Dr Ester Boix is leading the research group on ‘Human host defense RNases’ at the Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain. After five years of postdoctoral studies (one year at the National Institutes of Health and four years at the University of Bath) in 2002 she was called to the Ramon y Cajal program as a Senior Research Fellow. Over her career she has contributed to the structural-functional characterization of ribonucleases. She is a pioneer in the development of novel expression systems for RNases’ production, the first 3D crystal structures, identification of secondary substrate binding sites and design of novel RNase- based antimicrobial peptides. Dr Boix has published over 90 papers and her main research interest focuses on the mechanism of action of RNases, as lead proteins for the design of novel therapies.

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• Section I: Structure1. Overview. RNases, a family of multifaceted proteins2. Catalytic mechanism of action: mechanism, exonucleases vs endonucleases, single stranded vs double stranded.3. RNases diversity: vertebrate RNase A superfamily, RNase T2, RNase L, RNase kappa, plant RNase S, bacterial RNases4. RNase in evolution: RNAs and RNases5. RNA subsite binding sites6. From monomers to multimers7. RNases cellular traffic8. RNases and tyrosine kinase receptors9. RNases and posttranscriptional modifications10. RNases targeting non-coding RNAs11. RNase InhibitorsSection II: Research Methods12. Tools to study RNases:a) labelled probesb) HPLC product analysis,c) Cp-RNAseq…13. RNase-based tools: RNaseH, RNAse4 for RNA analysis,…CRISPR/Cas9Section III: Diseases14. RNases in infectious diseases15. RNases in inflammatory disorders16. RNases in cancer17. Human Natural Variants18. RNases as diagnostic tools19. RNases as therapeutic targets20. RNases and drug design: antitumoral, anti-inflammatory or antimicrobial agents

Dr Ester Boix is leading the research group on ‘Human host defense RNases’ at the Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain. After five years of postdoctoral studies (one year at the National Institutes of Health and four years at the University of Bath) in 2002 she was called to the Ramon y Cajal program as a Senior Research Fellow. Over her career she has contributed to the structural-functional characterization of ribonucleases. She is a pioneer in the development of novel expression systems for RNases’ production, the first 3D crystal structures, identification of secondary substrate binding sites and design of novel RNase- based antimicrobial peptides. Dr Boix has published over 90 papers and her main research interest focuses on the mechanism of action of RNases, as lead proteins for the design of novel therapies.

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• Section I: Structure1. Overview. RNases, a family of multifaceted proteins2. Catalytic mechanism of action: mechanism, exonucleases vs endonucleases, single stranded vs double stranded.3. RNases diversity: vertebrate RNase A superfamily, RNase T2, RNase L, RNase kappa, plant RNase S, bacterial RNases4. RNase in evolution: RNAs and RNases5. RNA subsite binding sites6. From monomers to multimers7. RNases cellular traffic8. RNases and tyrosine kinase receptors9. RNases and posttranscriptional modifications10. RNases targeting non-coding RNAs11. RNase InhibitorsSection II: Research Methods12. Tools to study RNases:a) labelled probesb) HPLC product analysis,c) Cp-RNAseq…13. RNase-based tools: RNaseH, RNAse4 for RNA analysis,…CRISPR/Cas9Section III: Diseases14. RNases in infectious diseases15. RNases in inflammatory disorders16. RNases in cancer17. Human Natural Variants18. RNases as diagnostic tools19. RNases as therapeutic targets20. RNases and drug design: antitumoral, anti-inflammatory or antimicrobial agents

Dr Ester Boix is leading the research group on ‘Human host defense RNases’ at the Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain. After five years of postdoctoral studies (one year at the National Institutes of Health and four years at the University of Bath) in 2002 she was called to the Ramon y Cajal program as a Senior Research Fellow. Over her career she has contributed to the structural-functional characterization of ribonucleases. She is a pioneer in the development of novel expression systems for RNases’ production, the first 3D crystal structures, identification of secondary substrate binding sites and design of novel RNase- based antimicrobial peptides. Dr Boix has published over 90 papers and her main research interest focuses on the mechanism of action of RNases, as lead proteins for the design of novel therapies.

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• Section I: Structure1. Overview. RNases, a family of multifaceted proteins2. Catalytic mechanism of action: mechanism, exonucleases vs endonucleases, single stranded vs double stranded.3. RNases diversity: vertebrate RNase A superfamily, RNase T2, RNase L, RNase kappa, plant RNase S, bacterial RNases4. RNase in evolution: RNAs and RNases5. RNA subsite binding sites6. From monomers to multimers7. RNases cellular traffic8. RNases and tyrosine kinase receptors9. RNases and posttranscriptional modifications10. RNases targeting non-coding RNAs11. RNase InhibitorsSection II: Research Methods12. Tools to study RNases:a) labelled probesb) HPLC product analysis,c) Cp-RNAseq…13. RNase-based tools: RNaseH, RNAse4 for RNA analysis,…CRISPR/Cas9Section III: Diseases14. RNases in infectious diseases15. RNases in inflammatory disorders16. RNases in cancer17. Human Natural Variants18. RNases as diagnostic tools19. RNases as therapeutic targets20. RNases and drug design: antitumoral, anti-inflammatory or antimicrobial agents