DNA Deamination and the Immune System : Aid in Health and Disease /

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Bibliographic Details
Imprint:London : Imperial College Press ; Hackensack, NJ : Distributed by World Scientific Pub., ©2011.
Description:1 online resource (xiii, 217 pages) : illustrations
Language:English
Series:Molecular medicine and medicinal chemistry ; v. 3
Molecular medicine and medicinal chemistry ; v. 3.
Subject:
Format: E-Resource Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/11258565
Hidden Bibliographic Details
Other authors / contributors:Fugmann, Sebastian.
Diaz, Marilyn.
Papavasiliou, Nina.
ISBN:9781848165939
1848165935
9781848165922
1848165927
Digital file characteristics:data file
Notes:Includes bibliographical references and index.
Print version record.
Summary:This book covers the current understanding of the role of activation-induced cytidine deaminase (AID) in the generation of antibody response to antigenic challenge. Since the discovery of AID, and the genetic demonstration of its role in somatic hypermutation and class-switch recombination of antibody genes, much has been learned about the biochemistry of this enzyme. However, some key questions remain hotly contested, such as : how does this enzyme get to the antibody locus leaving the rest of the genome intact, and why are DNA repair pathways which normally repair deamination events co-opted into actually fixing mutations into the genome? These questions, among others, will be addressed in this monograph from various perspectives. Being leading experts in their respective fields, the contributors of this highly valued title summarize current research in the field of AID and put forth hypotheses in order to provide a platform for future experiments.
Other form:Print version: DNA deamination and the immune system. London : Imperial College Press ; Hackensack, NJ : Distributed by World Scientific Pub., ©2011 9781848165922

MARC

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245 0 0 |a DNA Deamination and the Immune System :  |b Aid in Health and Disease /  |c editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou. 
260 |a London :  |b Imperial College Press ;  |a Hackensack, NJ :  |b Distributed by World Scientific Pub.,  |c ©2011. 
300 |a 1 online resource (xiii, 217 pages) :  |b illustrations 
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490 1 |a Molecular medicine and medicinal chemistry ;  |v v. 3 
504 |a Includes bibliographical references and index. 
505 0 |a 1. Introduction. 1.1. Discovery of AID. 1.2. Current model of AID function. 1.3. Open questions. 1.4. A unifying model for AID function. 1.5. Acknowledgements. 1.6. References -- 2. Switch regions, chromatin accessibility and AID targeting. 2.1. Introduction. 2.2. Transcriptional elements determine long-range regulation of CSR. 2.3. Cis-regulatory elements as recruiters for AID. 2.4. Transcription and accessibility to AID attack. 2.5. S region sequence determines chromatin accessibility. 2.6. AID-induced mutation distribution and transcription. 2.7. Processing of GLTs and the introduction of AID-induced mutations. 2.8. Future directions. 2.9. Acknowledgements. 2.10. References -- 3. Cis-regulatory elements that target AID to immunoglobulin loci. 3.1. Introduction. 3.2. Targeting by Ig promoters -- Are high levels of transcription all there is to it? 3.3. SHM targeting elements in Ig light chain loci. 3.4. Targeting elements in the murine IgH locus. 3.5. Outlook. 3.6. Acknowledgements. 3.7. References -- 4. Partners in diversity : The search for AID co-factors. 4.1. Introduction and overview. 4.2. Compartmentalization of AID. 4.3. The C-terminal domain of AID. 4.4. Targeting AID in the context of cotranscriptional pre-mRNA splicing by CTNNBL1. 4.5. Replication Protein A (RPA). 4.6. Protein kinase A (PKA) and regulation of AID activity by phosphorylation. 4.7. Recruitment of PKA to switch region sequences. 4.8. Concluding remarks. 4.9. Acknowledgements. 4.10. References -- 5. Resolution of AID lesions in class switch recombination. 5.1. Introduction. 5.2. Conversion of AID lesions to double-strand DNA breaks. 5.3. Repair of double-strand DNA breaks in class switch recombination. 5.4. Concluding comments and future questions. 5.5. References -- 6. Error-prone and error-free resolution of AID lesions in SHM. 6.1. Introduction. 6.2. Direct replication across the Uracil : G/C transitions. 6.3. UNG2-dependent SHM across AP sites : G/C transversions and transitions. 6.4. MutS[symbol]-dependent SHM at MMR gaps : A/T mutations. 6.5. UNG-dependent A/T mutations. 6.6. Half of all G/C transversions require MutS[symbol] and UNG2. 6.7. Translesion synthesis DNA polymerases. 6.8. Regulating TLS by ubiquitylation of PCNA. 6.9. SHM : Mutagenesis at template A/T requires PCNA-Ub. 6.10. PCNA-Ub-independent G/C transversions during SHM. 6.11. MutS[symbol] and UNG2 do not compete during SHM : Cell cycle and error-free repair. 6.12. Aberrant targeting of AID and error-free repair of AID-induced uracils. 6.13. Acknowledgements. 6.14. References -- 7. Regulatory mechanisms of AID function. 7.1. Introduction. 7.2. Transcriptional regulation of AID gene expression. 7.3. Posttranscriptional regulation of mRNA levels. 7.4. Posttranslational control of AID. 7.5. Integration of AID regulation : The outstanding questions. 7.6. Acknowledgements. 7.7. References -- 8. AID in immunodeficiency and cancer. 8.1. AID and immunodeficiencies. 8.2. AID and cancer. 8.3. Acknowledgements. 8.4. References -- 9. AID in aging and in autoimmune disease. 9.1. AID and aging. 9.2. Aging decreases humoral immune responses. 9.3. AID in autoimmunity. 9.4. Conclusion. 9.5. Acknowledgements. 9.6. References. 
520 |a This book covers the current understanding of the role of activation-induced cytidine deaminase (AID) in the generation of antibody response to antigenic challenge. Since the discovery of AID, and the genetic demonstration of its role in somatic hypermutation and class-switch recombination of antibody genes, much has been learned about the biochemistry of this enzyme. However, some key questions remain hotly contested, such as : how does this enzyme get to the antibody locus leaving the rest of the genome intact, and why are DNA repair pathways which normally repair deamination events co-opted into actually fixing mutations into the genome? These questions, among others, will be addressed in this monograph from various perspectives. Being leading experts in their respective fields, the contributors of this highly valued title summarize current research in the field of AID and put forth hypotheses in order to provide a platform for future experiments. 
588 0 |a Print version record. 
650 0 |a Autoimmune diseases  |x Molecular aspects. 
650 0 |a Autoimmune diseases  |x Gene therapy. 
650 0 |a Deamination.  |0 http://id.loc.gov/authorities/subjects/sh85036076 
650 0 |a Immunoglobulins.  |0 http://id.loc.gov/authorities/subjects/sh85064568 
650 0 |a Enzymes.  |0 http://id.loc.gov/authorities/subjects/sh85044229 
650 2 |a DNA  |x physiology. 
650 2 |a Deamination  |x immunology. 
650 7 |a SCIENCE  |x Life Sciences  |x Anatomy & Physiology.  |2 bisacsh 
650 7 |a Immunoglobulins.  |2 fast  |0 (OCoLC)fst00967961 
650 7 |a Enzymes.  |2 fast  |0 (OCoLC)fst00913605 
650 7 |a Autoimmune diseases  |x Molecular aspects.  |2 fast  |0 (OCoLC)fst00822670 
650 7 |a Deamination.  |2 fast  |0 (OCoLC)fst00888602 
655 4 |a Electronic books. 
700 1 |a Fugmann, Sebastian. 
700 1 |a Diaz, Marilyn. 
700 1 |a Papavasiliou, Nina. 
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