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Members of the Enterovirus genus are positive-stranded RNA viruses encompassing important human pathogens and include poliovirus, coxsackievirus and rhinovirus. Several enteroviruses, such as enterovirus-71 and enterovirus-D68, have emerged from relative obscurity to become worldwide public health threats, highlighting the need to develop effective therapeutic strategies to combat these important viruses. To do this, understanding the genomics and the cellular and molecular biology of infection of enteroviruses is critical.This book represents a comprehensive tour of the current most important enterovirus research. The editors, Dr. Jackson and Dr. Coyne, have assembled a group of enteroviral experts who cover topics including viral entry and the hijacking of host functions; the dynamic analysis of ever-evolving virus genomes; the cellular membrane changes promoting virus assembly and release.This volume is a must-read for anyone with an interest in this family of viruses and an important acquisition for all microbiology libraries.

Enteroviruses.

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This monograph reviews information published since 1997 on the group B coxsackieviruses (CVB), a large and important group of human enteroviruses. The CVB were discovered in the mid-20th century, during the search for other poliovirus types, and within a very few years of this discovery, the CVB had been implicated as causes of human myocarditis and pancreatitis. The study of the CVB is still inextricably linked with the fate of their well-known relatives, the polioviruses, for as poliovirus eradication proceeds around the world, the CVB emerge more prominently as the enteroviruses best suited for continuing studies in enteroviral molecular biology as well as understanding the mechanisms underlying enteroviral pathogenesis. This volume reviews and presents modern views on the spectrum of CVB biologies, from interaction of the virus with its receptor through replication, speciation, and induction of disease.

Coxsackievirus infections. --- Coxsackieviruses. --- Coxsackie virus infections --- Coxsackievirus diseases --- Enterovirus diseases --- Coxsackie virus --- Enteroviruses --- Medical virology. --- Microbiology. --- Virology. --- Medical Microbiology. --- Microbial biology --- Biology --- Microorganisms --- Medical microbiology --- Virology --- Virus diseases --- Medical microbiology. --- Microbiology

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This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.

Research & information: general --- Biology, life sciences --- Biochemistry --- protein lysine methylation --- H3K9 methylation --- PKMT --- enzyme specificity --- enzyme regulation --- heterochromatin --- protein post-translational modification --- NSD3 --- WHSC1L1 --- structure and function --- protein arginine methylation --- PRMT7 --- epigenetics --- cancer --- immunity --- pluripotency --- SETDB1 --- methyltransferase --- schizophrenia --- Huntington’s disease --- Rett syndrome --- Prader–Willi syndrome --- congenital heart diseases --- inflammatory bowel disease --- MLL2 --- structure --- H3K4me3 --- chromatin regulation --- disease --- dystonia --- NSD1 --- H3K36 --- SOTOS --- NUP98-NSD1 --- AML --- PRMT6 --- post-translational modification --- H3R2me2a --- SETD3 --- posttranslational modifications --- protein histidine methylation --- actin --- polymerization --- cytoskeleton --- enteroviruses --- oncogenesis --- PRMT5 --- cardiovascular disease --- neurodegenerative diseases --- diabetes --- inflammation --- G9a --- GLP --- EHMT2 --- EHMT1 --- post translational modification --- lysine methylation --- N-terminal methylation --- translation --- eEF1A --- METTL13 --- neuron --- synapse --- dendritic spine --- actin cytoskeleton --- GTPase --- PRMT1 --- arginine methylation --- H4R3 methylation --- transcriptional regulation --- cell signaling --- DNA damage repair --- PRMT2 --- SH3 --- SETMAR --- Metnase --- H3K36me2 --- Hsmar1 --- non-homologous end joining repair --- NHEJ --- transposase --- transposable elements --- histone --- SET7/9 --- SETD7 --- lysine-specific methyltransferase (PKMT) --- cell proliferation --- stress response --- post-translational protein modification --- n/a --- Huntington's disease --- Prader-Willi syndrome

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This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.

Research & information: general --- Biology, life sciences --- Biochemistry --- protein lysine methylation --- H3K9 methylation --- PKMT --- enzyme specificity --- enzyme regulation --- heterochromatin --- protein post-translational modification --- NSD3 --- WHSC1L1 --- structure and function --- protein arginine methylation --- PRMT7 --- epigenetics --- cancer --- immunity --- pluripotency --- SETDB1 --- methyltransferase --- schizophrenia --- Huntington's disease --- Rett syndrome --- Prader-Willi syndrome --- congenital heart diseases --- inflammatory bowel disease --- MLL2 --- structure --- H3K4me3 --- chromatin regulation --- disease --- dystonia --- NSD1 --- H3K36 --- SOTOS --- NUP98-NSD1 --- AML --- PRMT6 --- post-translational modification --- H3R2me2a --- SETD3 --- posttranslational modifications --- protein histidine methylation --- actin --- polymerization --- cytoskeleton --- enteroviruses --- oncogenesis --- PRMT5 --- cardiovascular disease --- neurodegenerative diseases --- diabetes --- inflammation --- G9a --- GLP --- EHMT2 --- EHMT1 --- post translational modification --- lysine methylation --- N-terminal methylation --- translation --- eEF1A --- METTL13 --- neuron --- synapse --- dendritic spine --- actin cytoskeleton --- GTPase --- PRMT1 --- arginine methylation --- H4R3 methylation --- transcriptional regulation --- cell signaling --- DNA damage repair --- PRMT2 --- SH3 --- SETMAR --- Metnase --- H3K36me2 --- Hsmar1 --- non-homologous end joining repair --- NHEJ --- transposase --- transposable elements --- histone --- SET7/9 --- SETD7 --- lysine-specific methyltransferase (PKMT) --- cell proliferation --- stress response --- post-translational protein modification --- protein lysine methylation --- H3K9 methylation --- PKMT --- enzyme specificity --- enzyme regulation --- heterochromatin --- protein post-translational modification --- NSD3 --- WHSC1L1 --- structure and function --- protein arginine methylation --- PRMT7 --- epigenetics --- cancer --- immunity --- pluripotency --- SETDB1 --- methyltransferase --- schizophrenia --- Huntington's disease --- Rett syndrome --- Prader-Willi syndrome --- congenital heart diseases --- inflammatory bowel disease --- MLL2 --- structure --- H3K4me3 --- chromatin regulation --- disease --- dystonia --- NSD1 --- H3K36 --- SOTOS --- NUP98-NSD1 --- AML --- PRMT6 --- post-translational modification --- H3R2me2a --- SETD3 --- posttranslational modifications --- protein histidine methylation --- actin --- polymerization --- cytoskeleton --- enteroviruses --- oncogenesis --- PRMT5 --- cardiovascular disease --- neurodegenerative diseases --- diabetes --- inflammation --- G9a --- GLP --- EHMT2 --- EHMT1 --- post translational modification --- lysine methylation --- N-terminal methylation --- translation --- eEF1A --- METTL13 --- neuron --- synapse --- dendritic spine --- actin cytoskeleton --- GTPase --- PRMT1 --- arginine methylation --- H4R3 methylation --- transcriptional regulation --- cell signaling --- DNA damage repair --- PRMT2 --- SH3 --- SETMAR --- Metnase --- H3K36me2 --- Hsmar1 --- non-homologous end joining repair --- NHEJ --- transposase --- transposable elements --- histone --- SET7/9 --- SETD7 --- lysine-specific methyltransferase (PKMT) --- cell proliferation --- stress response --- post-translational protein modification

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Antiviral agents are used for the treatment of viral diseases. Antiviral drugs have been successfully developed and used clinically for a limited number of important human viral diseases notably caused by human immunodeficiency virus (HIV), hepatitis C virus (HCV), hepatitis B virus (HBV), herpes, and influenza viruses. Despite the successes of these antiviral drugs, issues with drug resistance and toxicity remain challenging. These challenges are driving research to identify new drug candidates and to investigate novel drug targets to develop new mechanistic drug classes. Antiviral agents are not available against many viruses that cause human disease and economic burdens; in particular, the development of antiviral agents against emerging, re-emerging, and neglected viruses is increasingly becoming a priority. This book includes six review articles that discuss new antiviral strategies. The reviews either discuss advances relating to a specific virus or new therapeutic targets and approaches. The book includes 15 original research articles reporting new antiviral agents against a variety of clinically and economically important viruses and studies into the prevalence or acquisition of drug resistance. Overall, this book is an exciting collection of new research and ideas relating to the development of antiviral agents.

Research & information: general --- Biology, life sciences --- Zika virus --- nucleoside analogues --- antiviral agents --- NS5 --- prodrugs --- ProTides --- neural stem cells --- RNA-dependent RNA polymerase --- cytomegalovirus --- latent infection --- TALEN --- Surveyor nuclease mutation detection assay --- ie-1 gene --- quantitative real-time PCR --- Epstein-Barr virus --- herpes viruses --- lytic gene expression --- Burkitt lymphoma cells --- clozapine --- antipsychotic drug --- antiviral drug --- enteroviruses --- coxsackievirus B4 --- persistent infection --- fluoxetine --- resistance --- mutations --- herpes B virus --- macacine herpesvirus-1 --- genistein --- flavonoids --- acyclovir --- ganciclovir --- Plantago asiatica --- Clerodendrum trichotomum --- RSV --- therapeutic effects --- acteoside --- human antimicrobial peptides --- antiviral strategies --- defensins --- cathelicidins --- hepcidins --- transferrins --- influenza A virus --- brevilin A --- antiviral --- sesquiterpene lactone --- replication --- PRRSV --- polyethylenimine --- PEI --- virion internalization --- endocytosis --- HIV --- pediatrics --- Ethiopia --- pre-treatment drug resistance --- combination antiretroviral therapy (cART) --- dried plasma spots --- dried blood spots --- sphingolipids --- glycosphingolipids --- viruses --- lipid biosynthesis --- flavivirus --- Japanese encephalitis virus --- furin inhibitor --- precursor membrane protein --- measles virus --- central nervous system --- tropism --- treatments --- porcine reproductive and respiratory syndrome virus --- ginsenoside Rg1 --- antiviral activity --- pro-inflammatory factor --- NF-κB signaling pathway --- acute/latent infection --- congenital infection --- antiviral agent --- therapeutic strategies --- nucleic acid-based therapeutic approach --- HCMV vaccine --- adoptive cell therapy --- Rev response element --- chemical footprinting --- SHAPE --- drug discovery --- branched peptides --- herpesvirus --- immediate-early --- IE1 --- IE2 --- ribozyme --- RNA interference --- CRISPR/Cas --- small molecule --- orthohantavirus --- phenyl-benzotriazoles --- C-FRA --- Porcine circovirus type 2 --- epigallocatechin gallate --- heparan sulfate --- antiviral effect --- virus attachment --- microvirin --- lectin --- human immunodeficiency virus --- hepatitis C virus --- antiviral inhibitor --- non-immunogenic --- viral entry --- protein drugs --- LUMS1 --- oleanane-type derivatives --- influenza A virus (IAV) --- virus entry inhibitors --- hemagglutinin (HA) --- Zika virus --- nucleoside analogues --- antiviral agents --- NS5 --- prodrugs --- ProTides --- neural stem cells --- RNA-dependent RNA polymerase --- cytomegalovirus --- latent infection --- TALEN --- Surveyor nuclease mutation detection assay --- ie-1 gene --- quantitative real-time PCR --- Epstein-Barr virus --- herpes viruses --- lytic gene expression --- Burkitt lymphoma cells --- clozapine --- antipsychotic drug --- antiviral drug --- enteroviruses --- coxsackievirus B4 --- persistent infection --- fluoxetine --- resistance --- mutations --- herpes B virus --- macacine herpesvirus-1 --- genistein --- flavonoids --- acyclovir --- ganciclovir --- Plantago asiatica --- Clerodendrum trichotomum --- RSV --- therapeutic effects --- acteoside --- human antimicrobial peptides --- antiviral strategies --- defensins --- cathelicidins --- hepcidins --- transferrins --- influenza A virus --- brevilin A --- antiviral --- sesquiterpene lactone --- replication --- PRRSV --- polyethylenimine --- PEI --- virion internalization --- endocytosis --- HIV --- pediatrics --- Ethiopia --- pre-treatment drug resistance --- combination antiretroviral therapy (cART) --- dried plasma spots --- dried blood spots --- sphingolipids --- glycosphingolipids --- viruses --- lipid biosynthesis --- flavivirus --- Japanese encephalitis virus --- furin inhibitor --- precursor membrane protein --- measles virus --- central nervous system --- tropism --- treatments --- porcine reproductive and respiratory syndrome virus --- ginsenoside Rg1 --- antiviral activity --- pro-inflammatory factor --- NF-κB signaling pathway --- acute/latent infection --- congenital infection --- antiviral agent --- therapeutic strategies --- nucleic acid-based therapeutic approach --- HCMV vaccine --- adoptive cell therapy --- Rev response element --- chemical footprinting --- SHAPE --- drug discovery --- branched peptides --- herpesvirus --- immediate-early --- IE1 --- IE2 --- ribozyme --- RNA interference --- CRISPR/Cas --- small molecule --- orthohantavirus --- phenyl-benzotriazoles --- C-FRA --- Porcine circovirus type 2 --- epigallocatechin gallate --- heparan sulfate --- antiviral effect --- virus attachment --- microvirin --- lectin --- human immunodeficiency virus --- hepatitis C virus --- antiviral inhibitor --- non-immunogenic --- viral entry --- protein drugs --- LUMS1 --- oleanane-type derivatives --- influenza A virus (IAV) --- virus entry inhibitors --- hemagglutinin (HA)