Frederick W. Alt's AID for Immunoglobulin Diversity PDF

By Frederick W. Alt

ISBN-10: 0123737060

ISBN-13: 9780123737069

Advances in Immunology, a protracted confirmed and hugely revered serial, provides present advancements in addition to accomplished reports in immunology. Articles tackle the wide variety of issues that contain immunology, together with molecular and mobile activation mechanisms, phylogeny and molecular evolution, and medical modalities. Edited and authored by way of the most important scientists within the box, each one quantity presents updated info and instructions for destiny study.

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37 38 38 39 48 49 50 51 52 63 63 Abstract The activation‐induced cytidine deaminase (AID)/apolipoprotein B RNA‐ editing catalytic component (APOBEC) family is a vertebrate‐restricted subgrouping of a superfamily of zinc (Zn)‐dependent deaminases that has members distributed throughout the biological world. AID and APOBEC2 are the oldest family members with APOBEC1 and the APOBEC3s being later arrivals restricted to placental mammals. Many AID/APOBEC family members exhibit cytidine deaminase activity on polynucleotides, although in different physiological contexts.

2005), suggesting that the in vivo action of UNG may differ from what we know about structure–function of UNG as purified molecule. Most importantly, the complete rescue of CSR by loss‐of‐catalytic‐function mutants certainly indicates that the CSR reduction in UNG‐deficient mice is not due to loss of U removal activity, but to loss of an as‐yet‐unknown activity of UNG. 2. Replication‐Coupling Motifs of UNG Are Dispensable for CSR Structurally, both human and mouse full‐length UNG show similar architecture: a short, nonstructural N‐terminal domain comprising $1/3 of the total amino acid length, and a core catalytic domain comprising 1/2 of the length of the protein.

And Krokan, H. E. (2004). Repair of U/G and U/A in DNA by UNG2‐associated repair complexes takes place predominantly by short‐patch repair both in proliferating and growth‐arrested cells. Nucleic Acids Res. 32, 5486–5498. Allen, R. , Armitage, R. , Conley, M. , Jenkins, N. , Copeland, N. , Bedell, M. , Disteche, C. , Simoneaux, D. , Fanslow, W. , et al. (1993). CD40 ligand gene defects responsible for X‐linked hyper‐IgM syndrome. Science 259, 990–993. , and Koonin, E. V. (2000). The a/b fold uracil DNA glycosylases: A common origin with diverse fates.

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AID for Immunoglobulin Diversity by Frederick W. Alt


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