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PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin
| PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin |
| Edizione | [3rd ed.] |
| Pubbl/distr/stampa | Boca Raton : , : Taylor & Francis, , 2013 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina | 572.8/636 |
| Altri autori (Persone) |
NolanTania
BustinStephen A. <1954-> |
| Soggetto topico |
DNA polymerases
Transferases |
| Soggetto genere / forma | Electronic books. |
| ISBN |
0-429-11045-6
1-4398-4813-0 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | pt. 1. Template preparation -- pt. 2. Reaction components -- pt. 3. Instruments -- pt. 4. Design, optimization, QC, and standardization -- pt. 5. Data analysis -- pt. 6. Applications. |
| Record Nr. | UNINA-9910463255903321 |
| Boca Raton : , : Taylor & Francis, , 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin
| PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin |
| Edizione | [3rd ed.] |
| Pubbl/distr/stampa | Boca Raton : , : Taylor & Francis, , 2013 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina | 572.8/636 |
| Altri autori (Persone) |
NolanTania
BustinStephen A. <1954-> |
| Soggetto topico |
DNA polymerases
Transferases |
| ISBN |
0-429-11045-6
1-4398-4813-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | pt. 1. Template preparation -- pt. 2. Reaction components -- pt. 3. Instruments -- pt. 4. Design, optimization, QC, and standardization -- pt. 5. Data analysis -- pt. 6. Applications. |
| Record Nr. | UNINA-9910786960003321 |
| Boca Raton : , : Taylor & Francis, , 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin
| PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin |
| Edizione | [3rd ed.] |
| Pubbl/distr/stampa | Boca Raton : , : Taylor & Francis, , 2013 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina | 572.8/636 |
| Altri autori (Persone) |
NolanTania
BustinStephen A. <1954-> |
| Soggetto topico |
DNA polymerases
Transferases |
| ISBN |
0-429-11045-6
1-4398-4813-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | pt. 1. Template preparation -- pt. 2. Reaction components -- pt. 3. Instruments -- pt. 4. Design, optimization, QC, and standardization -- pt. 5. Data analysis -- pt. 6. Applications. |
| Record Nr. | UNINA-9910800200003321 |
| Boca Raton : , : Taylor & Francis, , 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin
| PCR technology : current innovations / / edited by Tania Nolan, Stephen A. Bustin |
| Edizione | [3rd ed.] |
| Pubbl/distr/stampa | Boca Raton, Fla., : CRC Press, 2013 |
| Descrizione fisica | 1 online resource (457 p.) |
| Disciplina | 572.8/636 |
| Altri autori (Persone) |
NolanTania
BustinStephen A. <1954-> |
| Soggetto topico |
DNA polymerases
Transferases |
| ISBN |
0-429-11045-6
1-4398-4813-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | pt. 1. Template preparation -- pt. 2. Reaction components -- pt. 3. Instruments -- pt. 4. Design, optimization, QC, and standardization -- pt. 5. Data analysis -- pt. 6. Applications. |
| Record Nr. | UNINA-9910825871003321 |
| Boca Raton, Fla., : CRC Press, 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Springer handbook of enzymes . Supplement, Volume S9 Class 2-3.2 transferases, hydrolases : EC 2-3.2 / / Dietmar Schomburg, Ida Schomburg (eds.); co-edited by Antje Chang
| Springer handbook of enzymes . Supplement, Volume S9 Class 2-3.2 transferases, hydrolases : EC 2-3.2 / / Dietmar Schomburg, Ida Schomburg (eds.); co-edited by Antje Chang |
| Edizione | [2nd ed.] |
| Pubbl/distr/stampa | Berlin ; ; Heidleberg, : Springer-Verlag, 2013 |
| Descrizione fisica | 1 online resource (698 p.) |
| Disciplina |
572.7
572.792 572/.792 |
| Altri autori (Persone) |
SchomburgD (Dietmar)
SchomburgIda <1954-> ChangAntje |
| Collana | Springer Handbook of Enzymes |
| Soggetto topico |
Transferases
Hydrolases |
| ISBN | 3-642-36240-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | 2.1.1.163 demethylmenaquinone methyltransferase -- 2.1.1.164 demethylrebeccamycin-D-glucose Omethyltransferase -- 2.1.1.165 methyl halide transferase -- 2.1.1.166 23S rRNA (uridine2552-2’-O-)-methyltransferase -- 2.1.1.167 27S pre-rRNA (guanosine2922-2’-O)-methyltransferase -- 2.1.1.168 21S rRNA (uridine2791-2’-O)-methyltransferase -- 2.1.1.169 tricetin 3’,4’,5’-O-trimethyltransferase -- 2.1.1.170 16S rRNA (guanine527-N7)-methyltransferase -- 2.1.1.171 16S rRNA (guanine966-N2)-methyltransferase -- 2.1.1.172 16S rRNA (guanine1207-N2)-methyltransferase -- 2.1.1.173 23S rRNA (guanine2445-N2)-methyltransferase -- 2.1.1.174 23S rRNA (guanine1835-N2)-methyltransferase -- 2.1.1.175 tricin synthase -- 2.1.1.176 16S rRNA (cytosine967-C5)-methyltransferase -- 2.1.1.177 23S rRNA (pseudouridine1915-N3)-methyltransferase -- 2.1.1.178 16S rRNA (cytosine1407-C5)-methyltransferase -- 2.1.1.179 16S rRNA (guanine1405-N7)-methyltransferase -- 2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferase -- 2.1.1.181 23S rRNA (adenine1618-N6)-methyltransferase -- 2.1.1.182 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase -- 2.1.1.183 18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase -- 2.1.1.184 23S rRNA (adenine2085-N6)- dimethyltransferase -- 2.1.1.185 23S rRNA (guanosine2251-2’-O-)- methyltransferase -- 2.1.1.186 23S rRNA (cytidine2498-2’-O)-methyltransferase -- 2.1.1.195 cobalt-precorrin-5B (C1)-methyltransferase -- 2.1.1.196 cobalt-precorrin-7 (C15)-methyltransferase[decarboxylating] -- 2.1.1.197 malonyl-CoA O-methyltransferase -- 2.1.1.198 16S rRNA (cytidine1402-2’-O)-methyltransferase -- 2.1.1.199 16S rRNA (cytosine1402-N4)-methyltransferase -- 2.1.2.13 UDP-4-amino-4-deoxy-L-arabinose formyltransferase -- 2.1.3.10 malonyl-S-ACP:biotin-protein carboxyltransferase:- 2.1.3.11 N-succinylornithine carbamoyltransferase -- 2.2.1.9 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase -- 2.3.1.185 tropine acyltransferase -- 2.3.1.186 pseudotropine acyltransferase -- 2.3.1.187 acetyl-S-ACP:malonate ACP transferase -- 2.3.1.188 w-hydroxypalmitate O-feruloyl transferase -- 2.3.1.189 mycothiol synthase -- 2.3.1.190 acetoin dehydrogenase -- 2.3.1.191 UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase -- 2.3.1.192 glycine N-phenylacetyltransferase -- 2.3.2.16 lipid II:glycine glycyltransferase -- 2.3.2.17 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-glycyl)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine glycyltransferase -- 2.3.2.18 N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl- (N6-triglycine)-D-alanyl-D-alaninediphosphoundecaprenyl-Nacetylglucosamine: glycine lycyltransferase -- 2.4.1.245 a,a-trehalose synthase -- 2.4.1.247 b-D-galactosyl-(1!4)-L-rhamnose phosphorylase -- 2.4.1.248 cycloisomaltooligosaccharide glucanotransferase -- 2.4.1.249 delphinidin 3’,5’-O-glucosyltransferase -- 2.4.1.250 D-inositol-3-phosphate glycosyltransferase -- 2.4.1.251 GlcA-b-(1!2)-D-Man-a-(1!3)-D-Glc-b- (1!4)-D-Glc-a-1-diphospho-ditrans,octacisundecaprenol 4-b-mannosyltransferase -- 2.4.1.252 GDP-mannose:cellobiosyldiphosphopolyprenol a-mannosyltransferase -- 2.4.1.253 baicalein 7-O-glucuronosyltransferase -- 2.4.2.41 xylogalacturonan b-1,3-xylosyltransferase -- 2.4.2.42 UDP-D-xylose:b-D-glucoside a-1,3-Dxylosyltransferase -- 2.4.2.43 lipid IVA 4-amino-4-deoxy-Larabinosyltransferase -- 2.4.99.12 lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.13 (KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase -- 2.4.99.14 (KDO)2-lipid IVA (2-8) 3-deoxy-D-mannooctulosonic acid transferase -- 2.4.99.15 (KDO)3-lipid IVA (2-4) 3-deoxy-D-mannooctulosonic acid transferase -- 2.5.1.72 quinolinate synthase -- 2.5.1.73 O-phospho-L-seryl-tRNA:Cys-tRNA synthase -- 2.5.1.74 1,4-dihydroxy-2-naphthoate polyprenyltransferase -- 2.5.1.75 tRNA dimethylallyltransferase -- 2.5.1.76 cysteate synthase -- 2.5.1.77 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase -- 2.5.1.78 6,7-dimethyl-8-ribityllumazine synthase -- 2.5.1.79 thermospermine synthase -- 2.5.1.80 7-dimethylallyltryptophan synthase -- 2.5.1.81 geranylfarnesyl diphosphate synthase -- 2.5.1.82 hexaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.83 hexaprenyl-diphosphate synthase [(2E,6E)- farnesyl-diphosphate specific] -- 2.5.1.84 all-trans-nonaprenyl-diphosphate synthase [geranyl-diphosphate specific] -- 2.5.1.85 all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.86 trans,polycis-decaprenyl diphosphate Synthase -- 2.5.1.87 ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] -- 2.5.1.88 trans,polycis-polyprenyl diphosphate synthase [(2Z,6E)-farnesyl diphosphate specific] -- 2.5.1.89 tritrans,polycis-undecaprenyl-diphosphate synthase [geranylgeranyl-diphosphate specific] -- 2.5.1.93 4-hydroxybenzoate geranyltransferase -- 2.5.1.94 adenosyl-chloride synthase -- 2.6.1.86 2-amino-4-deoxychorismate synthase -- 2.6.1.87 UDP-4-amino-4-deoxy-L-arabinose aminotransferase -- 2.7.1.161 CTP-dependent riboflavin kinase -- 2.7.1.162 N-acetylhexosamine 1-kinase -- 2.7.1.163 hygromycin B 4-O-kinase -- 2.7.1.164 O-phosphoseryl-tRNASec kinase -- 2.7.1.165 glycerate 2-kinase -- 2.7.1.166 3-deoxy-D-manno-octulosonic acid kinase -- 2.7.1.167 D-glycero-b-D-manno-heptose-7-phosphate kinase -- 2.7.1.168 D-glycero-a-D-manno-heptose-7-phosphate kinase -- 2.7.1.169 pantoate kinase -- 2.7.4.25 (d)CMP kinase -- 2.7.7.66 malonate decarboxylase holo-[acyl-carrier protein] synthase -- 2.7.7.67 CDP-archaeol synthase -- 2.7.7.68 2-phospho-L-lactate guanylyltransferase -- 2.7.7.70 D-glycero-b-D-manno-heptose 1-phosphate adenylyltransferase -- 2.7.7.71 D-glycero-a-D-manno-heptose 1-phosphate guanylyltransferase -- 2.7.7.72 CCA tRNA nucleotidyltransferase -- 2.7.8.28 2-phospho-L-lactate transferase -- 2.7.8.29 L-serine-phosphatidylethanolamine phosphatidyltransferase -- 2.7.8.30 undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase -- 2.7.8.31 undecaprenyl-phosphate glucose phosphotransferase -- 2.8.2.35 dermatan 4-sulfotransferase -- 2.8.4.2 arsenate-mycothiol transferase -- 2.9.1.2 O-phospho-L-seryl-tRNASec:L-selenocysteinyltRNA synthase -- 3.1.1.83 monoterpene e-lactone hydrolase -- 3.1.1.84 cocaine esterase -- 3.1.2.28 1,4-dihydroxy-2-naphthoyl-CoA hydrolase -- 3.1.3.78 phosphatidylinositol-4,5-bisphosphate 4-phosphatase -- 3.1.3.80 2,3-bisphosphoglycerate 3-phosphatase -- 3.1.3.81 diacylglycerol diphosphate phosphatase -- 3.1.3.82 -glycero-b-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.3.83 D-glycero-a-D-manno-heptose 1,7-bisphosphate 7-phosphatase -- 3.1.4.53 3’,5’-cyclic-AMP phosphodiesterase -- 3.1.7.4 sclareol cyclase -- 3.1.7.5 geranylgeranyl diphosphate diphosphatase -- 3.1.7.6 farnesyl diphosphatase -- 3.1.26.12 ribonuclease E -- 3.1.26.13 retroviral ribonuclease H -- 3.2.1.165 exo-1,4-b-D-glucosaminidase -- 3.2.1.167 baicalin-b-D-glucuronidase -- 3.2.1.168 hesperidin 6-O-a-L-rhamnosyl-b-Dglucosidase -- 3.2.2.27 uracil-DNA glycosylase -- 3.2.2.28 double-stranded uracil-DNA glycosylase -- 3.2.2.29 thymine-DNA glycosylase. |
| Record Nr. | UNINA-9910437616803321 |
| Berlin ; ; Heidleberg, : Springer-Verlag, 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Viral polymerases : structures, functions and roles as antiviral drug targets / / edited by Satya P. Gupta
| Viral polymerases : structures, functions and roles as antiviral drug targets / / edited by Satya P. Gupta |
| Pubbl/distr/stampa | London, United Kingdom : , : Academic Press, An imprint of Elsevier, , [2019] |
| Descrizione fisica | 1 online resource (498 pages) |
| Disciplina | 616.925061 |
| Soggetto topico |
Antiviral agents
Transferases |
| ISBN |
0-12-815423-3
0-12-815422-5 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Front Cover -- Viral Polymerases -- Copyright Page -- Contents -- List of Contributors -- Preface -- 1 RNA-Dependent RNA Polymerases and Their Emerging Roles in Antiviral Therapy -- 1.1 Introduction -- 1.2 RNA Polymerase -- 1.2.1 DNA-Dependent RNA Polymerases -- 1.2.2 RNA-Dependent RNA Polymerases -- 1.3 Structure of Viral RNA-Dependent RNA Polymerases -- 1.3.1 Structural Flexibility -- 1.3.2 Divalent Metal Ions -- 1.4 Mechanism of Enzyme Action -- 1.4.1 Two Metal Ion Mechanism -- 1.4.2 Initiation of RNA Synthesis -- 1.4.2.1 De Novo Initiation Mechanism -- 1.4.2.2 Primer-Dependent Initiation -- 1.5 Structures of Different Viral RdRPs -- 1.5.1 Hepatitis C Virus -- 1.5.2 Poliovirus -- 1.5.3 Influenza A Virus -- 1.5.3.1 Polymerase Basic 1 Subdomain -- 1.5.3.2 Polymerase Basic 2 Subdomain -- 1.5.3.3 Polymerase Acidic Subdomain -- 1.5.4 Dengue Virus -- 1.5.5 Zika Virus -- 1.5.6 Japanese Encephalitis Virus -- 1.5.7 Human Rhinoviruses -- 1.6 Enzyme-Ligand Interaction Strategies (Drug Design and Development) -- 1.7 Synthetic Inhibitors of RdRPs -- 1.7.1 Nucleoside Inhibitors -- 1.7.1.1 Purine Nucleoside Inhibitors -- 1.7.1.2 Pyrimidine Nucleoside Inhibitors -- 1.7.1.3 Miscellaneous Nucleoside Inhibitors -- 1.7.2 Nonnucleoside Inhibitors -- 1.7.2.1 Active Site Inhibitors -- 1.7.2.2 Allosteric Site Inhibitors -- 1.7.2.2.1 Anthranilic Acid Derivatives -- 1.7.2.2.2 Benzimidazole Derivatives -- 1.7.2.2.3 Benzothiadiazine Derivatives -- 1.7.2.2.4 Indole Derivatives -- 1.7.2.2.5 Proline Sulfonamide Derivatives -- 1.7.2.2.6 Pyrrolidine Diacid Derivatives -- 1.7.2.2.7 Pyridobenzothiazole Derivatives -- 1.7.2.3 Miscellaneous -- 1.8 Conclusion -- 1.9 Future Prospective -- References -- 2 Structure-Function Relationship of Negative-Stranded Viral RNA Polymerases: Prospectives for Antiviral Therapy -- 2.1 Introduction -- 2.2 Polyprotein Processing.
2.3 Genome Organization of Polymerase of segmented negative-strand RNA Viruses -- 2.4 Mechanism of Capping by RdRps -- 2.5 Structures of L-Proteins (Polymerases) -- 2.5.1 Structures of SNS RNA Virus L-Proteins (Polymerases) -- 2.5.1.1 La Crosse Orthobunyavirus RNA Polymerase (L-Protein) -- 2.5.1.2 Influenza Virus (H3N2) RNA Polymerase -- 2.5.1.3 Lymphocytic Choriomeningitis Virus RNA Polymerase (L-Protein) -- 2.5.1.4 Avian Influenza Virus (H5N1) RNA Polymerase -- 2.5.2 Structure of NNS RNA Virus L-Proteins (Polymerases) -- 2.6 Activity Assays -- 2.6.1 Mini-Replicon Assay -- 2.6.2 Nuclease Activity and Thermal Stability Assay -- 2.6.3 UV Cross-Linking Assays for Nucleotide Binding -- 2.6.4 Band Shift Assay for RNA Binding -- 2.6.5 Fluorescence-Based Assay -- 2.7 Inhibition Studies -- 2.7.1 Synergistic Action of Favipiravir and Ribavirin -- 2.7.2 Neutral Red Uptake Assay for Assessing Inhibition of Viral Replication by Antiviral Compounds -- 2.7.3 Negative-Strand Viral Replication Inhibition Through Gene Silencing approaches -- 2.7.4 Exploration of Antiviral Agents for Influenza in Clinical Trials -- 2.7.5 Targeting of Viral RNA in Eukaryotic Cells Through Cas9 -- 2.7.6 Novel Sugar-Modified Nucleosides Inhibitors Against Human RSV Polymerase -- 2.8 Conclusion -- References -- Further Reading -- 3 RNA-Dependent RNA Polymerase of Alphaviruses: A Potential Target for the Design of Drugs Against Alphaviruses -- 3.1 Introduction -- 3.2 Genome Structure -- 3.3 Viral Life Cycle -- 3.4 Replication Complexes in Alphavirus -- 3.5 Structure of RNA-Dependent RNA Polymerases -- 3.5.1 Divalent Metal Binding Site -- 3.5.2 Nucleotide Binding Site -- 3.6 Initiation of Replication -- 3.6.1 Primer-Independent Initiation -- 3.6.2 Primer-Dependent Initiation -- 3.7 Polymerase Activity of Alphaviral RdRP -- 3.7.1 Promoter Recognition by the Polymerase -- 3.7.1.1 5' end. 3.7.1.2 3' end -- 3.7.1.3 SG Promoter -- 3.7.2 Temperature Sensitivity of Polymerase -- 3.7.3 Fidelity of RdRP -- 3.8 Inhibitors Against Replication of Alphaviruses -- 3.9 Conclusions -- References -- 4 DNA-Dependent DNA Polymerases as Drug Targets in Herpesviruses and Poxviruses -- 4.1 Introduction -- 4.2 DNA Viruses: Mechanisms of Genomic DNA Replication -- 4.2.1 Bidirectional and Rolling Circle Replication -- 4.2.2 Single-Stranded DNA Formation Through Strand Displacement Replication -- 4.3 Herpesviruses -- 4.3.1 Types and Classification -- 4.3.2 Herpesvirus DNA Polymerase Structure -- 4.3.3 DNA Polymerase Properties: Processivity and Nucleotide Specificity -- 4.4 Antiviral Drugs Targeting Herpesvirus DNA Polymerases -- 4.4.1 Approved Drugs -- 4.4.2 Resistance to Approved Drugs Targeting Herpesvirus Replication -- 4.4.3 Drugs in Preclinical and Clinical Development -- 4.5 Poxviruses -- 4.5.1 Poxvirus DNA Polymerase -- 4.5.2 Drugs Targeting Poxvirus DNA Polymerases -- 4.6 Conclusions -- References -- 5 Poliovirus Polymerase: An Effective Target for Design and Development of Antipolio Drugs -- 5.1 Introduction -- 5.2 Poliovirus RNA-Dependent RNA Polymerase -- 5.2.1 Structure -- 5.2.1.1 The Palm Subdomain and Its Motifs -- 5.2.1.2 Fingers Subdomain -- 5.2.1.3 Thumb Subdomain -- 5.2.1.3.1 Roles of Subdomains -- 5.2.1.4 Metal Ions -- 5.2.2 Function -- 5.3 Isolation, Purification, and Characterization of Poliovirus RNA Polymerase -- 5.3.1 Isolation From HeLa cells -- 5.3.2 Recombinant Baculovirus Infected Insect Cells -- 5.3.3 Escherichia coli Transformed With an Expression Plasmid Containing 3Dpol Sequences -- 5.4 RNA-Dependent RNA Polymerase Inhibitors -- 5.5 Conclusions and Future Perspective -- References -- 6 Studies on HIV-1 Polymerase and Its Inhibitors -- 6.1 Introduction -- 6.2 Structure of Reverse Transcriptase. 6.3 Role and Mechanism of Action of HIV-1 RT -- 6.4 HIV-1 RT Inhibitors -- 6.5 Binding of NNRTIs With the Receptor -- 6.6 Theoretical Studies -- 6.7 RNH Inhibitors -- 6.8 HIV-1 Capsid and Its Role on Reverse Transcription Regulation and Control of Entry of RT Inhibitors -- 6.9 Conclusions -- References -- Further Reading -- 7 A Focus on Ebola Virus Polymerase: Structure, Functions and Antiviral Therapies -- 7.1 Introduction -- 7.1.1 History and Epidemiology -- 7.1.2 Transmission and Pathology -- 7.2 Structure and Genome -- 7.3 Replication -- 7.4 L-Protein -- 7.4.1 RNA-Dependent RNA Polymerase Domain -- 7.4.2 Capping Domain -- 7.4.3 Methyl Transferase Domain -- 7.4.4 Connector and C-Terminal Domains -- 7.4.5 Domain Organization -- 7.4.6 L-Protein in Virus Replication -- 7.5 Antiviral Strategies -- 7.5.1 Brincidofovir (CMX-001) -- 7.5.2 Lamivudine (BCH-189) -- 7.5.3 Favipiravir (T-705) -- 7.5.4 Immucillin A (BCX4430) -- 7.5.5 The FGI (Functional Genetics Inc.) Compounds -- 7.5.6 Neplanocin A (3-deazaneplanocin A) -- 7.5.7 Bioinformatics Approach to Drug Discovery -- 7.6 Ebola Vaccine -- 7.7 Conclusions -- References -- 8 Hepatitis C Virus NS5B RNA-Dependent RNA Polymerase Inhibitor: An Integral Part of HCV Antiviral Therapy -- 8.1 Introduction -- 8.2 The HCV Genome and Viral Replication -- 8.3 Development of HCV-Specific DAA drugs Targeting the NS3 Protease -- 8.4 Development of HCV-Specific DAA drugs Targeting NS5A -- 8.5 Structural and Functional Studies of HCV RNA Polymerase -- 8.6 Initiation of HCV Replication by NS5B Polymerase -- 8.7 Direct-Acting Antivirals Targeting the HCV RNA Polymerase -- 8.7.1 Nucleos(t)ide Inhibitors -- 8.7.2 Nonnucleos(t)ide Inhibitors -- 8.7.2.1 Thumb 1 inhibitors -- 8.7.2.2 Thumb 2 Inhibitors -- 8.7.2.3 Palm 1 Inhibitors -- 8.7.2.4 Palm 2 Inhibitors -- 8.8 Conclusions -- Acknowledgments -- References -- Further Reading. 9 HBV Polymerase as a Target for Development of Anti-HBV Drugs -- 9.1 Introduction -- 9.2 Structure and Biology of HBV -- 9.2.1 Structure -- 9.2.2 Genome -- 9.2.2.1 Size of Genome -- 9.2.2.2 Encoding -- 9.2.2.3 Genotypes -- 9.3 Life Cycle of HBV -- 9.3.1 Attachment -- 9.3.2 Penetration -- 9.3.3 Uncoating -- 9.3.4 Replication -- 9.3.5 Assembly -- 9.3.6 Release -- 9.4 Structure of HBV Polymerase -- 9.4.1 TP Domain -- 9.4.2 Spacer Domain -- 9.4.3 RT Domain -- 9.4.4 RNase H Domain -- 9.5 Multiple Roles of HBV Polymerase -- 9.6 A Potential Target for Anti-HBV Drugs -- 9.6.1 HBV Mutants -- 9.7 Need for New Drugs -- 9.7.1 Sites of Action for New Drugs -- 9.8 Present Status of Drugs Used Against HBV -- 9.8.1 Rational Synthetic Drugs -- 9.8.2 Empirical Indigenous Drugs -- 9.8.2.1 Choices -- 9.9 Recent Studies on HP Inhibitors -- 9.10 Conclusions -- Acknowledgment -- References -- Further Reading -- 10 Polymerases of Coronaviruses: Structure, Function, and Inhibitors -- 10.1 Introduction -- 10.2 Structure of HCoV RdRP -- 10.3 Function of HCoV RdRP -- 10.4 Clinical Therapies for HCoV Infections -- 10.4.1 Approaches to Identify the Suitable Treatment for SARS -- 10.4.2 RNA-Dependent RNA Polymerase Inhibitors -- 10.4.3 Marketed RdRP Inhibitors -- 10.4.4 Preclinical RdRP Inhibitors -- 10.4.5 Design of SARS-CoV RdRP Inhibitors -- 10.4.5.1 Nucleoside Analog Inhibitors -- 10.4.5.2 Nonnucleoside Analog Inhibitors -- 10.5 Conclusions -- References -- 11 Rhinovirus RNA Polymerase: Structure, Function, and Inhibitors -- 11.1 Introduction -- 11.2 Classification -- 11.3 Structural Features of HRV Polymerase -- 11.3.1 Crystal Structure of HRV 3Dpol -- 11.3.2 Description of Individual Domains -- 11.3.3 Potassium Binding Site -- 11.3.4 Metal Binding at the Active Site -- 11.3.5 Modeling of Duplex Oligonucleotide for HRV 3Dpol -- 11.3.6 Potential Oligomerization Interfaces. 11.3.7 Conformational Analysis Showing the Flexibility of the Enzyme. |
| Record Nr. | UNINA-9910583019503321 |
| London, United Kingdom : , : Academic Press, An imprint of Elsevier, , [2019] | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Soggetto topico
-
Transferases
(6)
- DNA polymerases (4)
- Antiviral agents (1)
- Hydrolases (1)