| pubmed-article:1551483 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1551483 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:1551483 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:1551483 | lifeskim:mentions | umls-concept:C0679823 | lld:lifeskim |
| pubmed-article:1551483 | lifeskim:mentions | umls-concept:C1160520 | lld:lifeskim |
| pubmed-article:1551483 | lifeskim:mentions | umls-concept:C0038185 | lld:lifeskim |
| pubmed-article:1551483 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1551483 | pubmed:dateCreated | 1992-4-27 | lld:pubmed |
| pubmed-article:1551483 | pubmed:abstractText | A protease involved in oocyte maturation of a starfish, Asterina pectinifera, was explored. Trypsin-like and chymotrypsin-like activities of the 650-kDa protease in oocyte extract were revealed to increase more than twice under the influence of 1-methyladenine before germinal vesicle breakdown (GVBD) during maturation. The inhibitory potencies of leupeptin and its five analogs against the chymotrypsin-like activity, but not the trypsin-like activity, of this protease was well in accord with those against GVBD (Takagi Sawada et al. (1989). Dev. Biol. 133, 609-612). These results indicate that the chymotrypsin-like activity of the 650-kDa protease (most probably 20 S proteasome) plays a key role in starfish oocyte maturation. | lld:pubmed |
| pubmed-article:1551483 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1551483 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1551483 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1551483 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1551483 | pubmed:issn | 0012-1606 | lld:pubmed |
| pubmed-article:1551483 | pubmed:author | pubmed-author:SawadaHH | lld:pubmed |
| pubmed-article:1551483 | pubmed:author | pubmed-author:HoshiMM | lld:pubmed |
| pubmed-article:1551483 | pubmed:author | pubmed-author:SomenoTT | lld:pubmed |
| pubmed-article:1551483 | pubmed:author | pubmed-author:SawadaM TMT | lld:pubmed |
| pubmed-article:1551483 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1551483 | pubmed:volume | 150 | lld:pubmed |
| pubmed-article:1551483 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1551483 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1551483 | pubmed:pagination | 414-8 | lld:pubmed |
| pubmed-article:1551483 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:meshHeading | pubmed-meshheading:1551483-... | lld:pubmed |
| pubmed-article:1551483 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1551483 | pubmed:articleTitle | Participation of 650-kDa protease (20 S proteasome) in starfish oocyte maturation. | lld:pubmed |
| pubmed-article:1551483 | pubmed:affiliation | Department of Life Science, Faculty of Science, Tokyo Institute of Technology, Japan. | lld:pubmed |
| pubmed-article:1551483 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1551483 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1551483 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1551483 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1551483 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1551483 | lld:pubmed |
