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010   $a3-319-18102-5
024 7 $a10.1007/978-3-319-18102-8
035   $a(CKB)3710000000416706
035   $a(EBL)2094800
035   $a(SSID)ssj0001500649
035   $a(PQKBManifestationID)11866009
035   $a(PQKBTitleCode)TC0001500649
035   $a(PQKBWorkID)11522404
035   $a(PQKB)10400799
035   $a(DE-He213)978-3-319-18102-8
035   $a(MiAaPQ)EBC2094800
035   $a(PPN)186026757
035   $a(EXLCZ)993710000000416706
100   $a20150529d2015      u|         0
101 0 $aeng
135   $aur|n|---|||||
181   $ctxt
182   $cc
183   $acr
200 10$aHistone Recognition /$fedited by Ming-Ming Zhou
205   $a1st ed. 2015.
210  1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2015.
215   $a1 online resource (284 p.)
300   $aDescription based upon print version of record.
311   $a3-319-18101-7 
320   $aIncludes bibliographical references and index.
327   $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.
330   $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.
606   $aGene expression
606   $aPosttranslational modification
606   $aProteins 
606   $aMedical genetics
606   $aGene Expression$3https://scigraph.springernature.com/ontologies/product-market-codes/B12010
606   $aPosttranslational Modification$3https://scigraph.springernature.com/ontologies/product-market-codes/L14090
606   $aProtein-Ligand Interactions$3https://scigraph.springernature.com/ontologies/product-market-codes/L14060
606   $aGene Function$3https://scigraph.springernature.com/ontologies/product-market-codes/B12030
615  0$aGene expression.
615  0$aPosttranslational modification.
615  0$aProteins .
615  0$aMedical genetics.
615 14$aGene Expression.
615 24$aPosttranslational Modification.
615 24$aProtein-Ligand Interactions.
615 24$aGene Function.
676   $a572.6
676   $a610
676   $a611.01816
702   $aZhou$b Ming-Ming$4edt$4http://id.loc.gov/vocabulary/relators/edt
906   $aBOOK
912   $a9910298296503321
996   $aHistone Recognition$92508865
997   $aUNINA