| pubmed-article:11258900 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11258900 | lifeskim:mentions | umls-concept:C0182158 | lld:lifeskim |
| pubmed-article:11258900 | lifeskim:mentions | umls-concept:C0446373 | lld:lifeskim |
| pubmed-article:11258900 | lifeskim:mentions | umls-concept:C0001516 | lld:lifeskim |
| pubmed-article:11258900 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:11258900 | pubmed:dateCreated | 2001-3-22 | lld:pubmed |
| pubmed-article:11258900 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258900 | pubmed:abstractText | Achieving a satisfactory biochemical explanation for the opportunistic underwater adhesion of marine invertebrates such as mussels and barnacles requires a detailed characterization of proteins extracted from holdfast structures produced by these organisms. Mefp-5 is an adhesive protein derived from the foot of the common mussel, Mytilus edulis, and deposited into the byssal attachment pads. Purification and primary structure of mefp-5 was determined by peptide mapping and cDNA sequencing. The protein is 74 residues long and has a mass of about 9500 Da. Mefp-5 composition shows a strong amino acid bias: aromatic amino acids, lysine, and glycine represent 65 mol % of the composition. More than a third of all the residues in the protein are posttranslationally modified by hydroxylation or phosphorylation. The conversion of tyrosine to 3, 4-dihydroxyphenyl-L-alanine (DOPA) and serine to O-phosphoserine accounts for the hydroxylation and phosphorylation, respectively. Neither modification is complete since variations in the extent of phosphorylation and hydroxylation can be detected by mass spectrometry. More than 75% of the DOPA is adjacent to basic residues, e.g., Lys-DOPA and DOPA-Lys. Phosphoserine occurs in sequences strikingly reminiscent of acidic mineral-binding motifs that appear in statherin, osteopontin, and others. This may be an adaptation for adhesion to the most common substrata for mussels, i.e., calcareous materials. | lld:pubmed |
| pubmed-article:11258900 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258900 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11258900 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258900 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11258900 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11258900 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11258900 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11258900 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:11258900 | pubmed:author | pubmed-author:WaiteJ HJH | lld:pubmed |
| pubmed-article:11258900 | pubmed:author | pubmed-author:QiuSS | lld:pubmed |
| pubmed-article:11258900 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11258900 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:11258900 | pubmed:volume | 40 | lld:pubmed |
| pubmed-article:11258900 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11258900 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11258900 | pubmed:pagination | 2887-93 | lld:pubmed |
| pubmed-article:11258900 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11258900 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11258900 | pubmed:articleTitle | Polyphosphoprotein from the adhesive pads of Mytilus edulis. | lld:pubmed |
| pubmed-article:11258900 | pubmed:affiliation | Department of Cell Biology, Duke University, Durham, North Carolina 27706, USA. waite@lifesci.ucsb.edu | lld:pubmed |
| pubmed-article:11258900 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11258900 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11258900 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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