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Coronaviruses /

Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Ziebuhr, John (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Cambridge, MA : Academic Press, �2016.
Colección:Advances in virus research ; v. 96.
Temas:
Acceso en línea:Texto completo
Tabla de Contenidos:
  • Front Cover; Coronaviruses; Copyright; In Memoriam; Contents; Contributors; Preface; Chapter One: Supramolecular Architecture of the Coronavirus Particle; 1. Introduction; 2. Virion Structure and Durability; 3. Viral Proteins in Assembly and Fusion; 3.1. Membrane Protein; 3.2. Nucleoprotein; 3.3. Envelope Protein; 3.4. Spike Protein; 4. Evolution of the Structural Proteins; References; Chapter Two: Coronavirus Spike Protein and Tropism Changes; 1. Introduction; 2. Structure of the Coronavirus S Protein; 2.1. Structure of the S1 Subunit; 2.2. Structure of the S2 Subunit.
  • 3. Spike-Receptor Interactions3.1. Different Domains Within S1 May Act as RBD; 3.2. CoV Protein Receptor Preference; 4. S Protein Proteolytic Cleavage and Conformational Changes; 5. Tropism Changes Associated with S Protein Mutations; 5.1. S1 Receptor Interactions Determining Tropism; 5.1.1. S1 NTR Changes; 5.1.2. S1 CTR Changes; 5.2. Changes in Proteolytic Cleavage Site and Other S2 Mutations Associated with Altered Tropism; 5.2.1. Changes in Proteolytic Cleavage Sites; 5.2.2. Other S2 Mutations Associated with Altered Tropism; 6. Concluding Remarks; Acknowledgments; References.
  • Chapter Three: The Nonstructural Proteins Directing Coronavirus RNA Synthesis and Processing1. Introduction; 2. Coronavirus nsp7-10: Small but Critical Regulatory Subunits?; 2.1. Coronavirus nsp7; 2.2. Coronavirus nsp8 and nsp7-nsp8 Complexes; 2.3. Coronavirus nsp9; 2.4. Coronavirus nsp10; 3. Coronavirus nsp12: A Multidomain RNA Polymerase; 3.1. The nsp12 RdRp Domain; 3.2. The Initiation Mechanism of the nsp12 RdRp; 3.3. Inhibitors of the nsp12 RdRp; 3.4. The nsp12 NiRAN Domain; 4. Coronavirus nsp13: A Multifunctional and Highly Conserved Helicase Subunit.
  • 4.1. The Coronavirus nsp13 SF1 Helicase (HEL1)4.2. The Helicase-Associated ZBD; 4.3. Nidovirus Helicase Structural Biology; 4.4. Functional Characterization of the Nidovirus Helicase; 4.5. The Coronavirus Helicase as Drug Target; 5. The Coronavirus Capping Machinery: nsp10-13-14-16; 5.1. The nsp13 RNA 5' Triphosphatase; 5.2. The Elusive RNA GTase; 5.3. The nsp14 N7-Methyl Transferase; 5.4. The nsp16 2'-O-Methyl Transferase; 6. Coronavirus nsp14 ExoN: Key to a Unique Mismatch Repair Mechanism That Promotes Fidelity; 7. Coronavirus nsp15: A Remarkable Endoribonuclease with Elusive Functions.
  • 8. Summary and Future PerspectivesAcknowledgments; References; Chapter Four: Coronavirus cis-Acting RNA Elements; 1. Introduction; 2. Coronavirus Genome Replication and Transcription; 3. Coronavirus cis-Acting RNA Elements; 3.1. 5-Terminal cis-Acting RNA Elements; 3.1.1. Structural Features of Coronavirus 5'-Terminal cis-Acting Elements; 3.1.2. Functional Roles of Coronavirus 5'-Terminal cis-Acting Elements; 3.1.2.1. Stem-Loops 1 and 2; 3.1.2.2. Stem-Loop 3; 3.1.2.3. Stem-Loop 4; 3.1.2.4. Stem-Loop 5; 3.2. 3'-Terminal cis-Acting RNA Elements.