The 1.85 Å Structure of Vaccinia Protein VP39: A Bifunctional Enzyme That Participates in the Modification of Both mRNA Ends
- 1 April 1996
- Vol. 85 (2) , 247-256
- https://doi.org/10.1016/s0092-8674(00)81101-0
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- On base flippingCell, 1995
- Universal Catalytic Domain Structure of AdoMet-dependent MethyltransferasesJournal of Molecular Biology, 1995
- The KH module has an αβ foldFEBS Letters, 1995
- Sliding Clamps of DNA PolymerasesJournal of Molecular Biology, 1993
- Proton, carbon-13, and nitrogen-15 NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteinsBiochemistry, 1992
- Poly(A) polymerase and a dissociable polyadenylation stimulatory factor encoded by vaccinia virusCell, 1991
- CHAIN — A crystallographic modeling programJournal of Molecular Graphics, 1988
- Structure of the ColE1 Rop protein at 1.7 Å resolutionJournal of Molecular Biology, 1987
- Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolutionJournal of Molecular Biology, 1981
- Chemical and biological evolution of a nucleotide-binding proteinNature, 1974