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Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation

About Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation

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 varioushuman diseases.

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  • Language:
  • English
  • ISBN:
  • 9789811525117
  • Binding:
  • Paperback
  • Pages:
  • 163
  • Published:
  • March 20, 2021
  • Edition:
  • 2020
  • Dimensions:
  • 155x235x0 mm.
  • Weight:
  • 454 g.
Delivery: 2-4 weeks
Expected delivery: August 10, 2025

Description of Study on the Cellular Regulation and Function of Lysine Malonylation, Glutarylation and Crotonylation

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 varioushuman diseases.

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