| pubmed-article:7556077 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0066030 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C0002270 | lld:lifeskim |
| pubmed-article:7556077 | lifeskim:mentions | umls-concept:C1517645 | lld:lifeskim |
| pubmed-article:7556077 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:7556077 | pubmed:dateCreated | 1995-10-27 | lld:pubmed |
| pubmed-article:7556077 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7556077 | pubmed:abstractText | Accumulation of globin mRNAs during erythroid differentiation is dependent on their extraordinary stability. The longevity of human alpha-globin mRNA is associated with a ribonucleoprotein complex (alpha-complex) formed on the 3' untranslated region (3'UTR). One or more of the proteins within this alpha-complex contain strong polycytosine [poly(C)] binding (alpha PCB) activity. In the present report we purify alpha PCB activity from human erythroid K562 cells. Although not able to bind the alpha-globin 3'UTR directly, alpha PCB activity is sufficient to complement alpha-complex formation in a cytosolic extract depleted of poly(C) binding activity. Peptide microsequencing demonstrates that alpha PCB activity contains two structurally related poly(C) binding proteins. These two proteins, alpha-complex protein (alpha CP)-1 and -2, have an overall structural identity of 80% and contain three repeats of the K homology (KH) domain which is found in a subset of RNA binding proteins. Epitope-tagged recombinant alpha CP-1 and alpha CP-2 expressed in cells are each incorporated into the alpha-complex. We conclude that alpha CP-1 and alpha CP-2, members of the KH domain RNA binding protein family, are involved in formation of a sequence-specific alpha-globin mRNP complex associated with alpha-globin mRNA stability. As such this represents the first example of a specific function for this class of proteins and suggests potential roles for other members of this protein family. | lld:pubmed |
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| pubmed-article:7556077 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7556077 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7556077 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7556077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7556077 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7556077 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7556077 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7556077 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7556077 | pubmed:author | pubmed-author:LiebhaberS... | lld:pubmed |
| pubmed-article:7556077 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:7556077 | pubmed:author | pubmed-author:KiledjianMM | lld:pubmed |
| pubmed-article:7556077 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7556077 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7556077 | pubmed:volume | 14 | lld:pubmed |
| pubmed-article:7556077 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7556077 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7556077 | pubmed:pagination | 4357-64 | lld:pubmed |
| pubmed-article:7556077 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7556077 | pubmed:meshHeading | pubmed-meshheading:7556077-... | lld:pubmed |
| pubmed-article:7556077 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7556077 | pubmed:articleTitle | Identification of two KH domain proteins in the alpha-globin mRNP stability complex. | lld:pubmed |
| pubmed-article:7556077 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Genetics, Philadelphia 19104-6145, USA. | lld:pubmed |
| pubmed-article:7556077 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7556077 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7556077 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7556077 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
