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008			150529s2015 gw | s |||| 0|eng d
020			_a9783319181028
024	7		_a10.1007/978-3-319-18102-8 _2doi
040			_bspa _dES-MaUEC
050		4	_aQP110.G45
082	0	4	_a611.01816
245	1	0	_aHistone Recognition _cedited by Ming-Ming Zhou.
260			_aCham, Switzerland _bSpringer _c2015
300			_a1 recurso en línea (VIII, 282 p.) _b69 ilustraciones, 51 ilustraciones en color
336			_aTexto (visual) _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
505	0		_aThe Bromodomain as the Acetyl-Lysine Binding Domain in Gene Transcription -- PHD Fingers as Histone Readers -- Methyl-Lysine Recognition by the Royal Family Modules: Chromo, Tudor, MBT, Chromo Barrel, and PWWP Domains -- Histone Recognition by WD40 Proteins -- Methyl-Lys Recognition by Ankyrin Repeat Proteins -- Methyl-Arginine Recognition by Tudor Domains -- Histone Recognition by Tandem Modules and Modulation by Multiple PTMs -- Genome-Wide Profiling of Molecular Recognition of Histone PTMs -- BET Bromodomain Inhibition as a Therapeutic Approach in Hematological Malignancies -- Anti-Inflammatory Effects of BET Protein Inhibition Through Modulation of Gene Transcription -- Activating Latent HIV by Inhibiting Bromodomain Proteins -- Small Molecule Modulation of Methyl-Lysine Mediated Interactions.
520			_aThis book provides a timely review of the role of histone modifications in epigenetic control of gene expression. Topics covered include: basic mechanisms of molecular recognition of histone post-translational modification (PTMs); combinatorial readout of histone PTMs by tandem epigenome reader domains; genome-wide profiling of histone PTM interactions; small molecule modulation of histone PTM interactions and their potential as a new approach to therapeutic intervention in human diseases. All chapters were written by leading scientists who made the original key discoveries of the structure and mechanism of evolutionarily conserved reader domains, which serve to direct gene transcription in chromatin through interactions with DNA-packing histones in a PTM-sensitive manner.
650		0	_9162770 _aExpresión génica _0LocalX
650		7	_aGenética médica _0LocalX _2embne _9144879
650		7	_aProteínas _0LocalX _2embne _9139861
650		7	_aCompuestos orgánicos _xSíntesis _0LocalX _2embne _9187864
650	2	7	_aCompuestos orgánicos _xSíntesis _0LocalX _2embne _9187864
650		7	_aMedicina _0LocalX _2embne _9405021
700	1		_aZhou, Ming-Ming _eeditor literario _993821 _0Local
710	2		_aSpringerLink (Online service) _0Local _9106996
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://link.springer.com/book/10.1007/978-3-319-18102-8 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
907			_a.b12900072 _b10-10-17 _c18-01-16
942			_2lcc _cLE
945			_aQP110.G45 EB _g1 _ieBOOK _j0 _lmae _o- _pEUR0.00 _q- _r- _sb _t15 _u0 _v0 _w0 _x0 _y.i11569694 _z06-04-17
988			_aEBOOK, EBSPRINGER
998			_am _a_alco _a_vill _b - - _cm _dz _e- _feng _ggw _h0