| pubmed-article:2223080 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C0029974 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C0037850 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C0008807 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C1705944 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C1522408 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C0109710 | lld:lifeskim |
| pubmed-article:2223080 | lifeskim:mentions | umls-concept:C0453946 | lld:lifeskim |
| pubmed-article:2223080 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:2223080 | pubmed:dateCreated | 1990-12-10 | lld:pubmed |
| pubmed-article:2223080 | pubmed:abstractText | In Ciona intestinalis, sperm penetration through the egg vitelline coat is an essential event of fertilization. We investigated whether trypsin- and chymotrypsin-like enzymes are involved in this event. Inhibitors and peptide substrates for chymotrypsin-like enzymes blocked the overall process of fertilization in a concentration-dependent manner. The inhibitory activity was specifically exerted on the step of sperm penetration. Chymotrypsin-like protease activity was identified in spermatozoa with the fluorogenic synthetic substrate Suc-Ala-Ala-Phe-AMC, which was the most effective substrate in blocking sperm penetration. These data indicate that a chymotrypsin-like protease activity is a sperm lysin of Ciona intestinalis. | lld:pubmed |
| pubmed-article:2223080 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2223080 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2223080 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2223080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2223080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2223080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2223080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2223080 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2223080 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:2223080 | pubmed:issn | 1040-452X | lld:pubmed |
| pubmed-article:2223080 | pubmed:author | pubmed-author:MarinoRR | lld:pubmed |
| pubmed-article:2223080 | pubmed:author | pubmed-author:HoshiMM | lld:pubmed |
| pubmed-article:2223080 | pubmed:author | pubmed-author:AmorosoAA | lld:pubmed |
| pubmed-article:2223080 | pubmed:author | pubmed-author:De SantisRR | lld:pubmed |
| pubmed-article:2223080 | pubmed:author | pubmed-author:PintoM RMR | lld:pubmed |
| pubmed-article:2223080 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2223080 | pubmed:volume | 26 | lld:pubmed |
| pubmed-article:2223080 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2223080 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2223080 | pubmed:pagination | 319-23 | lld:pubmed |
| pubmed-article:2223080 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:meshHeading | pubmed-meshheading:2223080-... | lld:pubmed |
| pubmed-article:2223080 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2223080 | pubmed:articleTitle | Chymotrypsin-like enzymes are involved in sperm penetration through the vitelline coat of Ciona intestinalis egg. | lld:pubmed |
| pubmed-article:2223080 | pubmed:affiliation | Institute of Protein Biochemistry and Enzymology, CNR, Napoli, Italy. | lld:pubmed |
| pubmed-article:2223080 | pubmed:publicationType | Journal Article | lld:pubmed |
