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

Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53.

The Journal of biological chemistry - 6 Jul 2012

Milbradt Jens, Auerochs Sabrina, Sevvana Madhumati, Muller Yves A, Sticht Heinrich, Marschall Manfred

Abstract excerpt

Herpesviral capsids are assembled in the host cell nucleus and are subsequently translocated to the cytoplasm. During this process it has been demonstrated that the human cytomegalovirus proteins pUL50 and pUL53 interact and form, together with other viral and cellular proteins, the nuclear egress complex at the nuclear envelope. In this study we provide evidence that specific residues of a conserved N-terminal...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytomegalovirus

Share to Glutamic Acid

Share to Green Fluorescent Proteins

Share to Microscopy, Confocal

Share to Protein Structure, Secondary

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 22589554
DOI: 10.1074/jbc.M111.331207
PMCID: PMC3390675

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Specific residues of a conserved domain in the N terminus of the human cytomegalovirus pUL50 protein determine its intranuclear interaction with pUL53.PMID 22589554Read ↗

The cytomegalovirus egress proteins pUL50 and pUL53 are translocated to the nuclear envelope through two distinct modes of nuclear importSemantic proximity Read ↗

Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication.Semantic proximity Read ↗

Phenotypical Characterization of the Nuclear Egress of Recombinant Cytomegaloviruses Reveals Defective Replication upon ORF-UL50 Deletion but Not pUL50 Phosphosite Mutation.Semantic proximity Read ↗

Functional and structural insights into HCMV terminase accessory proteins pUL77 and pUL93.Semantic proximity Read ↗

Remodelling of the nuclear lamina during human cytomegalovirus infection: role of the viral proteins pUL50 and pUL53Semantic proximity Read ↗

Cytomegaloviral proteins pUL50 and pUL53 are associated with the nuclear lamina and interact with cellular protein kinase CSemantic proximity Read ↗

Human Cytomegalovirus UL97 Phosphorylates the Viral Nuclear Egress ComplexSemantic proximity Read ↗

Human cytomegalovirus UL50 and UL53 recruit viral protein kinase UL97, not protein kinase C, for disruption of nuclear lamina and nuclear egress in infected cells.Semantic proximity Read ↗

The Herpes Simplex Virus Protein pUL31 Escorts Nucleocapsids to Sites of Nuclear Egress, a Process Coordinated by Its N-Terminal DomainSemantic proximity Read ↗

Analysis of intracellular and intraviral localization of the human cytomegalovirus UL53 proteinSemantic proximity Read ↗

Proteomic Analysis of the Multimeric Nuclear Egress Complex of Human CytomegalovirusSemantic proximity Read ↗

The C-terminal part of the human cytomegalovirus terminase subunit pUL51 is central for terminase complex assembly.Semantic proximity Read ↗

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