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Intracellular transport blockade caused by disruption of the disulfide bridge in the third external domain of major histocompatibility complex class I antigen.

The third external domain of major histocompatibility class I antigens has a highly conserved disulfide bridge between cysteine-203 and cysteine-259. To elucidate the functional significance of this disulfide bridge, we have produced a mutant H-2Ld gene by site-directed mutagenesis in which the codo...

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Библиографические подробности
Главные авторы: Miyazaki, J, Appella, E, Ozato, K
Формат: Artigo
Язык:Inglês
Опубликовано: 1986
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC322944/
https://ncbi.nlm.nih.gov/pubmed/3080749
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