| pubmed-article:3461464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0043167 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0087111 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0041236 | lld:lifeskim |
| pubmed-article:3461464 | lifeskim:mentions | umls-concept:C0040018 | lld:lifeskim |
| pubmed-article:3461464 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:3461464 | pubmed:dateCreated | 1986-9-25 | lld:pubmed |
| pubmed-article:3461464 | pubmed:abstractText | Permeabilization of human platelets with saponin (15-25 micrograms/ml) allows the determination of the ADP-ribosylation of a 41-kDa protein by pertussis toxin. The ADP-ribosylated protein is present in the particulate fraction. ADP-ribosylation of the 41-kDa protein increases for 20 min; it is not affected by indomethacin, prostacyclin, and 1,2-diacylglycerols but is inhibited by 1 mM Ca2+ and phorbol esters. Treatment of platelets with trypsin, thrombin, or collagen before saponin addition precludes subsequent pertussis toxin-induced ADP-ribosylation of the 41-kDa protein. The effect of trypsin or thrombin is blocked by soybean trypsin inhibitor and leupeptin. Trypsin proteolytically cleaves the ADP-ribosylated 41-kDa protein to an ADP-ribosylated fragment slightly smaller than 20 kDa. The results suggest that a modification of a guanine nucleotide-binding regulatory protein is associated with the actions of trypsin, thrombin, and collagen on platelet activation. | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3461464 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3461464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3461464 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3461464 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3461464 | pubmed:author | pubmed-author:ChangK JKJ | lld:pubmed |
| pubmed-article:3461464 | pubmed:author | pubmed-author:LapetinaE GEG | lld:pubmed |
| pubmed-article:3461464 | pubmed:author | pubmed-author:ReepBB | lld:pubmed |
| pubmed-article:3461464 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3461464 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:3461464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3461464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3461464 | pubmed:pagination | 5880-3 | lld:pubmed |
| pubmed-article:3461464 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:meshHeading | pubmed-meshheading:3461464-... | lld:pubmed |
| pubmed-article:3461464 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3461464 | pubmed:articleTitle | Treatment of human platelets with trypsin, thrombin, or collagen inhibits the pertussis toxin-induced ADP-ribosylation of a 41-kDa protein. | lld:pubmed |
| pubmed-article:3461464 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3461464 | lld:pubmed |
