| pubmed-article:3031084 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0230770 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0009013 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0006556 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0204727 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0079941 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0140512 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0441587 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:3031084 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:3031084 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:3031084 | pubmed:dateCreated | 1987-5-8 | lld:pubmed |
| pubmed-article:3031084 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3031084 | pubmed:abstractText | Ribophorins I and II are two transmembrane glycoproteins that are characteristic of the rough endoplasmic reticulum and are thought to be part of the apparatus that affects the co-translational translocation of polypeptides synthesized on membrane-bound polysomes. A ribophorin I cDNA clone containing a 0.6-kb insert was isolated from a rat liver lambda gtll cDNA library by immunoscreening with specific antibodies. This cDNA was used to isolate a clone (2.3 kb) from a rat brain lambda gtll cDNA library that contains the entire ribophorin I coding sequence. SP6 RNA transcripts of the insert in this clone directed the in vitro synthesis of a polypeptide of the expected size that was immunoprecipitated with anti-ribophorin I antibodies. When synthesized in the presence of microsomes, this polypeptide, like the translation product of the natural ribophorin I mRNA, underwent membrane insertion, signal cleavage, and co-translational glycosylation. The complete amino acid sequence of the polypeptide encoded in the cDNA insert was derived from the nucleotide sequence and found to contain a segment that corresponds to a partial amino terminal sequence of ribophorin I that was obtained by Edman degradation. This confirmed the identity of the cDNA clone and established that ribophorin I contains 583 amino acids and is synthesized with a cleavable amino terminal insertion signal of 22 residues. Analysis of the amino acid sequence of ribophorin I suggested that the polypeptide has a simple transmembrane disposition with a rather hydrophilic carboxy terminal segment of 150 amino acids exposed on the cytoplasmic face of the membrane, and a luminal domain of 414 amino acids containing three potential N-glycosylation sites. Hybridization measurements using the cloned cDNA as a probe showed that ribophorin I mRNA levels increase fourfold 15 h after partial hepatectomy, in confirmation of measurements made by in vitro translation of liver mRNA. Southern blot analysis of rat genomic DNA suggests that there is a single copy of the ribophorin I gene in the haploid rat genome. | lld:pubmed |
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| pubmed-article:3031084 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3031084 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3031084 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3031084 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3031084 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3031084 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:3031084 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:RosenfeldM... | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:ColmanD RDR | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:MarcantonioEE | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:SabatiniD DDD | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:PrakashKK | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:KreibichGG | lld:pubmed |
| pubmed-article:3031084 | pubmed:author | pubmed-author:AdesnikMM | lld:pubmed |
