Adenosine Deaminases Acting on RNA (ADARs) and A-to-I Editing (Current Topics in Microbiology and Immunology, Vol. 353)

“The objective of this CTMI volume is to provide readers with a foundation for understanding what ADARs are and how they act to affect gene expression and function. It is becoming increasingly apparent that ADARs may possess roles not only as enzymes that deaminate adenosine to produce inosine in RNA substrates with double-stranded character, but also as proteins independent of their catalytic property. Because A-to-I editing may affect base-pairing and RNA structure, processes including translation, splicing, RNA replication, and miR and siRNA silencing may be affected. Future studies of ADARs no doubt will provide us with additional surprises and new insights into the modulation of biological processes by the ADAR family of proteins.” Adar Proteins : Structure And Catalytic Mechanism / Rena A. Goodman, Mark R. Macbeth And Peter A. Beal -- Adar Proteins : Double-stranded Rna And Z-dna Binding Domains / Pierre Barraud And Frédéric H.-t. Allain -- Editing Of Neurotransmitter Receptor And Ion Channel Rnas In The Nervous System / Jennifer L. Hood And Ronald B. Emeson -- Modulation Of Microrna Expression And Function By Adars / Bjorn-erik Wulff And Kazuko Nishikura -- Nuclear Editing Of Mrna 3'-utrs / Ling-ling Chen And Gordon G. Carmichael -- Control Of Adar1 Editing Of Hepatitis Delta Virus Rnas / John L. Casey -- Bioinformatic Approaches For Identification Of A-to-i Editing Sites / Eli Eisenberg -- Adars : Viruses And Innate Immunity / Charles E. Samuel -- Role Of Adars In Mouse Development / Carl R. Walkley, Brian Liddicoat And Jochen C. Hartner -- Regulation And Functions Of Adar In Drosophila / Simona Paro, Xianghua Li, Mary A. O'connell And Liam P. Keegan. Charles E. Samuel, Editor. Includes Bibliographical References And Index. “The objective of this __CTMI__ volume is to provide readers with a foundation for understanding what ADARs are and how they act to affect gene expression and function. It is becoming increasingly apparent that ADARs may possess roles not only as enzymes that deaminate adenosine to produce inosine in RNA substrates with double-stranded character, but also as proteins independent of their catalytic property. Because A-to-I editing may affect base-pairing and RNA structure, processes including translation, splicing, RNA replication, and miR and siRNA silencing may be affected. Future studies of ADARs no doubt will provide us with additional surprises and new insights into the modulation of biological processes by the ADAR family of proteins.” The objective of this CTMI volume is to provide readers with a foundation for understanding what ADARs are and how they act to affect gene expression and function. Because A-to-I editing may affect base-pairing and RNA structure, processes including translation, splicing, RNA replication, and miR and siRNA silencing may be affected.¡ It also is becoming increasingly apparent that ADARs may possess roles not only as enzymes that deaminate adenosine to produce inosine in RNA substrates with double-stranded character, but also as proteins independent of their catalytic property. Future studies of ADARs no doubt will provide us with additional surprises and new insights into the modulation of biological processes by the ADAR family of proteins Front Matter....Pages i-x ADAR Proteins: Structure and Catalytic Mechanism....Pages 1-33 ADAR Proteins: Double-stranded RNA and Z-DNA Binding Domains....Pages 35-60 Editing of Neurotransmitter Receptor and Ion Channel RNAs in the Nervous System....Pages 61-90 Modulation of MicroRNA Expression and Function by ADARs....Pages 91-109 Nuclear Editing of mRNA 3′-UTRs....Pages 111-121 Control of ADAR1 Editing of Hepatitis Delta Virus RNAs....Pages 123-143 Bioinformatic Approaches for Identification of A-to-I Editing Sites....Pages 145-162 ADARs: Viruses and Innate Immunity....Pages 163-195 Role of ADARs in Mouse Development....Pages 197-220 Regulation and Functions of ADAR in Drosophila ....Pages 221-236 Back Matter....Pages 237-238