| pubmed-article:11399764 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11399764 | lifeskim:mentions | umls-concept:C0596119 | lld:lifeskim |
| pubmed-article:11399764 | lifeskim:mentions | umls-concept:C0032150 | lld:lifeskim |
| pubmed-article:11399764 | lifeskim:mentions | umls-concept:C1514570 | lld:lifeskim |
| pubmed-article:11399764 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11399764 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:11399764 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:11399764 | pubmed:dateCreated | 2001-8-13 | lld:pubmed |
| pubmed-article:11399764 | pubmed:abstractText | Plasmodium falciparum apical membrane antigen-1 (PfAMA-1) is a malaria merozoite integral membrane protein that plays an essential but poorly understood role in invasion of host erythrocytes. The PfAMA-1 ectodomain comprises three disulfide-constrained domains, the first of which (domain I) is preceded by an N-terminal prosequence. PfAMA-1 is initially routed to secretory organelles at the apical end of the merozoite, where the 83-kDa precursor (PfAMA-1(83)) is converted to a 66-kDa form (PfAMA-1(66)). At about the time of erythrocyte invasion, PfAMA-1(66) selectively translocates onto the merozoite surface. Here we use direct microsequencing and mass spectrometric peptide mass fingerprinting to characterize in detail the primary structure and proteolytic processing of PfAMA-1. We have determined the site at which processing takes place to convert PfAMA-1(83) to PfAMA-1(66) and have shown that both species possess a completely intact and unmodified transmembrane and cytoplasmic domain. Following relocation to the merozoite surface, PfAMA-1(66) is further proteolytically cleaved at one of two alternative sites, either between domains II and III, or at a membrane-proximal site following domain III. As a result, the bulk of the ectodomain is shed from the parasite surface in the form of two soluble fragments of 44 and 48 kDa. PfAMA-1 is not detectably modified by the addition of N-linked oligosaccharides. | lld:pubmed |
| pubmed-article:11399764 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11399764 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11399764 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11399764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11399764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11399764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11399764 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11399764 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11399764 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11399764 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11399764 | pubmed:author | pubmed-author:ThomasA WAW | lld:pubmed |
| pubmed-article:11399764 | pubmed:author | pubmed-author:BlackmanM JMJ | lld:pubmed |
| pubmed-article:11399764 | pubmed:author | pubmed-author:HowellS ASA | lld:pubmed |
| pubmed-article:11399764 | pubmed:author | pubmed-author:KockenC HCH | lld:pubmed |
| pubmed-article:11399764 | pubmed:author | pubmed-author:Withers-Marti... | lld:pubmed |
| pubmed-article:11399764 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11399764 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:11399764 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11399764 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11399764 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11399764 | pubmed:pagination | 31311-20 | lld:pubmed |
| pubmed-article:11399764 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11399764 | pubmed:meshHeading | pubmed-meshheading:11399764... | lld:pubmed |
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| pubmed-article:11399764 | pubmed:meshHeading | pubmed-meshheading:11399764... | lld:pubmed |
| pubmed-article:11399764 | pubmed:meshHeading | pubmed-meshheading:11399764... | lld:pubmed |
| pubmed-article:11399764 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11399764 | pubmed:articleTitle | Proteolytic processing and primary structure of Plasmodium falciparum apical membrane antigen-1. | lld:pubmed |
| pubmed-article:11399764 | pubmed:affiliation | Division of Protein Structure and the Division of Parasitology, National Institute for Medical Research, Mill Hill, London NW7 1AA, United Kingdom. | lld:pubmed |
| pubmed-article:11399764 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11399764 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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