| pubmed-article:19767749 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19767749 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:19767749 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:19767749 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19767749 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:19767749 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:19767749 | pubmed:dateCreated | 2009-10-7 | lld:pubmed |
| pubmed-article:19767749 | pubmed:abstractText | Two fundamental questions with regard to proteolytic networks and pathways concern the structural repertoire and kinetic threshold that distinguish legitimate signaling substrates. We used N-terminal proteomics to address these issues by identifying cleavage sites within the Escherichia coli proteome that are driven by the apoptotic signaling protease caspase-3 and the bacterial protease glutamyl endopeptidase (GluC). Defying the dogma that proteases cleave primarily in natively unstructured loops, we found that both caspase-3 and GluC cleave in alpha-helices nearly as frequently as in extended loops. Notably, biochemical and kinetic characterization revealed that E. coli caspase-3 substrates are greatly inferior to natural substrates, suggesting protease and substrate coevolution. Engineering an E. coli substrate to match natural catalytic rates defined a kinetic threshold that depicts a signaling event. This unique combination of proteomics, biochemistry, kinetics and substrate engineering reveals new insights into the structure-function relationship of protease targets and their validation from large-scale approaches. | lld:pubmed |
| pubmed-article:19767749 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19767749 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19767749 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19767749 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19767749 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19767749 | pubmed:issn | 1545-9985 | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:SalvesenGuy... | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:ReganTimT | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:ZhuWenhongW | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:RiedlStefan... | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:PopCristinaC | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:SnipasScott... | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:EroshkinAlexe... | lld:pubmed |
| pubmed-article:19767749 | pubmed:author | pubmed-author:TimmerJohn... | lld:pubmed |
| pubmed-article:19767749 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19767749 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:19767749 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19767749 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19767749 | pubmed:pagination | 1101-8 | lld:pubmed |
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| pubmed-article:19767749 | pubmed:meshHeading | pubmed-meshheading:19767749... | lld:pubmed |
| pubmed-article:19767749 | pubmed:meshHeading | pubmed-meshheading:19767749... | lld:pubmed |
| pubmed-article:19767749 | pubmed:meshHeading | pubmed-meshheading:19767749... | lld:pubmed |
| pubmed-article:19767749 | pubmed:meshHeading | pubmed-meshheading:19767749... | lld:pubmed |
| pubmed-article:19767749 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19767749 | pubmed:articleTitle | Structural and kinetic determinants of protease substrates. | lld:pubmed |
| pubmed-article:19767749 | pubmed:affiliation | Apoptosis and Cell Death Research Program at the Burnham Institute for Medical Research, La Jolla, California, USA. | lld:pubmed |
| pubmed-article:19767749 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19767749 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19767749 | lld:pubmed |
