-article:12051774 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12051774 | pubmed:day | 10 | lld:pubmed |
pubmed-article:12051774 | pubmed:volume | 293 | lld:pubmed |
pubmed-article:12051774 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12051774 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12051774 | pubmed:pagination | 1107-13 | lld:pubmed |
pubmed-article:12051774 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:12051774 | pubmed:year | 2002 | lld:pubmed |
pubmed-article:12051774 | pubmed:articleTitle | Acid-labile formylation of amino terminal proline of human immunodeficiency virus type 1 p24(gag) was found by proteomics using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry. | lld:pubmed |
pubmed-article:12051774 | pubmed:affiliation | Department of Biochemistry, Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, Japan. | lld:pubmed |
pubmed-article:12051774 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12051774 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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