pubmed-article:11256612 | rdf:type | pubmed:Citation | lld:pubmed |
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pubmed-article:11256612 | lifeskim:mentions | umls-concept:C0332298 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C0180860 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C0581406 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C1522664 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C1550638 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:11256612 | lifeskim:mentions | umls-concept:C0069437 | lld:lifeskim |
pubmed-article:11256612 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:11256612 | pubmed:dateCreated | 2001-3-20 | lld:pubmed |
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pubmed-article:11256612 | pubmed:abstractText | Proteases have a variety of strategies for selecting substrates in order to prevent uncontrolled protein degradation. A recent crystal structure determination of prolyl oligopeptidase has suggested a way for substrate selection involving an unclosed seven-bladed beta-propeller domain. We have engineered a disulfide bond between the first and seventh blades of the propeller, which resulted in the loss of enzymatic activity. These results provided direct evidence for a novel strategy of regulation in which oscillating propeller blades act as a gating filter during catalysis, letting small peptide substrates into the active site while excluding large proteins to prevent accidental proteolysis. | lld:pubmed |
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pubmed-article:11256612 | pubmed:language | eng | lld:pubmed |
pubmed-article:11256612 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:11256612 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:11256612 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:11256612 | pubmed:month | Sep | lld:pubmed |
pubmed-article:11256612 | pubmed:issn | 1469-221X | lld:pubmed |
pubmed-article:11256612 | pubmed:author | pubmed-author:PolgárLL | lld:pubmed |
pubmed-article:11256612 | pubmed:author | pubmed-author:FülöpVV | lld:pubmed |
pubmed-article:11256612 | pubmed:author | pubmed-author:SzeltnerZZ | lld:pubmed |
pubmed-article:11256612 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:11256612 | pubmed:volume | 1 | lld:pubmed |
pubmed-article:11256612 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:11256612 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:11256612 | pubmed:pagination | 277-81 | lld:pubmed |
pubmed-article:11256612 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:11256612 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:11256612 | pubmed:articleTitle | Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. | lld:pubmed |
pubmed-article:11256612 | pubmed:affiliation | Department of Biological Sciences, University of Warwick, Coventry, UK. | lld:pubmed |
pubmed-article:11256612 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:11256612 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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