1988
DOI: 10.1016/0022-4731(88)90159-8
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Photoaffinity labelling with [3H]R1881 of androgen receptors from human cultured genital fibroblasts of normal individuals and patients with androgen receptor abnormalities

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Cited by 6 publications
(5 citation statements)
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“…We determined that androgen binding was diminished, but not absent, suggesting a qualitative defect of binding. We have also previously shown that partially purified AR from subject Te24 has a reduced molecular weight (M r ∼43 kDa), suggesting this receptor is truncated (Gyorki et al, 1988). The presence of detectable androgen binding in fibroblasts from this subject suggests that the AR is not truncated in vivo.…”
Section: Te24mentioning
confidence: 77%
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“…We determined that androgen binding was diminished, but not absent, suggesting a qualitative defect of binding. We have also previously shown that partially purified AR from subject Te24 has a reduced molecular weight (M r ∼43 kDa), suggesting this receptor is truncated (Gyorki et al, 1988). The presence of detectable androgen binding in fibroblasts from this subject suggests that the AR is not truncated in vivo.…”
Section: Te24mentioning
confidence: 77%
“…Her testes were removed at age 6 yrs, and a genital skin biopsy was taken at age 12 yrs. (Gyorki et al, 1988). 3 n/d -binding not determined.…”
Section: Subjectsmentioning
confidence: 99%
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“…2a and 2b). Further information concerning the structure of the AR has become available from photoaffinity labelling with R1881 [34][35][36] and cloning of the gene [5][6][7][8]: the AR protein has a molecular mass ranging from 90 to 110 kDa, with an androgen-binding domain corresponding to a 30 kDa portion of the molecule [36].…”
Section: Discussionmentioning
confidence: 99%