Front Cover -- Progress in Molecular Biology and Translational Science -- Copyright -- Contents -- Contributors -- Preface -- Chapter One: Targeting the Recently Deorphanized Receptor GPR83 for the Treatment of Immunological, Neuroendocrine and Ne ... -- 1. Introduction -- 1.1. Discovery of GPR83 -- 1.2. Discovery of proSAAS and the Signaling Peptide PEN -- 1.3. ProSAAS Expression and Function -- 2. Expression and Significance of GPR83 in the Brain -- 2.1. Expression of GPR83 in the Mouse Brain -- 2.2. Differential GPR83 Expression Between Mouse, Rat and Human -- 2.3. Regulation of GPR83 Expression in the Brain -- 2.4. Role of GPR83 in Hypothalamic Function -- 2.5. Role of GPR83 in Stress, Reward and Learning and Memory -- 3. Role of GPR83 in Immune Function -- 3.1. Expression of GPR83 in Immune Cells -- 3.2. Significance of GPR83 in Immune Function -- 4. Current Understanding of GPR83 and PEN -- 4.1. The Deorphanization of GPR83 -- 5. Conclusions -- 5.1. Relationship Between GPR83, Stress, Reward, and Immune Function: Future Research Considerations -- 5.2. The GPR83-PEN Neuropeptide System as a Novel Therapeutic Drug Target -- 5.3. Summary -- Acknowledgment -- References -- Chapter Two: Arrestins in the Cardiovascular System: An Update -- 1. Introduction -- 2. Cardiovascular Adrenergic Receptors and ßarrestins -- 2.1. Cardiovascular αARs and ßarrestins -- 2.2. Cardiac ßARs and ßarrestins -- 2.3. Other Cardiovascular ßARs and ßarrestins -- 3. Cardiovascular Angiotensin II Receptors and ßarrestins -- 3.1. Cardiac AT1Rs and ßarrestins -- 3.2. Vascular AT1Rs and ßarrestins -- 3.3. Adrenal AT1Rs and ßarrestins -- 4. Other Cardiovascular GPCRs and ßarrestins -- 4.1. Endothelin Receptors -- 4.2. Vasopressin Receptors -- 4.3. Niacin Receptor (GPR109A) -- 4.4. P2Y Receptors -- 4.5. Protease-Activated Receptors -- 4.6. Apelin Receptor.

4.7. Sphingosine-1-Phosphate 1 Receptor -- 5. Therapeutic Implications of the Functional Divergence of Cardiovascular ßarrestins -- 6. Conclusions and Future Perspectives -- References -- Chapter Three: Global Aquatic Hazard Assessment of Ciprofloxacin: Exceedances of Antibiotic Resistance Development and Ec ... -- 1. Background -- 2. Materials and Methods -- 2.1. Literature Review -- 2.2. Probabilistic Aquatic Hazard Assessments -- 3. Results and Discussion -- 3.1. Ciprofloxacin in Municipal and Hospital Sewage and Effluent Discharges -- 3.2. Ciprofloxacin in Freshwater, Marine Systems and Groundwater -- 4. Conclusions -- References -- Chapter Four: Group I Intron-Based Therapeutics Through Trans-Splicing Reaction -- 1. Introduction -- 2. Group I Intron -- 2.1. Self-Splicing Activity of Group I Intron -- 2.2. Development of Trans-Splicing Group I Ribozyme -- 3. Group I Intron as Therapeutics -- 3.1. Trans-Splicing Ribozyme for RNA Repair -- 3.2. Trans-Splicing Ribozyme for RNA Reprogramming -- 4. Concluding Remarks -- Acknowledgments -- References -- Chapter Five: Major 3′-5′ Exoribonucleases in the Metabolism of Coding and Non-coding RNA -- 1. Introduction -- 2. Polynucleotide Phosphorylase -- 2.1. PNPase Function and Regulation -- 2.1.1. PNPase Activity on RNA -- 2.1.2. PNPase Activity on DNA -- 2.1.3. Regulation of PNPase Activity -- 2.1.4. Regulation of PNPase Expression -- 2.2. PNPase Complexes -- 2.3. PNPase Structure -- 2.4. PNPase Substrates -- 2.4.1. PNPase in the Metabolism of Coding RNA -- 2.4.2. PNPase in the Metabolism of Non-coding RNA -- 2.4.3. PNPase in Eukaryotes -- 2.4.4. PNPase in Pathogenesis and Disease -- 3. RNase II -- 3.1. RNase II Function and Regulation -- 3.1.1. RNase II Activity on RNA -- 3.1.2. Regulation of RNase II Activity -- 3.1.3. Regulation of RNase II Expression -- 3.1.4. RNase II Complexes.

3.2. RNase II Structure -- 3.3. RNase II Substrates -- 3.3.1. RNase II in the Metabolism of Coding RNA -- 3.3.2. RNase II in the Metabolism of Non-coding RNA -- 4. RNase R -- 4.1. RNase R Function and Regulation -- 4.1.1. RNase R Activity on RNA -- 4.1.2. Regulation of RNase R Stability -- 4.1.3. RNase R Complexes -- 4.2. RNase R Structure -- 4.3. RNase R Substrates -- 4.3.1. RNase R in the Metabolism of Coding RNA -- 4.3.2. RNase R in the Metabolism of Non-coding RNA -- 4.4. RNase II/RNase R in Eukaryotes -- 4.5. RNase II/RNase R Family Members in Pathogenesis and Disease -- 5. Concluding Remarks -- Acknowledgments -- References -- Chapter Six: Different Methods of Delivering CRISPR/Cas9 Into Cells -- 1. Introduction -- 1.1. Programmable Nucleases -- 1.2. Genome Silencing vs Genome Editing -- 1.3. Advantages of CRISPR Over ZFN and TALEN -- 2. Delivery Methods of CRISPR/Cas9 for Genome Editing -- 2.1. Viral-Mediated Delivery -- 2.1.1. Adeno-Associated Viral Vector-Mediated Delivery -- 2.1.2. Lentiviral Vector-Mediated Delivery -- 2.1.3. Adenovirus-Mediated Delivery -- 2.2. Non-viral Vectors -- 2.2.1. Cationic Vectors -- 2.2.2. Cell-Penetrating Peptides -- 2.2.3. Other Non-viral Methods -- 2.3. Physical Methods -- 3. Opportunities and Challenges in CRISPR/Cas9 Delivery to Stem Cells -- 4. Conclusions and Future Perspectives -- Acknowledgments -- References -- Chapter Seven: Structural Simplicity and Mechanistic Complexity in the Hammerhead Ribozyme -- 1. Background and Structural Overview -- 2. Fast Minimal Hammerhead Ribozymes -- 3. Acid-Base Catalysis and the Hammerhead Ribozyme -- 4. Is the Hammerhead Ligation Reaction the Reverse of the Cleavage Reaction? -- 5. Do Cooperative Interactions in the Hammerhead Ribozyme Facilitate General Base Catalysis in the Cleavage Reaction? -- 6. Summary and Concluding Remarks.

6.1. The Structure of the Hammerhead Ribozyme May Be Much Simpler Than We Have Thought -- 6.2. The Mechanism of the Hammerhead Ribozyme May Be Much More Complicated Than We Have Thought -- 6.2.1. The Ligation Reaction Mechanism Might Not Be the Reverse of the Cleavage Mechanism -- 6.2.2. General Base Catalysis in the Cleavage Reaction Mechanism Might Be More Complex -- 6.3. Concluding Remarks -- References -- Index -- Back Cover.