Discover Community Create You

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

Article

Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation.

Journal of virology - 1 Oct 1999

Michel D, Kramer S, Höhn S, Schaarschmidt P, Wunderlich K, Mertens T

Abstract excerpt

Thirteen point mutations targeting predicted domains conserved in homologous protein kinases were introduced into the UL97 coding region of the human cytomegalovirus. All mutagenized proteins were expressed in cells infected with recombinant vaccinia viruses (rVV). Several mutations drastically reduced ganciclovir (GCV) phosphorylation. Mutations at amino acids G340, A442, L446, and F523 resulted in a complete...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Amino Acids
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytomegalovirus

Share to Molecular Sequence Data

Share to Phosphorylation

Share to Phosphotransferases (Alcohol Group Acceptor)

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 10482650
DOI: 10.1128/JVI.73.10.8898-8901.1999
PMCID: PMC112917

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation.PMID 10482650Read ↗

Mutations in the UL97 ORF of ganciclovir-resistant clinical cytomegalovirus isolates differentially affect GCV phosphorylation as determined in a recombinant vaccinia virus systemSemantic proximity Read ↗

Analysis of the structure-activity relationship of four herpesviral UL97 subfamily protein kinases reveals partial but not full functional conservation.Semantic proximity Read ↗

Mapping of a self-interaction domain of the cytomegalovirus protein kinase pUL97.Semantic proximity Read ↗

Conserved domains and structure prediction of human cytomegalovirus UL27 protein.Semantic proximity Read ↗

Inhibitors of human cytomegalovirus replication drastically reduce the activity of the viral protein kinase pUL97.Semantic proximity Read ↗

GCV resistance due to the mutation A594P in the cytomegalovirus protein UL97 is partially reconstituted by a second mutation at D605E.Semantic proximity Read ↗

Cyclin-Dependent Kinase-Like Function Is Shared by the Beta- and Gamma- Subset of the Conserved Herpesvirus Protein KinasesSemantic proximity Read ↗

The protein kinase pUL97 of human cytomegalovirus interacts with and phosphorylates the DNA polymerase processivity factor pUL44.Semantic proximity Read ↗

Human Cytomegalovirus Protein Kinase UL97 Forms a Complex with the Tegument Phosphoprotein pp65Semantic proximity Read ↗

A nine-codon deletion mutation in the cytomegalovirus UL97 phosphotransferase gene confers resistance to ganciclovir.Semantic proximity Read ↗

Highly conserved interaction profiles between clinically relevant mutants of the cytomegalovirus CDK-like kinase pUL97 and human cyclins: functional significance of cyclin HSemantic proximity Read ↗

Protein kinases conserved in herpesviruses potentially share a function mimicking the cellular protein kinase cdc2Semantic proximity Read ↗

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