Domain structure of vaccinia virus mRNA capping enzyme. Activity of the Mr 95,000 subunit expressed in Escherichia coli.

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Domain structure of vaccinia virus mRNA capping enzyme. Activity of the Mr 95,000 subunit expressed in Escherichia coli.

The Journal of biological chemistry - 15 Jul 1990

Shuman S, Morham S G

Abstract excerpt

The D1 gene encoding the large subunit of vaccinia virus mRNA capping enzyme was expressed in Escherichia coli BL21(DE3) under the control of a bacteriophage T7 promoter. Guanylyltransferase activity (assayed as the formation of a covalent enzyme-guanylate complex) was detected in soluble lysates...

Topics

Centrifugation, Density Gradient
Chromosome Deletion
Cloning, Molecular
Escherichia coli
Genes, Viral
Macromolecular Substances
Methyltransferases
Molecular Weight
Multienzyme Complexes
Mutation
Nucleotidyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphoric Monoester Hydrolases

Recombinant Proteins

Vaccinia virus

Viral Proteins

Viral Structural Proteins

mRNA Guanylyltransferases

Source

Open in PubMed

Identifiers

PMID: 2164023

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2164023-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Domain structure of vaccinia virus mRNA capping enzyme. Activity of the Mr 95,000 subunit expressed in Escherichia coli.PMID 2164023Read ↗

Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.Semantic proximity Read ↗

A yeast-based genetic system for functional analysis of viral mRNA capping enzymes.Semantic proximity Read ↗

The domain order of mammalian capping enzyme can be inverted and baculovirus phosphatase can function in cap formation in vivo.Semantic proximity Read ↗

Analysis of a temperature-sensitive vaccinia virus mutant in the viral mRNA capping enzyme isolated by clustered charge-to-alanine mutagenesis and transient dominant selection.Semantic proximity Read ↗

Covalent catalysis in nucleotidyl transfer. A KTDG motif essential for enzyme-GMP complex formation by mRNA capping enzyme is conserved at the active sites of RNA and DNA ligases.Semantic proximity Read ↗

Amino acid residues within conserved domain VI of the vesicular stomatitis virus large polymerase protein essential for mRNA cap methyltransferase activity.Semantic proximity Read ↗

Mutations in the measles virus C protein that up regulate viral RNA synthesis.Semantic proximity Read ↗

Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein.Semantic proximity Read ↗

Identification of the amino acid residue involved in rabbit hemorrhagic disease virus VPg uridylylation.Semantic proximity Read ↗

Functional characterization of glycosylation-deficient human P-glycoprotein using a vaccinia virus expression system.Semantic proximity Read ↗

Investigations on the Tobacco Necrosis Virus D p60 replicase protein.Semantic proximity Read ↗

Effects of terminal deletions in C5 protein on promoting RNase P catalysis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.