| pubmed-article:1344885 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0004896 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0024660 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0014239 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0041385 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C2350324 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:1344885 | lifeskim:mentions | umls-concept:C0061421 | lld:lifeskim |
| pubmed-article:1344885 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:1344885 | pubmed:dateCreated | 1994-6-1 | lld:pubmed |
| pubmed-article:1344885 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1344885 | pubmed:abstractText | Treatment of developing bean cotyledons with the inhibitor of N-glycosylation tunicamycin enhanced the synthesis of at least two polypeptides with molecular mass 78 kDa and 97 kDa. Pulse-chase experiments and subcellular fractionation indicated that these are endoplasmic reticulum (ER) residents. The 78 kDa protein is a major component of the ER protein fraction and, by N-terminal sequencing, was identified as a bean homolog of the mammalian 78 kDa glucose-regulated protein (GRP78). This is a molecular chaperone that is probably involved in the folding and oligomerization of several animal and yeast proteins in the ER. When newly synthesized storage glycoproteins phaseolin, phytohemagglutinin or alpha-amylase inhibitor were immunoprecipitated from an ER preparation of tunicamycin-treated tissue, the GRP78 homolog was always co-precipitated. Bound GRP78 homolog could be released by ATP treatment. These results suggest that, at least when glycosylation is inhibited, this protein plays a role in the early stages of the synthesis of vacuolar storage proteins. | lld:pubmed |
| pubmed-article:1344885 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1344885 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1344885 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1344885 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1344885 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1344885 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1344885 | pubmed:issn | 0960-7412 | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:VitaleAA | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:D'AmicoLL | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:BolliniRR | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:NittiGG | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:CeriottiAA | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:FabbriniM SMS | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:ValsasinaBB | lld:pubmed |
| pubmed-article:1344885 | pubmed:author | pubmed-author:DaminatiM GMG | lld:pubmed |
| pubmed-article:1344885 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1344885 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:1344885 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1344885 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1344885 | pubmed:pagination | 443-55 | lld:pubmed |
| pubmed-article:1344885 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:1344885 | pubmed:meshHeading | pubmed-meshheading:1344885-... | lld:pubmed |
| pubmed-article:1344885 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1344885 | pubmed:articleTitle | Bean homologs of the mammalian glucose-regulated proteins: induction by tunicamycin and interaction with newly synthesized seed storage proteins in the endoplasmic reticulum. | lld:pubmed |
| pubmed-article:1344885 | pubmed:affiliation | Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, Milano, Italy. | lld:pubmed |
| pubmed-article:1344885 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1344885 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1344885 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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