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Author: Ming-Ming Zhou
Publisher: Springer
ISBN: 3319181025
Category : Medical
Languages : en
Pages : 284
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Book Description
This 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.
Author: Ming-Ming Zhou
Publisher: Springer
ISBN: 3319181025
Category : Medical
Languages : en
Pages : 284
Get Book Here
Book Description
This 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.
Author: Stefan Jurga
Publisher: Springer Nature
ISBN: 3030147924
Category : Medical
Languages : en
Pages : 624
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Book Description
This book reviews the chemical, regulatory, and physiological mechanisms of protein arginine and lysine methyltransferases, as well as nucleic acid methylations and methylating enzymes. Protein and nucleic acid methylation play key and diverse roles in cellular signalling and regulating macromolecular cell functions. Protein arginine and lysine methyltransferases are the predominant enzymes that catalyse S-adenosylmethionine (SAM)-dependent methylation of protein substrates. These enzymes catalyse a nucleophilic substitution of a methyl group to an arginine or lysine side chain nitrogen (N) atom. Cells also have additional protein methyltransferases, which target other amino acids in peptidyl side chains or N-termini and C-termini, such as glutamate, glutamine, and histidine. All these protein methyltransferases use a similar mechanism. In contrast, nucleic acids (DNA and RNA) are substrates for methylating enzymes, which employ various chemical mechanisms to methylate nucleosides at nitrogen (N), oxygen (O), and carbon (C) atoms. This book illustrates how, thanks to there ability to expand their repertoire of functions to the modified substrates, protein and nucleic acid methylation processes play a key role in cells.
Author: Anna Elizabeth Smith
Publisher:
ISBN:
Category :
Languages : en
Pages : 259
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Book Description
Author: Marie Jung
Publisher:
ISBN:
Category :
Languages : en
Pages :
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Book Description
Author: Ina Bock
Publisher:
ISBN:
Category :
Languages : en
Pages : 63
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Book Description
Molecular epigenetics is described as the study of heritable changes in gene function without alterations in DNA sequence. Epigenetic phenomena are regulated by three interconnected players: DNA methylation, post-translational histone modifications and non-coding RNAs, which are involved in the regulation of many cellular processes including cellular differentiation and transcription. Post-translational histone modifications either directly modulate chromatin structure or they can serve as binding signals for reading domains, which recognize the modifications and mediate most of the biological functions of these modifications. In the present PhD work, we have introduced Celluspots peptide arrays as a tool for the initial screening of putative reading domains interacting with a diverse set of post-translational histone modifications in one experiment in competition. With this tool, we studied the binding specificities of antibodies and reading domains with known as well as unknown primary targets. Furthermore, we studied differences and similarities in substrate recognition of two histone lysine methyltransferases, MLL3 and MLL1, from the same protein family. Celluspots peptide arrays were first validated with antibodies directed towards post-translational histone tail modifications. In this study, we found that most of the antibodies bound well to the modification they had been raised for, but some failed. Some antibodies showed high cross-reactivity and most of the antibodies were inhibited by additional modifications close to the primary one. Furthermore, the comparison of the specificity profiles of antibodies, which had been raised for the same modification, revealed that the binding profiles sometimes differed greatly. Therefore, we did not only validate the method with this approach, but we further introduced Celluspots peptide arrays as a good tool for the quality control of epigenetic antibodies. Additionally, we applied Celluspots peptide arrays for the investigation of the specificity of the interaction of reading domains with known substrate specificity with histone peptides. The results that we obtained with this approach agreed with literature concerning the primary targets of the reading domains, but we also obtained previously unknown information concerning the influence of secondary modifications for the binding affinity to the primary targets of these reading domains. After validation of Celluspots peptide arrays, we screened approximately 20 reading domain candidates and proceeded with the most promising candidates for further analysis. One such candidate is a human polycomb group protein, which was shown to associate with the core components of the Polycomb repressive complex 2. The Polycomb repressive complex 2 is the major histone 3 lysine 27 methyltransferase-containing complex, which tri-methylates this lysine residue. Tri-methylated histone 3 lysine 27 is a post-translational modification, which is associated with transcriptional repression of developmental genes, especially HOX genes. We found that this polycomb group protein recognizes this histone tail modification in a histone variant specific manner. This histone variant is thought to be exclusively expressed in the mammalian testis and we propose that this polycomb group protein is involved in targeting the complex to this histone variant tri-methylated at lysine 27 in the human testis. The histone lysine methyltransferases of the mixed lineage leukemia (MLL) protein family mono-, di- and tri-methylate histone 3 lysine 4. We studied the substrate specificity for two members of this family, MLL3 and MLL1, and revealed that the preferred substrate sequences are different. With these differences in substrate recognition we searched for non-histone targets and found similar, but also different non-histone targets at the peptide level. This is the first time that differences in substrate recognition was observed for MLL methyltransferases, which do not depend on differing MLL-complex members, which are known to be involved in targeting the methyltransferases to their gene targets.
Author: Atsushi Kaneda
Publisher: Springer
ISBN: 3319597868
Category : Medical
Languages : en
Pages : 616
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Book Description
This book will focus on DNA and histone methylation in epigenetics and describe how it is involved in the molecular mechanisms responsible for the development of cancer. Chapters will summarize the current knowledge of the molecular basis of DNA and histone methylation and explain how it is involved in cancer, describe the features of DNA and histone methylation associated with particular types of cancer, diagnostic/therapeutic applications, and future directions of DNA and histone methylation as cancer targets.
Author:
Publisher: ScholarlyEditions
ISBN: 1481674978
Category : Medical
Languages : en
Pages : 414
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Book Description
Diamino Amino Acids—Advances in Research and Application: 2013 Edition is a ScholarlyEditions™ book that delivers timely, authoritative, and comprehensive information about Citrulline. The editors have built Diamino Amino Acids—Advances in Research and Application: 2013 Edition on the vast information databases of ScholarlyNews.™ You can expect the information about Citrulline in this book to be deeper than what you can access anywhere else, as well as consistently reliable, authoritative, informed, and relevant. The content of Diamino Amino Acids—Advances in Research and Application: 2013 Edition has been produced by the world’s leading scientists, engineers, analysts, research institutions, and companies. All of the content is from peer-reviewed sources, and all of it is written, assembled, and edited by the editors at ScholarlyEditions™ and available exclusively from us. You now have a source you can cite with authority, confidence, and credibility. More information is available at http://www.ScholarlyEditions.com/.
Author: Ramón Cacabelos
Publisher: Academic Press
ISBN: 0128139404
Category : Medical
Languages : en
Pages : 986
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Book Description
Pharmacoepigenetics provides a comprehensive volume on the role of epigenetics and epigenomics in drug discovery and development, providing a detailed, but accessible, view of the field, from basic principles, to applications in disease therapeutics. Leading international researchers from across academia, clinical settings and the pharmaceutical industry discuss the influence of epigenetics and epigenomics in human pathology, epigenetic biomarkers for disease prediction, diagnosis, and treatment, current epigenetic drugs, and the application of epigenetic procedures in drug development. Throughout the book, chapter authors offer a balanced and objective discussion of the future of pharmacoepigenetics and its crucial contribution to the growth of precision and personalized medicine. - Fully examines the influence of epigenetics and epigenomics in human pathology, epigenetic biomarkers for disease prediction, diagnosis, treatment, current epigenetic drugs and the application of epigenetic procedures in drug development - Features chapter contributions from leading international researchers in academia, clinical settings and the pharmaceutical industry - Instructs researchers, students and clinicians on how to better interpret and employ pharmacoepigenetics in drug development, efficiency and safety - Provides a balanced and objective discussion of the future of pharmacoepigenetics and its crucial role in precision medicine
Author: Philippe Jeanteur
Publisher:
ISBN: 9783662097298
Category :
Languages : en
Pages : 266
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Book Description
Author: Wolfgang Sippl
Publisher: John Wiley & Sons
ISBN: 3527809287
Category : Medical
Languages : en
Pages : 480
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Book Description
This broad view of epigenetic approaches in drug discovery combines methods and strategies with individual targets, including new and largely unexplored ones such as sirtuins and methyl-lysine reader proteins. Presented in three parts - Introduction to Epigenetics, General Aspects and Methodologies, and Epigenetic Target Classes - it covers everything any drug researcher would need in order to know about targeting epigenetic mechanisms of disease. Epigenetic Drug Discovery is an important resource for medicinal chemists, pharmaceutical researchers, biochemists, molecular biologists, and molecular geneticists.
