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International Review of Cell and Molecular Biology. Vol. 308 /
International Review of Cell and Molecular Biology presents comprehensive reviews and current advances in cell and molecular biology. Articles address structure and control of gene expression, nucleocytoplasmic interactions, control of cell development and differentiation, and cell transformation an...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
Burlington :
Elsevier Science,
2014.
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| Temas: | |
| Acceso en línea: | Texto completo Texto completo |
Tabla de Contenidos:
- Front Cover; International Review of Cell and Molecular Biology; Copyright; Contents; Contributors; Chapter One: Structure and Function of POTRA Domains of Omp85/TPS Superfamily; 1. Introduction; 1.1. Omp85/TPS superfamily in gram-negative bacteria; 1.2. Omp85/TPS superfamily in organelles; 1.2.1. Sam50/Tob55, a mitochondrial homolog of bacterial Omp85; 1.2.2. Toc75, a plastid homolog of bacterial Omp85; 2. Omp85/TPS Superfamily Architecture; 2.1. Highly conserved C-terminal [beta]-barrel domain; 2.2. Soluble N-terminus, containing POTRA domains; 3. Function of Omp85 Family of Proteins.
- 3.1. Role of Omp85 pore3.2. Role of POTRA domains; 4. Functions of Two-Partner Secretion B Proteins; 4.1. Role of TpsB pore; 4.2. Role of POTRA domains of TpsB; 4.2.1. FhaC; 5. Phototrophic Members of Omp85/TPS; 5.1. Cyanobacterial members of Omp85/TPS superfamily; 5.1.1. Omp85 of Nostoc sp. PCC 7120; 5.1.2. Omp85 of T. elongatus; 5.2. Chloroplast members of Omp85/TPS superfamily; 5.2.1. Toc75, a plastidic outer-membrane protein of Omp85/TPS superfamily; 5.2.2. Oep80, a chloroplastic paralog of Toc75; 5.3. Unique features of phototrophic Omp85 POTRA domains; 6. POTRA Domains Mode of Action.
- 6.1. Role and model of action for individual POTRA domains6.2. Models of POTRA interaction with peptide substrates; 6.2.1. MHC class I; 6.2.2. Hsp70/DnaK; 6.2.3. PDZ domains; 7. Concluding Remarks; References; Chapter Two: Molecular Cell Biology and Immunobiology of Mammalian Rod/Ring Structures; 1. Introduction; 2. Conserved RR Structures Across Species; 2.1. Nematin in mammalian cells; 2.2. IMPDH filaments induced by MPA in mammalian cells; 2.3. Drosophila cytoophidia-CTPS filaments; 2.4. Rod-like filaments in Saccharomyces cerevisiae; 2.5. CTPS filaments in Caulobacter crescentus.
- 2.6. Loukoumasomes in rat sympathetic neurons3. Known Components of RR; 3.1. Cytidine triphosphate synthetase; 3.2. Inosine monophosphate dehydrogenase; 3.3. Other candidate components; 3.3.1. Nucleotide biosynthetic enzymes; 3.3.2. RR candidate proteins from microarray screening; 3.3.3. Methods in RR component identification; 4. Biological Function of RR; 4.1. Nucleotide biosynthesis associated with RR; 4.2. Rod versus ring configurations; 4.3. Induced versus native RR; 4.4. Cytoplasmic versus nuclear rods; 4.5. Technical difficulties in rod/ring detection.
- 5. Immunobiology of RR-Autoimmune Response5.1. Autoantibodies in rheumatic diseases as cellular and molecular probes; 5.2. Anti-RR and chronic HCV infection and therapy; 5.2.1. Molecular structure and interactions with HCV; 5.2.2. HCV and autoantibodies; 5.3. Autoimmune response to rod/ring structures in HCV infection; 5.4. Clinical implications of anti-rods/rings autoantibodies; 5.4.1. Ribavirin as a therapeutic agent; 5.4.2. MPA as a therapeutic agent; 6. Concluding Remarks and Future Perspectives; Acknowledgments; References.