| pubmed-article:3402434 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3402434 | lifeskim:mentions | umls-concept:C0025954 | lld:lifeskim |
| pubmed-article:3402434 | lifeskim:mentions | umls-concept:C0031656 | lld:lifeskim |
| pubmed-article:3402434 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:3402434 | lifeskim:mentions | umls-concept:C0231448 | lld:lifeskim |
| pubmed-article:3402434 | lifeskim:mentions | umls-concept:C0085361 | lld:lifeskim |
| pubmed-article:3402434 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:3402434 | pubmed:dateCreated | 1988-9-16 | lld:pubmed |
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| pubmed-article:3402434 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3402434 | pubmed:abstractText | To determine how microbody proteins enter microbodies, we have previously compared the genes for the cytosolic and glycosomal (microbody) phosphoglycerate kinases (PGKs) of Trypanosoma brucei and found the microbody enzyme to differ from other PGKs and the cytosolic form in two respects: a high net positive charge and a C-terminal extension of 20 amino acids (Osinga et al., 1985). Here we present the comparison of the genes for the cytosolic and glycosomal PGKs of Crithidia fasciculata, another kinetoplastid organism. The amino acid sequences of the two Crithidia isoenzymes are virtually identical, except for a C-terminal extension of 38 amino acids. We conclude that this extension must direct the glycosomal PGK to the glycosome. The extensions of the Crithidia and Trypanosoma enzymes are both rich in small hydrophobic and hydroxyl amino acids. | lld:pubmed |
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| pubmed-article:3402434 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3402434 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3402434 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3402434 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3402434 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:3402434 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:3402434 | pubmed:author | pubmed-author:BorstPP | lld:pubmed |
| pubmed-article:3402434 | pubmed:author | pubmed-author:EversRR | lld:pubmed |
| pubmed-article:3402434 | pubmed:author | pubmed-author:SwinkelsB WBW | lld:pubmed |
| pubmed-article:3402434 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3402434 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:3402434 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3402434 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3402434 | pubmed:pagination | 1159-65 | lld:pubmed |
| pubmed-article:3402434 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:3402434 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3402434 | pubmed:articleTitle | The topogenic signal of the glycosomal (microbody) phosphoglycerate kinase of Crithidia fasciculata resides in a carboxy-terminal extension. | lld:pubmed |
| pubmed-article:3402434 | pubmed:affiliation | Division of Molecular Biology, The Netherlands Cancer Institute, Amsterdam. | lld:pubmed |
| pubmed-article:3402434 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3402434 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:3402434 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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