pubmed-article:2332434 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2332434 | lifeskim:mentions | umls-concept:C0025914 | lld:lifeskim |
pubmed-article:2332434 | lifeskim:mentions | umls-concept:C0026809 | lld:lifeskim |
pubmed-article:2332434 | lifeskim:mentions | umls-concept:C1416788 | lld:lifeskim |
pubmed-article:2332434 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:2332434 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:2332434 | pubmed:dateCreated | 1990-6-4 | lld:pubmed |
pubmed-article:2332434 | pubmed:abstractText | The disulfide structure of mouse lysosome-associated membrane protein 1 has been determined by reverse-phase isolation and sequence analysis of the cysteine-containing tryptic fragments of the reduced and non-reduced deglycosylated protein. Half-cystines were distinguished (a) by their localization within tryptic or chymotryptic peptides that formed reverse-phase peaks unique to the reduced digests and (b) by their 3H-carboxymethylation only after reduction of the protein. The disulfide arrangement of the cysteines was assigned after isolation of disulfide-linked peptide pairs. Each pair chromatographed as a peak present in the nonreduced (but not the corresponding reduced) tryptic digest. NH2-terminal sequencing as well as reduction, alkylation, and rechromatography of the disulfide-linked fragments led to the following assignment of disulfide bonds: Cys11 and Cys50, Cys125 and Cys161, Cys198 and Cys235, and Cys303 and Cys340. This structure creates four 36-38-residue loops that are symmetrically placed within the two halves of the protein's intraluminal domain. The loops formed by the Cys11-Cys50 and Cys198-Cys235 bridges are homologous, and the Cys125-Cys161 and Cys303-cys340 loops form a second set of homologous domains. The conservation of cysteine residues among lysosome-associated membrane proteins 1 and 2 suggests that this disulfide arrangement is common to both members of this family of lysosomal membrane glycoproteins. | lld:pubmed |
pubmed-article:2332434 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:language | eng | lld:pubmed |
pubmed-article:2332434 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2332434 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2332434 | pubmed:month | May | lld:pubmed |
pubmed-article:2332434 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:2332434 | pubmed:author | pubmed-author:AugustJ TJT | lld:pubmed |
pubmed-article:2332434 | pubmed:author | pubmed-author:EarlesB JBJ | lld:pubmed |
pubmed-article:2332434 | pubmed:author | pubmed-author:ArterburnL... | lld:pubmed |
pubmed-article:2332434 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2332434 | pubmed:day | 5 | lld:pubmed |
pubmed-article:2332434 | pubmed:volume | 265 | lld:pubmed |
pubmed-article:2332434 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2332434 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2332434 | pubmed:pagination | 7419-23 | lld:pubmed |
pubmed-article:2332434 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2332434 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2332434 | pubmed:articleTitle | The disulfide structure of mouse lysosome-associated membrane protein 1. | lld:pubmed |
pubmed-article:2332434 | pubmed:affiliation | Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205. | lld:pubmed |
pubmed-article:2332434 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2332434 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2332434 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
entrez-gene:16783 | entrezgene:pubmed | pubmed-article:2332434 | lld:entrezgene |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2332434 | lld:pubmed |