| pubmed-article:2677606 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C0074447 | lld:lifeskim |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:2677606 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:2677606 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:2677606 | pubmed:dateCreated | 1989-11-17 | lld:pubmed |
| pubmed-article:2677606 | pubmed:abstractText | Shiga toxin is a protein toxin produced by Shigella dysenteriae type I strains. In this report we present a procedure for the separation of functionally intact toxin A and B chains and for their reconstitution to form biologically active molecules. In agreement with the findings of others, the isolated A chain was shown to be a potent in vitro inhibitor of eukaryotic protein synthesis. The isolated B chain bound to HeLa cells and competitively inhibited the binding and cytotoxic activity of holotoxin. These findings show that the functional role of the B chain is to recognize cell surface functional receptors. By labelling the B subunit alone, prior to renaturation of holotoxin, the polypeptide chains were shown to associate noncovalently with a stoichiometry of one A chain and five B chains. | lld:pubmed |
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| pubmed-article:2677606 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2677606 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2677606 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2677606 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2677606 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2677606 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2677606 | pubmed:issn | 0950-382X | lld:pubmed |
| pubmed-article:2677606 | pubmed:author | pubmed-author:KeuschG TGT | lld:pubmed |
| pubmed-article:2677606 | pubmed:author | pubmed-author:JacewiczMM | lld:pubmed |
| pubmed-article:2677606 | pubmed:author | pubmed-author:Donohue-Rolfe... | lld:pubmed |
| pubmed-article:2677606 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2677606 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:2677606 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2677606 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2677606 | pubmed:pagination | 1231-6 | lld:pubmed |
| pubmed-article:2677606 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2677606 | pubmed:meshHeading | pubmed-meshheading:2677606-... | lld:pubmed |
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| pubmed-article:2677606 | pubmed:meshHeading | pubmed-meshheading:2677606-... | lld:pubmed |
| pubmed-article:2677606 | pubmed:meshHeading | pubmed-meshheading:2677606-... | lld:pubmed |
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| pubmed-article:2677606 | pubmed:meshHeading | pubmed-meshheading:2677606-... | lld:pubmed |
| pubmed-article:2677606 | pubmed:meshHeading | pubmed-meshheading:2677606-... | lld:pubmed |
| pubmed-article:2677606 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2677606 | pubmed:articleTitle | Isolation and characterization of functional Shiga toxin subunits and renatured holotoxin. | lld:pubmed |
| pubmed-article:2677606 | pubmed:affiliation | Department of Medicine, New England Medical Center, Boston, Massachusetts. | lld:pubmed |
| pubmed-article:2677606 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2677606 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2677606 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:2677606 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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