about
Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypesThioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluationStructure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 4. Incorporation of P1 lactam moieties as L-glutamine replacementsConservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor.Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity.A Quantitative Microtiter Assay for Sialylated Glycoform Analyses Using Lectin Complexes.Chinese hamster ovary cells can produce galactose-α-1,3-galactose antigens on proteins.Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 2. Peptide structure-activity studies.Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 1. Michael acceptor structure-activity studies.Design and synthesis of irreversible depsipeptidyl human rhinovirus 3C protease inhibitors.Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 6. Structure-activity studies of orally bioavailable, 2-pyridone-containing peptidomimetics.Structure-based design of a parallel synthetic array directed toward the discovery of irreversible inhibitors of human rhinovirus 3C protease.Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 8. Pharmacological optimization of orally bioavailable 2-pyridone-containing peptidomimetics.Structure-based design of ketone-containing, tripeptidyl human rhinovirus 3C protease inhibitors
P50
Q27619756-66DFEEE1-79D5-40A9-8F27-85FCAAA325B8Q27660408-434B7556-5085-4EFF-B049-BCF3211F0FCEQ28373315-784292F5-0339-4619-B4EF-D19AD59B7E88Q30448643-41B71F3B-7F1F-42F9-984C-2B9C39C4E0BDQ33420853-77210242-767D-45DC-B8E8-14328E70E263Q35882274-EF7131F3-B8CE-4F85-AC04-5631D57A23D0Q37733720-AC21CEF1-CE95-43CE-90FA-4EE541826565Q41024218-E34025DD-CBA9-4F3B-ADCD-FC061B561319Q41024226-2A439B05-D1B7-42D2-A129-5C9784D0305CQ43759893-03617A51-0CC0-4A13-B9CE-94F027DBE8C3Q43946307-B8E73EE9-EB34-4FE7-B89E-D05754B8D36FQ43977102-12369EE4-B789-4802-A4C9-06B422548044Q44604150-46C0B558-A9B8-4B69-8148-4F76782953E8Q73356245-51AA5814-9966-4997-9DA8-D6B5346CE67D
P50
description
researcher
@en
wetenschapper
@nl
name
J W Meador
@en
J W Meador
@nl
type
label
J W Meador
@en
J W Meador
@nl
prefLabel
J W Meador
@en
J W Meador
@nl
P106
P31
P496
0000-0002-5783-4327