| pubmed-article:1834945 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1834945 | lifeskim:mentions | umls-concept:C0063423 | lld:lifeskim |
| pubmed-article:1834945 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:1834945 | pubmed:issue | 6346 | lld:pubmed |
| pubmed-article:1834945 | pubmed:dateCreated | 1991-11-29 | lld:pubmed |
| pubmed-article:1834945 | pubmed:abstractText | Members of the heat-shock protein family (hsp70s) can distinguish folded from unfolded proteins. This property is crucial to the role of hsp70s as molecular chaperones and is attributable to the amino-acid specificity of the peptide-binding site. The specificity for peptide ligands is investigated using a set of peptides of random sequence but defined chain length. The peptide-binding site selects for aliphatic residues and accommodates them in an environment energetically equivalent to the interior of a folded protein. | lld:pubmed |
| pubmed-article:1834945 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1834945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1834945 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1834945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1834945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1834945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1834945 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1834945 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1834945 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:1834945 | pubmed:author | pubmed-author:PohlJJ | lld:pubmed |
| pubmed-article:1834945 | pubmed:author | pubmed-author:RothmanJ EJE | lld:pubmed |
| pubmed-article:1834945 | pubmed:author | pubmed-author:FlynnG CGC | lld:pubmed |
| pubmed-article:1834945 | pubmed:author | pubmed-author:FloccoM TMT | lld:pubmed |
| pubmed-article:1834945 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1834945 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:1834945 | pubmed:volume | 353 | lld:pubmed |
| pubmed-article:1834945 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1834945 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1834945 | pubmed:pagination | 726-30 | lld:pubmed |
| pubmed-article:1834945 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:1834945 | pubmed:meshHeading | pubmed-meshheading:1834945-... | lld:pubmed |
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| pubmed-article:1834945 | pubmed:meshHeading | pubmed-meshheading:1834945-... | lld:pubmed |
| pubmed-article:1834945 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1834945 | pubmed:articleTitle | Peptide-binding specificity of the molecular chaperone BiP. | lld:pubmed |
| pubmed-article:1834945 | pubmed:affiliation | Program in Cellular Biochemistry and Biophysics, Rockefeller Research Laboratory, Sloan-Kettering Institute, New York, New York 10021. | lld:pubmed |
| pubmed-article:1834945 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1834945 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1834945 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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