Amino acid substitutions in the DNA-binding domain of the human androgen receptor are a frequent cause of receptor-binding positive androgen resistance
- Author
- ZOPPI, S; MARCELLI, M; DESLYPERE, J.-P; GRIFFIN, J. E; WILSON, J. D; MCPHAUL, M. J
Univ. Texas Soutwestern medical cent., dep. internal medicine, Dallas TX 75235-8857, United States - Source
Molecular endocrinology (Baltimore, Md.). 1992, Vol 6, Num 3, pp 409-415 ; ref : 28 ref
- CODEN
- MOENEN
- ISSN
- 0888-8809
- Scientific domain
- Biochemistry, molecular biology, biophysics; Endocrinology
- Publisher
- Endocrine Society, Bethesda, MD
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Androgène Homme Interaction moléculaire Mutation Protéine liaison DNA Résistance tissu cible Structure domaine Testicule féminisant Appareil génital pathologie Endocrinopathie
- Keyword (en)
- Androgen Human Molecular interaction Mutation DNA binding protein Target tissue resistance Domain structure Testicular feminization Genital diseases Endocrinopathy
- Keyword (es)
- Andrógeno Hombre Interacción molecular Mutación Proteína enlace DNA Resistencia tejido blanco Estructura dominio Testículo feminizante Aparato genital patología Endocrinopatía
- Classification
- Pascal
- 002 Biological and medical sciences / 002B Medical sciences / 002B20 Gynecology. Andrology. Obstetrics / 002B20D Male and female genital diseases. Gonadal dysgenesis. Hermaphroditism. Sex hormones resistance
- Discipline
- Gynecology. Andrology. Obstetrics
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 5277335
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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