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The Journal of Biological Chemistry|October 15, 1990
A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 proteinP Digard, D M CoenVirology|July 16, 1999
Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elementsD Elton, E Medcalf, K Bishop, et al.Cell|May 19, 1989
Characterization of an efficient coronavirus ribosomal frameshifting signal: requirement for an RNA pseudoknotI Brierley, P Digard, S C InglisJournal of Virology|August 10, 1999
Temperature-sensitive lesions in two influenza A viruses defective for replicative transcription disrupt RNA binding by the nucleoproteinL Medcalf, E Poole, D Elton, et al.Virology|July 1, 1989
Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytesP Digard, V C Blok, S C InglisJournal of Virology|January 1, 1993
The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replicationP Digard, W R Bebrin, K Weisshart, et al.Journal of Virology|September 1, 1993
Unusual regulation of expression of the herpes simplex virus DNA polymerase geneK K Wobbe, P Digard, D Staknis, et al.Journal of Virology|March 1, 1993
Functional analysis of the herpes simplex virus UL42 proteinP Digard, C S Chow, L Pirrit, et al.Journal of Virology|August 10, 1999
Identification of amino acid residues of influenza virus nucleoprotein essential for RNA bindingD Elton, L Medcalf, K Bishop, et al.Journal of Virology|February 11, 1999
Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filamentsP Digard, D Elton, K Bishop, et al.Pageof 3