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Structure, ISSN 0969-2126, 01/2018, Volume 26, Issue 1, pp. 145 - 152.e3
The androgen receptor is a transcription factor that plays a key role in the development of prostate cancer, and its interactions with general transcription... 
transcription factor IIF | androgen receptor | transcription | castration-resistant prostate cancer | protein phosphorylation | intrinsic disorder | protein-protein interactions | RNA-POLYMERASE-II | INDUCED ALPHA-HELIX | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHOSPHATASE FCP1 | ADVANCED PROSTATE-CANCER | FACTOR-TFIIF | CELL BIOLOGY | BIOPHYSICS | ACTIVATION DOMAINS | STRUCTURAL BASIS | CARBOXYL-TERMINAL DOMAIN | NMR STRUCTURE | BINDING | Humans | Protein Multimerization | Receptors, Androgen - metabolism | Transcriptional Activation | Crystallography, X-Ray | Male | Prostatic Neoplasms, Castration-Resistant - genetics | Cloning, Molecular | Escherichia coli - metabolism | HEK293 Cells | Receptors, Androgen - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | DNA - metabolism | Intrinsically Disordered Proteins - genetics | Prostatic Neoplasms, Castration-Resistant - metabolism | Amino Acid Motifs | DNA - genetics | Transcription Factors, TFII - chemistry | DNA - chemistry | Transcription Factors, TFII - genetics | Receptors, Androgen - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Intrinsically Disordered Proteins - chemistry | Protein Binding | Transcription Factors, TFII - metabolism | Intrinsically Disordered Proteins - metabolism | Genetic transcription | Prostate cancer | Protein-protein interactions | Resveratrol | Receptors d'hormones | Andrògens | Hormone receptors | Androgens | Terapèutica | Càncer de pròstata | Therapeutics
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2005, Volume 391, Issue 3, pp. 449 - 464
Steroid hormones are important endocrine signalling molecules controlling reproduction, development, metabolism, salt balance and specialized cellular... 
Af1 transactivation domain | Post-translational modification | Steroid receptor | Allosteric regulation | Protein-protein interaction | Protein-nucleic acid interaction | Secondary structure | protein-nucleic acid interaction | RNA-POLYMERASE-II | HUMAN ESTROGEN-RECEPTOR | HUMAN MINERALOCORTICOID RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACTIVATION FUNCTION 1 | AF1 transactivation domain | allosteric regulation | post-translational modification | TRANSCRIPTION FACTOR-TFIIF | steroid receptor | secondary structure | AMINO-TERMINAL DOMAIN | HUMAN ANDROGEN RECEPTOR | HUMAN GLUCOCORTICOID-RECEPTOR | protein-protein interaction | LIGAND-BINDING DOMAIN | HUMAN PROGESTERONE-RECEPTORS | Protein Structure, Tertiary | Animals | Receptors, Steroid - metabolism | Humans | Transcriptional Activation | Models, Molecular | Protein Binding | Protein Processing, Post-Translational | Receptors, Steroid - chemistry | SMRT, silencing mediator of retinoid and thyroid hormone receptor | protein–protein interaction | PSA, prostate-specific antigen | PIC, pre-initiation complex | SRC-1, steroid receptor co-activator 1 | Review | PR, progesterone receptor | HCA, hydrophobic cluster analysis | IF, inhibitory function | protein–nucleic acid interaction | PKB, protein kinase B | FLASH, Fas-associated huge protein | AF, activation function | SC, synergy control | SHR, steroid hormone receptor | TIF2, transcription intermediary factor 2 | GTF, general transcription factor | β, oestrogen receptor α and β respectively | TFE, trifluoroethanol | DBD, DNA-binding domain | ERα | GRIP1, glucocorticoid receptor-interacting protein 1 | TBP, TATA-binding protein | LBD, ligand-binding domain | PIAS, protein inhibitor of activated STAT | TMAO, trimethylamine-N-oxide | NCoR, nuclear receptor co-repressor | MR, mineralocorticoid receptor | NTD, N-terminal domain | GR, glucocorticoid receptor | ERE, oestrogen-response element | FTIR spectroscopy, Fourier-transform infrared spectroscopy | AR, androgen receptor | CBP, CREB (cAMP-response-element-binding protein)-binding protein | MAPK, mitogen-activated protein kinase
Journal Article
Journal Article
PLoS Pathogens, ISSN 1553-7366, 2014, Volume 10, Issue 3, p. e1004042
Journal Article
Journal Article