| pubmed-article:8631838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C1533585 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C1414824 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C1321758 | lld:lifeskim |
| pubmed-article:8631838 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:8631838 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:8631838 | pubmed:dateCreated | 1996-7-1 | lld:pubmed |
| pubmed-article:8631838 | pubmed:abstractText | The gonadotropin/thyrotropin hormone family is characterized by a heterodimeric structure composed of a common alpha subunit noncovalently linked to a hormone-specific beta subunit. The conformation of the heterodimer is essential for controlling secretion, hormone-specific post-translational modifications, and signal transduction. Structure-function studies of follicle-stimulating hormone (FSH) and the other glycoprotein hormones are often hampered by mutagenesis-induced defects in subunit combination. Thus, the ability to overcome the limitation of subunit assembly would expand the range of structure-activity relationships that can be performed on these hormones. Here we converted the FSH heterodimer to a single chain by genetically fusing the carboxyl end of the FSH beta subunit to the amino end of the alpha subunit in the presence or absence of a linker sequence. In the absence of the CTP linker, the secretion rate was decreased over 3-fold. Unexpectedly, however, receptor binding/signal transduction was unaffected by the absence of the linker. These data show that the single-chain FSH was secreted efficiently and is biologically active and that the conformation determinants required for secretion and biologic activity are not the same. | lld:pubmed |
| pubmed-article:8631838 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8631838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8631838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8631838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8631838 | pubmed:month | May | lld:pubmed |
| pubmed-article:8631838 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:SatoAA | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:KudoMM | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:BoimeII | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:HsuehA JAJ | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:SugaharaTT | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:Ben-MenahemDD | lld:pubmed |
| pubmed-article:8631838 | pubmed:author | pubmed-author:PixleyM RMR | lld:pubmed |
| pubmed-article:8631838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8631838 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:8631838 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8631838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8631838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8631838 | pubmed:pagination | 10445-8 | lld:pubmed |
| pubmed-article:8631838 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:meshHeading | pubmed-meshheading:8631838-... | lld:pubmed |
| pubmed-article:8631838 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8631838 | pubmed:articleTitle | Expression of biologically active fusion genes encoding the common alpha subunit and the follicle-stimulating hormone beta subunit. Role of a linker sequence. | lld:pubmed |
| pubmed-article:8631838 | pubmed:affiliation | Department of Molecular Biology & Pharmacology, Washington University School of Medicine, St. Louis, Missouri 63110, USA. | lld:pubmed |
| pubmed-article:8631838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8631838 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8631838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8631838 | lld:pubmed |
