Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers.
The cysteine residues involved in the class I disulfide bonds between the alpha subunits in the (alpha beta)2 dimer of the human insulin receptor have been identified by labeling with N-ethylmaleimide and by site-directed mutagenesis. Both cysteine 524 and cysteine 682 form interchain disulfide bond...
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| Pubblicato in: | Mol Biol Cell |
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| Autori principali: | , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Cell Biology
1996
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC275922/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8744943/ https://ncbi.nlm.nih.govhttps://doi.org/10.1091/mbc.7.5.679 |
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