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| 003 | ES-MaUEC | ||
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| 007 | cr nn 008mamaa | ||
| 008 | 150819s2015 gw | s |||| 0|eng d | ||
| 020 | _a9783319187297 | ||
| 024 | 7 |
_a10.1007/978-3-319-18729-7 _2doi |
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| 040 |
_aES-MaUEC _bspa |
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| 050 | 4 |
_aQH603.C43 _bN835 2015 |
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| 245 | 1 | 0 |
_aNuclear Receptors : _bFrom Structure to the Clinic _cedited by Iain J. McEwan, Raj Kumar. |
| 250 | _a1st ed. 2015. | ||
| 260 |
_aCham, Switzerland _bSpringer _c2015 |
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| 300 |
_a1 recurso en línea (XI, 236 páginas) _b43 ilustraciones, 33 ilustraciones en color |
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| 336 |
_aTexto _btxt _2rdacontent |
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| 337 |
_aelectrónico _bc _2rdamedia |
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| 338 |
_arecurso electrónico _bcr _2rdacarrier |
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| 505 | 0 | _a1. Twenty-five Years of Nuclear Receptor Structure Analysis: From the Laboratory to the Clinic -- Part A. ALLOSTERIC REGULATION AND NUCLEAR RECEPTOR COMPLEX DYNAMICS. -2. Corticosteroid Receptors -- 3. Glucocorticoid Receptor Structure and Function -- 4. What Determines the Difference in DNA Binding Between the Androgen and the Glucocorticoid Receptors? -- 5. Allosteric Regulation and Intrinsic Disorder in Nuclear Hormone Receptors -- 6. Structural Analyses of Ordered and Disordered Regions in Ecdysteroid Receptor -- 7. Structural Analysis of Heterodimeric Nuclear Receptors -- Part B. NUCLEAR RECEPTOR CO-REGULATORY PROTEIN INTERACTIONS -- 8. Primate-specific Multi-functional Androgen Receptor Coregulator and Proto-oncogene Melanoma Antigen-A11 (MAGE-A11) -- 9. Assembly and Regulation of Nuclear Receptor Corepressor Complexes -- Part C. TAKING NUCLEAR RECEPTOR STRUCTURE INTO THE CLINIC -- 10. Thinking Outside the Box: Alternative Binding Sites in the Ligand Binding Domain of Nuclear Receptors -- 11. Selective Estrogen Receptor Modulators (SERMs) and Selective Androgen Receptor Modulators (SARMs). | |
| 520 | 3 | _aNuclear Receptors focuses on the structural analysis of nuclear receptors from the initial work using isolated protein domains to the more recent exciting developments investigating the conformational shape of full-length receptor complexes. The book also reviews the structure of key nuclear receptor co-regulatory proteins. The aim is to bring together, for the first time, a comprehensive review of nuclear receptor structure and the importance of receptor conformation underpinning allosteric regulation by different ligands (hormone, drugs, DNA response elements, protein-protein interactions) and receptor activity. The nuclear receptor superfamily, including receptors for steroid hormones and non-steroid ligands, are pivotal to normal physiology, regulating processes as diverse as reproduction, metabolism, the immune system and brain development. The first members of the family were cloned over 25 years ago, which heralded in the idea of a superfamily of intracellular receptor proteins that bound small molecule ligands: classical steroid hormones, vitamins, fatty acids and other products of metabolism. These signals are then transmitted through multiprotein receptor-DNA complexes, leading to the regulation of target genes, often in a cell-selective manner. The cloning of the receptor cDNAs also ushered in an era of unparalleled analysis of the mechanisms of action of these ligand-activated transcription factors. | |
| 650 | 7 |
_aFisiología humana _2embne _9140024 |
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| 650 | 7 |
_aEndocrinología _2embne _9139372 |
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| 650 | 7 |
_aGenética humana _2embne _9140562 |
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| 700 | 1 |
_aMcEwan, Iain J _eeditor literario _984922 _0Local |
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| 700 | 1 |
_aKumar, Raj _eeditor literario _993859 _0Local |
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| 710 | 2 |
_aSpringerLink (Online service) _0Local _9106996 |
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| 856 | 4 | 0 |
_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-319-18729-7 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid) |
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_2lcc _cLE |
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| 988 | _aEBOOK, EBSPRINGER, asignarmaterias_11febrero | ||
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