| pubmed-article:1577725 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1577725 | lifeskim:mentions | umls-concept:C0106132 | lld:lifeskim |
| pubmed-article:1577725 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
| pubmed-article:1577725 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
| pubmed-article:1577725 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
| pubmed-article:1577725 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:1577725 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:1577725 | pubmed:dateCreated | 1992-6-5 | lld:pubmed |
| pubmed-article:1577725 | pubmed:abstractText | Few experimental models have been used to investigate how proteins fold inside a cell. Using the formation of disulfide bonds as an index of conformational changes during protein folding, we have developed a unique system to determine the intracellular folding pathway of the beta subunit of human chorionic gonadotropin (hCG). Three folding intermediates of the beta subunit were purified from [35S]cysteine-labeled JAR choriocarcinoma cells by immunoprecipitation and by reverse-phase high performance liquid chromatography (HPLC). To identify unformed disulfide bonds, nonreduced folding intermediates were treated with trypsin to liberate non-disulfide-bound, [35S]cysteine-containing peptides from the disulfide-linked peptides. Released peptides were purified by HPLC and identified by amino acid sequencing. The amount of a peptide that was released indicated the extent of disulfide bond formation involving the cysteine in that peptide. Of the six disulfide bonds in hCG-beta, bonds 34-88 and 38-57 form first. The rate-limiting event of folding involves the formation of the S-S bonds between cysteines 23 and 72 and cysteines 9 and 90. Disulfide bond 93-100, the formation of which appears to be necessary for assembly with the alpha subunit of the hCG heterodimer, forms next. Finally, disulfide bond 26-110 forms after assembly with the alpha subunit, suggesting that completion of folding of the COOH terminus in the beta subunit occurs after assembly with the alpha subunit. | lld:pubmed |
| pubmed-article:1577725 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577725 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1577725 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577725 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1577725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577725 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577725 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1577725 | pubmed:month | May | lld:pubmed |
| pubmed-article:1577725 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1577725 | pubmed:author | pubmed-author:RuddonR WRW | lld:pubmed |
| pubmed-article:1577725 | pubmed:author | pubmed-author:PeriniFF | lld:pubmed |
| pubmed-article:1577725 | pubmed:author | pubmed-author:MountjoyKK | lld:pubmed |
| pubmed-article:1577725 | pubmed:author | pubmed-author:HuthJ RJR | lld:pubmed |
| pubmed-article:1577725 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1577725 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1577725 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1577725 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1577725 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1577725 | pubmed:pagination | 8870-9 | lld:pubmed |
| pubmed-article:1577725 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:meshHeading | pubmed-meshheading:1577725-... | lld:pubmed |
| pubmed-article:1577725 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1577725 | pubmed:articleTitle | Intracellular folding pathway of human chorionic gonadotropin beta subunit. | lld:pubmed |
| pubmed-article:1577725 | pubmed:affiliation | Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805. | lld:pubmed |
| pubmed-article:1577725 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1577725 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1577725 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1577725 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1577725 | lld:pubmed |
