| crystal structure of complete rhinovirus rna polymerase suggests front loading of protein primer. | picornaviruses utilize virally encoded rna polymerase and a uridylylated protein primer to ensure replication of the entire viral genome. the molecular details of this mechanism are not well understood due to the lack of structural information. we report the crystal structure of human rhinovirus 16 3d rna-dependent rna polymerase (hrv16 3dpol) at a 2.4-a resolution, representing the first complete polymerase structure from the picornaviridae family. hrv16 3dpol shares the canonical features of o ... | 2005 | 15596823 |
| structural and virological studies of the stages of virus replication that are affected by antirhinovirus compounds. | pleconaril is a broad-spectrum antirhinovirus and antienterovirus compound that binds into a hydrophobic pocket within viral protein 1, stabilizing the capsid and resulting in the inhibition of cell attachment and rna uncoating. when crystals of human rhinovirus 16 (hrv16) and hrv14 are incubated with pleconaril, drug occupancy in the binding pocket is lower than when pleconaril is introduced during assembly prior to crystallization. this effect is far more marked in hrv16 than in hrv14 and is m ... | 2004 | 15452226 |
| experimental common cold increases mucosal output of eotaxin in atopic individuals. | in view of recent observations demonstrating that rhinovirus infections are associated with increased local activity of eosinophils, we hypothesized that eotaxin, a selective eosinophil chemoattractant, may be involved in eosinophil recruitment/activation in common cold infections. | 1999 | 10604558 |