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Title DNA Deamination and the Immune System : Aid in Health and Disease / editors, Sebastian Fugmann, Marilyn Diaz, Nina Papavasiliou.

Imprint London : Imperial College Press ; Hackensack, NJ : Distributed by World Scientific Pub., 2011.

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Location Call No. OPAC Message Status
 Axe EBSCO Clinical Nursing E-Book  Electronic Book    ---  Available
Description 1 online resource (xiii, 217 pages) : illustrations.
text txt rdacontent
computer c rdamedia
online resource cr rdacarrier
data file rda
Series Molecular medicine and medicinal chemistry ; v. 3
Molecular medicine and medicinal chemistry ; v. 3.
Bibliography Includes bibliographical references and index.
Contents 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.
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.
Note Print version record.
Subject Autoimmune diseases -- Molecular aspects.
Autoimmune diseases -- Gene therapy.
Deamination.
Immunoglobulins.
Enzymes.
SCIENCE -- Life Sciences -- Anatomy & Physiology.
Immunoglobulins. (OCoLC)fst00967961
Enzymes. (OCoLC)fst00913605
Autoimmune diseases -- Molecular aspects. (OCoLC)fst00822670
Deamination. (OCoLC)fst00888602
Deamination -- immunology.
DNA -- physiology.
Genre/Form Electronic books.
Electronic book.
Added Author Fugmann, Sebastian.
Diaz, Marilyn.
Papavasiliou, Nina.
Other Form: Print version: DNA deamination and the immune system. London : Imperial College Press ; Hackensack, NJ : Distributed by World Scientific Pub., 2011 9781848165922 (OCoLC)651076605
ISBN 9781848165939 (electronic bk.)
1848165935 (electronic bk.)
9781848165922
1848165927
Standard No. AU@ 000048716176
AU@ 000051577231
AU@ 000058255701
DEBBG BV043098501
DEBBG BV044156181
DEBSZ 421584076
DEBSZ 456483748
HEBIS 286065037
NZ1 14167717

 
    
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