| pubmed-article:2920725 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2920725 | lifeskim:mentions | umls-concept:C0332255 | lld:lifeskim |
| pubmed-article:2920725 | lifeskim:mentions | umls-concept:C0069139 | lld:lifeskim |
| pubmed-article:2920725 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2920725 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:2920725 | pubmed:dateCreated | 1989-4-17 | lld:pubmed |
| pubmed-article:2920725 | pubmed:abstractText | Nucleolin (C23 or 100 kDa) is an abundant single-stranded-nucleic-acid-binding nucleolar protein proposed to be involved in the early stages of ribosome assembly. A stable 48-kDa fragment of the protein was produced either by proteolytic activity present in nucleolar extracts or by added trypsin. The hydrodynamic and DNA-binding properties of the 48-kDa fragment were compared with the parent molecule. Protein sequencing indicated that the fragment begins at residue 282; amino acid composition of the fragment including 10-12 methylated arginine residues suggested that the fragment contains the entire COOH-terminal two-thirds of the protein. The 48-kDa fragment was more globular than nucleolin, as indicated by a lower frictional coefficient (1.3 vs. 2.0 for nucleolin) and a similar sedimentation coefficient (4.1-4.3S) in spite of the reduction in molecular mass. Although the 48-kDa fragment retained single-stranded-DNA-binding activity, the binding capacity and the ability to reassociate DNA were about fivefold and sixfold lower, respectively, than nucleolin. Similarly, tenfold higher concentrations of the 48-kDa fragment were required to form nucleoprotein aggregates. These results suggest that nucleolin contains a globular COOH-terminal domain for nucleic-acid binding and a NH2-terminal region which is involved in protein-protein interactions and modulating nucleic-acid-binding activity. | lld:pubmed |
| pubmed-article:2920725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2920725 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2920725 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2920725 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:2920725 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:OlsonM OMO | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:RichterAA | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:AmalricFF | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:Caizergues-Fe... | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:SappMM | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:WeisshartKK | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:WallaceM OMO | lld:pubmed |
| pubmed-article:2920725 | pubmed:author | pubmed-author:KirsteinM NMN | lld:pubmed |
| pubmed-article:2920725 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2920725 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2920725 | pubmed:volume | 179 | lld:pubmed |
| pubmed-article:2920725 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2920725 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2920725 | pubmed:pagination | 541-8 | lld:pubmed |
| pubmed-article:2920725 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
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| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
| pubmed-article:2920725 | pubmed:meshHeading | pubmed-meshheading:2920725-... | lld:pubmed |
| pubmed-article:2920725 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2920725 | pubmed:articleTitle | Characterization of a 48-kDa nucleic-acid-binding fragment of nucleolin. | lld:pubmed |
| pubmed-article:2920725 | pubmed:affiliation | Fakultät für Biologie, Universität Konstanz. | lld:pubmed |
| pubmed-article:2920725 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2920725 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2920725 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2920725 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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