pubmed-article:17170131 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C2348042 | lld:lifeskim |
pubmed-article:17170131 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:17170131 | pubmed:issue | 52 | lld:pubmed |
pubmed-article:17170131 | pubmed:dateCreated | 2006-12-27 | lld:pubmed |
pubmed-article:17170131 | pubmed:abstractText | The [PSI(+)] prion of Saccharomyces cerevisiae is a self-propagating amyloid form of Sup35p, a subunit of the translation termination factor. Using solid-state NMR we have examined the structure of amyloid fibrils formed in vitro from purified recombinant Sup35(1-253), consisting of the glutamine- and asparagine-rich N-terminal 123-residue prion domain (N) and the adjacent 130-residue highly charged M domain. Measurements of magnetic dipole-dipole couplings among (13)C nuclei in a series of Sup35NM fibril samples, (13)C-labeled at backbone carbonyl sites of Tyr, Leu, or Phe residues or at side-chain methyl sites of Ala residues, indicate intermolecular (13)C-(13)C distances of approximately 0.5 nm for nearly all sites in the N domain. Certain sites in the M domain also exhibit intermolecular distances of approximately 0.5 nm. These results indicate that an in-register parallel beta-sheet structure underlies the [PSI(+)] prion phenomenon. | lld:pubmed |
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pubmed-article:17170131 | pubmed:language | eng | lld:pubmed |
pubmed-article:17170131 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17170131 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17170131 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17170131 | pubmed:month | Dec | lld:pubmed |
pubmed-article:17170131 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:17170131 | pubmed:author | pubmed-author:WicknerReed... | lld:pubmed |
pubmed-article:17170131 | pubmed:author | pubmed-author:TyckoRobertR | lld:pubmed |
pubmed-article:17170131 | pubmed:author | pubmed-author:ShewmakerFran... | lld:pubmed |
pubmed-article:17170131 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17170131 | pubmed:day | 26 | lld:pubmed |
pubmed-article:17170131 | pubmed:volume | 103 | lld:pubmed |
pubmed-article:17170131 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17170131 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17170131 | pubmed:pagination | 19754-9 | lld:pubmed |
pubmed-article:17170131 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:17170131 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:17170131 | pubmed:articleTitle | Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. | lld:pubmed |
pubmed-article:17170131 | pubmed:affiliation | Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |