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

Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal.

Biochemistry - 30 Dec 2008

Alvisi Gualtiero, Avanzi Simone, Musiani Daniele, Camozzi Daria, Leoni Valerio, Ly-Huynh Jennifer D, Ripalti Alessandro

Abstract excerpt

The polymerase accessory protein of the human herpes simplex virus type 1 (HSV-1) DNA polymerase UL42 plays an essential role in viral replication, conferring processivity to the catalytic subunit UL30. We show here that UL42 is imported to the nucleus of living cells in a Ran- and energy-depende...

Read the complete abstract on PubMed

Topics

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

Share to Active Transport, Cell Nucleus
Share to Consensus Sequence
Share to DNA-Directed DNA Polymerase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Exodeoxyribonucleases

Share to Herpesvirus 1, Human

Share to Nuclear Localization Signals

Share to Viral Proteins

Share to Virus Replication

Source

Identifiers

PMID: 19053255
DOI: 10.1021/bi800869y

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-19053255-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal.PMID 19053255Read ↗

The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region.Semantic proximity Read ↗

The C-terminal third of UL42, a HSV-1 DNA replication protein, is dispensable for viral growth.Semantic proximity Read ↗

Probing the nuclear import signal and nuclear transport molecular determinants of PRV ICP22Semantic proximity Read ↗

The essential in vivo function of the herpes simplex virus UL42 protein correlates with its ability to stimulate the viral DNA polymerase in vitro.Semantic proximity Read ↗

Uncoupling Uncoating of Herpes Simplex Virus Genomes from Their Nuclear Import and Gene ExpressionSemantic proximity Read ↗

ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase.Semantic proximity Read ↗

Nuclear targeting of the tegument protein pp65 (UL83) of human cytomegalovirus: an unusual bipartite nuclear localization signal functions with other portions of the protein to mediate its efficient nuclear transportSemantic proximity Read ↗

Nuclear delivery mechanism of herpes simplex virus type 1 genomeSemantic proximity Read ↗

Simian virus 40 Vp1 DNA-binding domain is functionally separable from the overlapping nuclear localization signal and is required for effective virion formation and full viability.Semantic proximity Read ↗

Nuclear Sequestration of Cellular Chaperone and Proteasomal Machinery during Herpes Simplex Virus Type 1 InfectionSemantic proximity Read ↗

Herpes simplex virus replication compartments can form by coalescence of smaller compartments.Semantic proximity Read ↗

Nucleolin Is Required for Efficient Nuclear Egress of Herpes Simplex Virus Type 1 NucleocapsidsSemantic proximity Read ↗

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