pubmed-article:16005683 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16005683 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
pubmed-article:16005683 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
pubmed-article:16005683 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
pubmed-article:16005683 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:16005683 | pubmed:dateCreated | 2005-8-8 | lld:pubmed |
pubmed-article:16005683 | pubmed:abstractText | Folding in the endoplasmic reticulum (ER) must couple protein-synthesis pathways operating outside of the compartment with ER-assisted folding (ERAF) pathways in the lumen. Chaperone-mediated folding imbalances that are associated with numerous misfolding diseases, including diabetes, trigger the unfolded-protein response (UPR), using both transcriptional and translational pathways to correct the problem. Recent work suggests that small-molecule inhibitors could be useful to help rebalance protein synthesis with ERAF pathways through the ribosomal initiating factor eIF2alpha. Reprogramming stress pathways with drugs provides a potential new approach for balancing ER-protein load with cellular-folding capacity, thus correcting disease. | lld:pubmed |
pubmed-article:16005683 | pubmed:language | eng | lld:pubmed |
pubmed-article:16005683 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16005683 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16005683 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16005683 | pubmed:month | Aug | lld:pubmed |
pubmed-article:16005683 | pubmed:issn | 1471-4914 | lld:pubmed |
pubmed-article:16005683 | pubmed:author | pubmed-author:BalchWilliam... | lld:pubmed |
pubmed-article:16005683 | pubmed:author | pubmed-author:WisemanR... | lld:pubmed |
pubmed-article:16005683 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16005683 | pubmed:volume | 11 | lld:pubmed |
pubmed-article:16005683 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16005683 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16005683 | pubmed:pagination | 347-50 | lld:pubmed |
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pubmed-article:16005683 | pubmed:meshHeading | pubmed-meshheading:16005683... | lld:pubmed |
pubmed-article:16005683 | pubmed:year | 2005 | lld:pubmed |
pubmed-article:16005683 | pubmed:articleTitle | A new pharmacology--drugging stressed folding pathways. | lld:pubmed |
pubmed-article:16005683 | pubmed:affiliation | Department of Chemistry and The Skaggs Institute of Chemical Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd, MB-6, La Jolla, CA 92037, USA. | lld:pubmed |
pubmed-article:16005683 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16005683 | pubmed:publicationType | Review | lld:pubmed |
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