| pubmed-article:5123421 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:5123421 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
| pubmed-article:5123421 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:5123421 | lifeskim:mentions | umls-concept:C0004965 | lld:lifeskim |
| pubmed-article:5123421 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:5123421 | lifeskim:mentions | umls-concept:C1706214 | lld:lifeskim |
| pubmed-article:5123421 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:5123421 | pubmed:dateCreated | 1972-2-2 | lld:pubmed |
| pubmed-article:5123421 | pubmed:abstractText | "Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, beta-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain and share the physical properties of amyloid fibrils. The relation between amyloidosis and immunoglobulins is thus more firmly established and a pathogenetic mechanism for amyloid fibril formation is suggested. | lld:pubmed |
| pubmed-article:5123421 | pubmed:language | eng | lld:pubmed |
| pubmed-article:5123421 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:5123421 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:5123421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:5123421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:5123421 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:5123421 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:5123421 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:5123421 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:EanesE DED | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:GlennerG GGG | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:PageD LDL | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:EinDD | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:TerryWW | lld:pubmed |
| pubmed-article:5123421 | pubmed:author | pubmed-author:BladenH AHA | lld:pubmed |
| pubmed-article:5123421 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:5123421 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:5123421 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:5123421 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:5123421 | pubmed:pagination | 712-4 | lld:pubmed |
| pubmed-article:5123421 | pubmed:dateRevised | 2009-10-27 | lld:pubmed |
| pubmed-article:5123421 | pubmed:meshHeading | pubmed-meshheading:5123421-... | lld:pubmed |
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| pubmed-article:5123421 | pubmed:meshHeading | pubmed-meshheading:5123421-... | lld:pubmed |
| pubmed-article:5123421 | pubmed:year | 1971 | lld:pubmed |
| pubmed-article:5123421 | pubmed:articleTitle | Creation of "amyloid" fibrils from Bence Jones proteins in vitro. | lld:pubmed |
| pubmed-article:5123421 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:5123421 | pubmed:publicationType | In Vitro | lld:pubmed |
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