Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes - sprookjes - yvandenbroek - TriplyDB

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

http://www.wikidata.org/entity/Q27619756

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Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies Molecular mechanisms of severe acute respiratory syndrome (SARS)Design of wide-spectrum inhibitors targeting coronavirus main proteases Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells Replication and Inhibitors of Enteroviruses and Parechoviruses Inhaled anti-infective chemotherapy for respiratory tract infections: successes, challenges and the road ahead From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.Structure of arterivirus nsp4. The smallest chymotrypsin-like proteinase with an alpha/beta C-terminal extension and alternate conformations of the oxyanion hole Structural basis for the substrate specificity of tobacco etch virus protease Structure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitors Structure of the Main Protease from a Global Infectious Human Coronavirus, HCoV-HKU1 Structural Basis of Inhibition Specificities of 3C and 3C-like Proteases by Zinc-coordinating and Peptidomimetic Compounds A Structural Study of Norovirus 3C Protease Specificity: Binding of a Designed Active Site-Directed Peptide Inhibitor Enterovirus 71 and Coxsackievirus A16 3C Proteases: Binding to Rupintrivir and Their Substrates and Anti-Hand, Foot, and Mouth Disease Virus Drug Design Crystal Structures of Enterovirus 71 3C Protease Complexed with Rupintrivir Reveal the Roles of Catalytically Important Residues Structural Basis for Antiviral Inhibition of the Main Protease, 3C, from Human Enterovirus 93 Structural Basis of Substrate Specificity and Protease Inhibition in Norwalk Virus 3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against Picornaviruses Structure of a Murine Norovirus NS6 Protease-Product Complex Revealed by Adventitious Crystallisation Structures of Enterovirus 71 3C proteinase (strain E2004104-TW-CDC) and its complex with rupintrivir Optimize the interactions at S4 with efficient inhibitors targeting 3C proteinase from enterovirus 71 In vitro antiviral activity of AG7088, a potent inhibitor of human rhinovirus 3C protease Inhibition of human rhinovirus-induced cytokine production by AG7088, a human rhinovirus 3C protease inhibitor Pharmacokinetics and safety of an antirhinoviral agent, ruprintrivir, in healthy volunteers Inhibition of Enterovirus 71 replication by 7-hydroxyflavone and diisopropyl-flavon7-yl Phosphate Covalent Modifiers: A Chemical Perspective on the Reactivity of α,β-Unsaturated Carbonyls with Thiols via Hetero-Michael Addition Reactions Functional binding of hexanucleotides to 3C protease of hepatitis A virus.Characterization of a torovirus main proteinase Enterovirus 71 infection and vaccines.Site-specific molecular design and its relevance to pharmacogenomics and chemical biology.In vitro resistance study of rupintrivir, a novel inhibitor of human rhinovirus 3C protease.In vitro antiviral activity and single-dose pharmacokinetics in humans of a novel, orally bioavailable inhibitor of human rhinovirus 3C protease.Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor.In vitro activity of expanded-spectrum pyridazinyl oxime ethers related to pirodavir: novel capsid-binding inhibitors with potent antipicornavirus activity.Signal propagation in proteins and relation to equilibrium fluctuations High-throughput screening identifies three inhibitor classes of the telomere resolvase from the lyme disease spirochete Rupintrivir is a promising candidate for treating severe cases of Enterovirus-71 infection.Inhibition of enterovirus 71 by adenosine analog NITD008

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P2860

Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

http://www.wikidata.org/entity/Q27619756

description

1999 nî lūn-bûn

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1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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Structure-assisted design of m ...... multiple rhinovirus serotypes

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Proceedings of the National Academy of Sciences of the United States of America

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Structure-assisted design of m ...... multiple rhinovirus serotypes

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P2860

Refined X-ray crystallographic structure of the poliovirus 3C gene product

Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 3. Structure-activity studies of ketomethylene-containing peptidomimetics

Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 4. Incorporation of P1 lactam moieties as L-glutamine replacements

Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyprotein.

Design, synthesis, and evaluation of nonpeptidic inhibitors of human rhinovirus 3C protease.

Chemotherapy of rhinovirus colds.

Viral proteinases.

Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases.

Processing of a cellular polypeptide by 3CD proteinase is required for poliovirus ribonucleoprotein complex formation.

Picornavirus protein processing--enzymes, substrates, and genetic regulation.

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