| pubmed-article:17517891 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C2717969 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1137683 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17517891 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:17517891 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:17517891 | pubmed:dateCreated | 2007-7-9 | lld:pubmed |
| pubmed-article:17517891 | pubmed:abstractText | Intramembrane proteolysis is now firmly established as a prominent biological process, and structure elucidation is emerging as the new frontier in the understanding of these novel membrane-embedded enzymes. Reproducing this unusual hydrolysis within otherwise water-excluding transmembrane regions with purified proteins is a challenging prerequisite for such structural studies. Here we show the bacterial expression, purification, and reconstitution of proteolytically active signal peptide peptidase (SPP), a membrane-embedded enzyme in the presenilin family of aspartyl proteases. This finding formally proves that, unlike presenilin, SPP does not require any additional proteins for proteolysis. Surprisingly, the conserved C-terminal half of SPP is sufficient for proteolytic activity; purification and reconstitution of this engineered fragment of several SPP orthologues revealed that this region defines a functional domain for an intramembrane aspartyl protease. The discovery of minimal requirements for intramembrane proteolysis should facilitate mechanistic and structural analysis and help define general biochemical principles of hydrolysis in a hydrophobic environment. | lld:pubmed |
| pubmed-article:17517891 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17517891 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17517891 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17517891 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17517891 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:17517891 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17517891 | pubmed:author | pubmed-author:WolfeMichael... | lld:pubmed |
| pubmed-article:17517891 | pubmed:author | pubmed-author:SatoToruT | lld:pubmed |
| pubmed-article:17517891 | pubmed:author | pubmed-author:NarayananSara... | lld:pubmed |
| pubmed-article:17517891 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17517891 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:17517891 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17517891 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17517891 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17517891 | pubmed:pagination | 20172-9 | lld:pubmed |
| pubmed-article:17517891 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:meshHeading | pubmed-meshheading:17517891... | lld:pubmed |
| pubmed-article:17517891 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17517891 | pubmed:articleTitle | A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis. | lld:pubmed |
| pubmed-article:17517891 | pubmed:affiliation | Center for Neurologic Diseases, Brigham and Women's Hospital and Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:17517891 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17517891 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17517891 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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