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Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation [electronic resource] / by Xiucong Bao.

By: Bao, Xiucong [author.]Contributor(s): SpringerLink (Online service)Material type: Text

TextSeries: Springer Theses, Recognizing Outstanding Ph.D. ResearchPublisher: Singapore : Springer Singapore : Imprint: Springer, 2020Edition: 1st ed. 2020Description: XVIII, 163 p. 132 illus., 96 illus. in color. online resourceContent type: text Media type: computer Carrier type: online resourceISBN: 9789811525094Subject(s): Bioorganic chemistry | Posttranslational modification | Proteins | Proteomics | Gene expression | Cell cycle | Bioorganic Chemistry | Posttranslational Modification | Protein Structure | Proteomics | Gene Expression | Cell Cycle AnalysisAdditional physical formats: Printed edition:: No title; Printed edition:: No title; Printed edition:: No titleDDC classification: 547 LOC classification: QD241-441Online resources: Click here to access online

Contents:

Introduction 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.

In: Springer Nature eBookSummary: This 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.

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This 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.

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