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Study on the cellular regulation and...

Bao, Xiucong.

Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylation

Record Type:	Electronic resources : Monograph/item
Title/Author:	Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylationby Xiucong Bao.
Author:	Bao, Xiucong.
Published:	Singapore :Springer Singapore :2020.
Description:	xviii, 163 p. :ill., digital ;24 cm.
Contained By:	Springer eBooks
Subject:	Lysine.
Online resource:	https://doi.org/10.1007/978-981-15-2509-4
ISBN:	9789811525094$q(electronic bk.)

Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylation
Bao, Xiucong.

Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylation[electronic resource] /by Xiucong Bao. - Singapore :Springer Singapore :2020. - xviii, 163 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..

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.

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.

ISBN: 9789811525094$q(electronic bk.)

Standard No.: 10.1007/978-981-15-2509-4doiSubjects--Topical Terms:

787177
Lysine.

LC Class. No.: QP562.L8 / B369 2020

Dewey Class. No.: 572.6

Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylation
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100 1 $a Bao, Xiucong. $3 859445
245 1 0 $a Study on the cellular regulation and function of lysine malonylation, glutarylation and crotonylation $h [electronic resource] / $c by Xiucong Bao.
260 $a Singapore : $b Springer Singapore : $b Imprint: Springer, $c 2020.
300 $a xviii, 163 p. : $b ill., digital ; $c 24 cm.
490 1 $a Springer theses, $x 2190-5053
505 0 $a 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.
520 $a 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.
650 0 $a Lysine. $3 787177
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650 2 4 $a Protein Structure. $3 348844
650 2 4 $a Proteomics. $3 220403
650 2 4 $a Gene Expression. $3 220379
650 2 4 $a Cell Cycle Analysis. $3 561444
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