| pubmed-article:17277449 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17277449 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:17277449 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:17277449 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:17277449 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:17277449 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:17277449 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:17277449 | pubmed:dateCreated | 2007-2-5 | lld:pubmed |
| pubmed-article:17277449 | pubmed:abstractText | The reversible modification of Atg8 with phosphatidylethanolamine (PE) is crucial for autophagy, the bulk degradation process of cytoplasmic components by the vacuolar/lysosomal system. Atg4 is a cysteine protease that is responsible for the processing and deconjugation of Atg8. Human Atg4B (HsAtg4B; a mammalian orthologue of yeast Atg4) and LC3 (a mammalian orthologue of yeast Atg8) were expressed and purified and two complexes, one consisting of HsAtg4B(1-354) and LC3(1-120) (complex I; the product complex) and the other consisting of HsAtg4B(1-354) and LC3(1-124) (complex II; the substrate complex), were crystallized using polyethylene glycol 3350 as a precipitant. In both complexes His280 of HsAtg4B was mutated to alanine. The crystals belong to the same space group P2(1)2(1)2(1), with unit-cell parameters a = 47.5, b = 91.8, c = 102.6 A for complex I and a = 46.9, b = 90.9, c = 102.5 A for complex II. Diffraction data were collected to a resolution of 1.9 A from both crystals. | lld:pubmed |
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| pubmed-article:17277449 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17277449 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17277449 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17277449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17277449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17277449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17277449 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17277449 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17277449 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17277449 | pubmed:issn | 1744-3091 | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:InagakiFuyuhi... | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:MizushimaNobo... | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:OhsumiYoshino... | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:SuzukiNobuo... | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:FujiokaYukoY | lld:pubmed |
| pubmed-article:17277449 | pubmed:author | pubmed-author:SatooKenjiK | lld:pubmed |
| pubmed-article:17277449 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:17277449 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17277449 | pubmed:volume | 63 | lld:pubmed |
| pubmed-article:17277449 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17277449 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17277449 | pubmed:pagination | 99-102 | lld:pubmed |
| pubmed-article:17277449 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17277449 | pubmed:meshHeading | pubmed-meshheading:17277449... | lld:pubmed |
| pubmed-article:17277449 | pubmed:meshHeading | pubmed-meshheading:17277449... | lld:pubmed |
| pubmed-article:17277449 | pubmed:meshHeading | pubmed-meshheading:17277449... | lld:pubmed |
| pubmed-article:17277449 | pubmed:meshHeading | pubmed-meshheading:17277449... | lld:pubmed |
| pubmed-article:17277449 | pubmed:meshHeading | pubmed-meshheading:17277449... | lld:pubmed |
| pubmed-article:17277449 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17277449 | pubmed:articleTitle | Crystallization and preliminary crystallographic analysis of human Atg4B-LC3 complex. | lld:pubmed |
| pubmed-article:17277449 | pubmed:affiliation | Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, N-12, W-6, Kita-ku, Sapporo 060-0812, Japan. | lld:pubmed |
| pubmed-article:17277449 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17277449 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
