Viral protease inhibitors.
Identifieur interne : 001A22 ( PubMed/Curation ); précédent : 001A21; suivant : 001A23Viral protease inhibitors.
Auteurs : Jeffrey Anderson [États-Unis] ; Celia Schiffer ; Sook-Kyung Lee ; Ronald SwanstromSource :
- Handbook of experimental pharmacology [ 0171-2004 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Antiviraux (pharmacologie), Association de médicaments, Cysteine endopeptidases, Cytomegalovirus (), Cytomegalovirus (enzymologie), Hepacivirus (), Hepacivirus (enzymologie), Humains, Inhibiteurs de protéase du VIH (pharmacologie), Inhibiteurs de protéases (pharmacologie), Modèles moléculaires, Peptide hydrolases (), Protéines virales (antagonistes et inhibiteurs), Protéines virales non structurales (antagonistes et inhibiteurs), Résistance virale aux médicaments, Virus (), Virus (enzymologie), Virus du SRAS (), Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Protéines virales, Protéines virales non structurales.
- enzymologie : Cytomegalovirus, Hepacivirus, Virus, Virus du SRAS.
- pharmacologie : Antiviraux, Inhibiteurs de protéase du VIH, Inhibiteurs de protéases.
- Animaux, Association de médicaments, Cysteine endopeptidases, Cytomegalovirus, Hepacivirus, Humains, Modèles moléculaires, Peptide hydrolases, Résistance virale aux médicaments, Virus, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Antiviral Agents (pharmacology), Cysteine Endopeptidases, Cytomegalovirus (drug effects), Cytomegalovirus (enzymology), Drug Resistance, Viral, Drug Therapy, Combination, HIV Protease Inhibitors (pharmacology), Hepacivirus (drug effects), Hepacivirus (enzymology), Humans, Models, Molecular, Peptide Hydrolases (chemistry), Protease Inhibitors (pharmacology), SARS Virus (drug effects), SARS Virus (enzymology), Viral Nonstructural Proteins (antagonists & inhibitors), Viral Proteins (antagonists & inhibitors), Viruses (drug effects), Viruses (enzymology).
- MESH :
- chemical , antagonists & inhibitors : Viral Nonstructural Proteins, Viral Proteins.
- chemical , chemistry : Peptide Hydrolases.
- chemical , pharmacology : Antiviral Agents, HIV Protease Inhibitors, Protease Inhibitors.
- drug effects : Cytomegalovirus, Hepacivirus, SARS Virus, Viruses.
- enzymology : Cytomegalovirus, Hepacivirus, SARS Virus, Viruses.
- Animals, Cysteine Endopeptidases, Drug Resistance, Viral, Drug Therapy, Combination, Humans, Models, Molecular.
Abstract
This review provides an overview of the development of viral protease inhibitors as antiviral drugs. We concentrate on HIV-1 protease inhibitors, as these have made the most significant advances in the recent past. Thus, we discuss the biochemistry of HIV-1 protease, inhibitor development, clinical use of inhibitors, and evolution of resistance. Since many different viruses encode essential proteases, it is possible to envision the development of a potent protease inhibitor for other viruses if the processing site sequence and the catalytic mechanism are known. At this time, interest in developing inhibitors is limited to viruses that cause chronic disease, viruses that have the potential to cause large-scale epidemics, or viruses that are sufficiently ubiquitous that treating an acute infection would be beneficial even if the infection was ultimately self-limiting. Protease inhibitor development is most advanced for hepatitis C virus (HCV), and we also provide a review of HCV NS3/4A serine protease inhibitor development, including combination therapy and resistance. Finally, we discuss other viral proteases as potential drug targets, including those from Dengue virus, cytomegalovirus, rhinovirus, and coronavirus.
DOI: 10.1007/978-3-540-79086-0_4
PubMed: 19048198
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We concentrate on HIV-1 protease inhibitors, as these have made the most significant advances in the recent past. Thus, we discuss the biochemistry of HIV-1 protease, inhibitor development, clinical use of inhibitors, and evolution of resistance. Since many different viruses encode essential proteases, it is possible to envision the development of a potent protease inhibitor for other viruses if the processing site sequence and the catalytic mechanism are known. At this time, interest in developing inhibitors is limited to viruses that cause chronic disease, viruses that have the potential to cause large-scale epidemics, or viruses that are sufficiently ubiquitous that treating an acute infection would be beneficial even if the infection was ultimately self-limiting. Protease inhibitor development is most advanced for hepatitis C virus (HCV), and we also provide a review of HCV NS3/4A serine protease inhibitor development, including combination therapy and resistance. Finally, we discuss other viral proteases as potential drug targets, including those from Dengue virus, cytomegalovirus, rhinovirus, and coronavirus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19048198</PMID><DateCompleted><Year>2009</Year><Month>03</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0171-2004</ISSN><JournalIssue CitedMedium="Print"><Issue>189</Issue><PubDate><Year>2009</Year></PubDate></JournalIssue><Title>Handbook of experimental pharmacology</Title><ISOAbbreviation>Handb Exp Pharmacol</ISOAbbreviation></Journal><ArticleTitle>Viral protease inhibitors.</ArticleTitle><Pagination><MedlinePgn>85-110</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/978-3-540-79086-0_4</ELocationID><Abstract><AbstractText>This review provides an overview of the development of viral protease inhibitors as antiviral drugs. We concentrate on HIV-1 protease inhibitors, as these have made the most significant advances in the recent past. Thus, we discuss the biochemistry of HIV-1 protease, inhibitor development, clinical use of inhibitors, and evolution of resistance. Since many different viruses encode essential proteases, it is possible to envision the development of a potent protease inhibitor for other viruses if the processing site sequence and the catalytic mechanism are known. At this time, interest in developing inhibitors is limited to viruses that cause chronic disease, viruses that have the potential to cause large-scale epidemics, or viruses that are sufficiently ubiquitous that treating an acute infection would be beneficial even if the infection was ultimately self-limiting. Protease inhibitor development is most advanced for hepatitis C virus (HCV), and we also provide a review of HCV NS3/4A serine protease inhibitor development, including combination therapy and resistance. Finally, we discuss other viral proteases as potential drug targets, including those from Dengue virus, cytomegalovirus, rhinovirus, and coronavirus.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>Jeffrey</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Division of Infectious Diseases, Department of Internal Medicine, University of Massachusetts, Worcester, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schiffer</LastName><ForeName>Celia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Sook-Kyung</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Swanstrom</LastName><ForeName>Ronald</ForeName><Initials>R</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM65347</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United 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MajorTopicYN="N">Cytomegalovirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024882" MajorTopicYN="N">Drug Resistance, Viral</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004359" MajorTopicYN="N">Drug Therapy, Combination</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017320" MajorTopicYN="N">HIV Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016174" MajorTopicYN="N">Hepacivirus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010447" MajorTopicYN="N">Peptide Hydrolases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014780" MajorTopicYN="N">Viruses</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>125</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>12</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>3</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>12</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19048198</ArticleId><ArticleId 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