| pubmed-article:10336646 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0241888 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0152025 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0032923 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C1706204 | lld:lifeskim |
| pubmed-article:10336646 | lifeskim:mentions | umls-concept:C1555721 | lld:lifeskim |
| pubmed-article:10336646 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10336646 | pubmed:dateCreated | 1999-6-24 | lld:pubmed |
| pubmed-article:10336646 | pubmed:abstractText | The Ile-->Ser84 substitution in the thyroid hormone transport protein transthyretin is one of over 50 variations found to be associated with familial amyloid polyneuropathy, a hereditary type of lethal amyloidosis. Using a peptide analogue of the loop containing residue 84 in transthyretin, we have examined the putative local structural effects of this substitution using 1H-NMR spectroscopy. The peptide, containing residues 71-93 of transthyretin with its termini linked via a disulfide bond, was found to possess the same helix-turn motif as in the corresponding region of the crystallographically derived structure of transthyretin in 20% trifluoroethanol (TFE) solution. It therefore, represents a useful model with which to examine the effects of amyloidogenic substitutions. In a peptide analogue containing the Ile84-->Ser substitution it was found that the substitution does not greatly disrupt the overall three-dimensional structure, but leads to minor local differences at the turn in which residue 84 is involved. Coupling constant and NOE measurements indicate that the helix-turn motif is still present, but differences in chemical shifts and amide-exchange rates reflect a small distortion. This is in keeping with observations that several other mutant forms of transthyretin display similar subunit interactions and those that have been structurally analysed possess a near native structure. We propose that the Ser84 mutation induces only subtle perturbations to the transthyretin structure which predisposes the protein to amyloid formation. | lld:pubmed |
| pubmed-article:10336646 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10336646 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10336646 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10336646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10336646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10336646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10336646 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10336646 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10336646 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10336646 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:10336646 | pubmed:author | pubmed-author:WebbG DGD | lld:pubmed |
| pubmed-article:10336646 | pubmed:author | pubmed-author:SalvatoreDD | lld:pubmed |
| pubmed-article:10336646 | pubmed:author | pubmed-author:CraigD FDF | lld:pubmed |
| pubmed-article:10336646 | pubmed:author | pubmed-author:WilceJ AJA | lld:pubmed |
| pubmed-article:10336646 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10336646 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:10336646 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10336646 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10336646 | pubmed:pagination | 586-94 | lld:pubmed |
| pubmed-article:10336646 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:meshHeading | pubmed-meshheading:10336646... | lld:pubmed |
| pubmed-article:10336646 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10336646 | pubmed:articleTitle | 1H-NMR structural studies of a cystine-linked peptide containing residues 71-93 of transthyretin and effects of a Ser84 substitution implicated in familial amyloidotic polyneuropathy. | lld:pubmed |
| pubmed-article:10336646 | pubmed:affiliation | Department of Chemistry/Biochemistry, University of Western Australia, Nedlands, Australia. | lld:pubmed |
| pubmed-article:10336646 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10336646 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10336646 | lld:pubmed |
