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010   $a981-15-2509-9
024 7 $a10.1007/978-981-15-2509-4
035   $a(CKB)4100000010673463
035   $a(DE-He213)978-981-15-2509-4
035   $a(MiAaPQ)EBC6142510
035   $a(PPN)24322382X
035   $a(EXLCZ)994100000010673463
100   $a20200320d2020      u|         0
101 0 $aeng
135   $aurnn|008mamaa
181   $ctxt$2rdacontent
182   $cc$2rdamedia
183   $acr$2rdacarrier
200 10$aStudy on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation /$fby Xiucong Bao
205   $a1st ed. 2020.
210  1$aSingapore :$cSpringer Singapore :$cImprint: Springer,$d2020.
215   $a1 online resource (XVIII, 163 p. 132 illus., 96 illus. in color.) 
225 1 $aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
300   $a"Doctoral Thesis accepted by The University of Hong Kong, China"--Title page.
311   $a981-15-2508-0 
320   $aIncludes bibliographical references.
327   $aIntroduction to Protein Posttranslational Modifications (PTMs) -- Chemical reporter for Lysine Malonylation -- Identification of Histone Lysine Glutarylation -- Glutarylation at Histone H4 lysine 91 Modulates Chromatin Assembly -- Identification of Sirt3 as an ?Eraser? for Histone Lysine Crotonylation Marks using a Chemical Proteomics Approach.
330   $aThis book presents pioneering findings on the characterization of cellular regulation and function for three recently identified protein posttranslational modifications (PTMs): lysine malonylation (Kmal), glutarylation (Kglu) and crotonylation (Kcr). It addresses three main topics: (i) Detecting Kmal substrates using a chemical reporter, which provides important information regarding the complex cellular networks modulated by Kmal; (ii) Identifying Kglu as a new histone PTM and assessing the direct impact of histone Kglu on chromatin structure and dynamics; and (iii) Revealing Sirt3?s value as a regulating enzyme for histone Kcr dynamics and gene transcription, which opens new avenues for examining the physiological significance of histone Kcr. Taken together, these studies provide information critical to understanding how these protein PTMs are associated with various human diseases, and to identifying therapeutic targets for the dysregulation of these novel protein markers in various human diseases.
410  0$aSpringer Theses, Recognizing Outstanding Ph.D. Research,$x2190-5053
606   $aBioorganic chemistry
606   $aPosttranslational modification
606   $aProteins 
606   $aProteomics
606   $aGene expression
606   $aCell cycle
606   $aBioorganic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C19010
606   $aPosttranslational Modification$3https://scigraph.springernature.com/ontologies/product-market-codes/L14090
606   $aProtein Structure$3https://scigraph.springernature.com/ontologies/product-market-codes/L14050
606   $aProteomics$3https://scigraph.springernature.com/ontologies/product-market-codes/L1403X
606   $aGene Expression$3https://scigraph.springernature.com/ontologies/product-market-codes/B12010
606   $aCell Cycle Analysis$3https://scigraph.springernature.com/ontologies/product-market-codes/L16030
615  0$aBioorganic chemistry.
615  0$aPosttranslational modification.
615  0$aProteins .
615  0$aProteomics.
615  0$aGene expression.
615  0$aCell cycle.
615 14$aBioorganic Chemistry.
615 24$aPosttranslational Modification.
615 24$aProtein Structure.
615 24$aProteomics.
615 24$aGene Expression.
615 24$aCell Cycle Analysis.
676   $a612.39
700   $aBao$b Xiucong$4aut$4http://id.loc.gov/vocabulary/relators/aut$01060594
801  0$bMiAaPQ
801  1$bMiAaPQ
801  2$bMiAaPQ
906   $aBOOK
912   $a9910410051803321
996   $aStudy on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation$92514386
997   $aUNINA