pubmed-article:3214435 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C0028959 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
pubmed-article:3214435 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:3214435 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:3214435 | pubmed:dateCreated | 1989-2-13 | lld:pubmed |
pubmed-article:3214435 | pubmed:abstractText | The effects of alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene (MMNT) on mannosidases involved in asparagine-linked oligosaccharide processing were investigated. MMNT was found to inhibit the activity of rat liver Golgi alpha-mannosidase I in a concentration-dependent manner (50% inhibition with 0.18 mM-MMNT), whereas rat liver endoplasmic-reticulum alpha-mannosidase appeared to be resistant (less than 5% inhibition at 1 mM-MMNT). Jack-bean alpha-mannosidase was also sensitive to inhibition by MMNT (50% inhibition with 0.32 mM-MMNT). Treatment of influenza-virus-infected chick-embryo cells with 1 mM-MMNT led to a decrease in the formation of complex-type asparagine-linked oligosaccharides and an accumulation of high-mannose-type oligosaccharides with the composition Man8(GlcNAc)2 and Man7(GlcNAc)2 on the viral glycoproteins. The biological activities of influenza-virus haemagglutinin and neuraminidase synthesized in the presence of 1 mM-MMNT remained unchanged, but the virus was less infectious than the control. | lld:pubmed |
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pubmed-article:3214435 | pubmed:language | eng | lld:pubmed |
pubmed-article:3214435 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3214435 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3214435 | pubmed:month | Nov | lld:pubmed |
pubmed-article:3214435 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:RottRR | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:SchwarzR TRT | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:MeyersR WRW | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:BeMillerJ NJN | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:McDowellWW | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:TlustyAA | lld:pubmed |
pubmed-article:3214435 | pubmed:author | pubmed-author:BohnJ AJA | lld:pubmed |
pubmed-article:3214435 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3214435 | pubmed:day | 1 | lld:pubmed |
pubmed-article:3214435 | pubmed:volume | 255 | lld:pubmed |
pubmed-article:3214435 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3214435 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3214435 | pubmed:pagination | 991-8 | lld:pubmed |
pubmed-article:3214435 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:3214435 | pubmed:year | 1988 | lld:pubmed |
pubmed-article:3214435 | pubmed:articleTitle | Inhibition of glycoprotein oligosaccharide processing in vitro and in influenza-virus-infected cells by alpha-D-mannopyranosylmethyl-p-nitrophenyltriazene. | lld:pubmed |
pubmed-article:3214435 | pubmed:affiliation | Institut für Virològie, Justus Liebig Universität Giessen, Federal Republic of Germany. | lld:pubmed |
pubmed-article:3214435 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3214435 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |