Evidence map›Paper›PMID 34452409›Full record

ArticleViruses2021

The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex.

Christina Funk, Débora Marques da Silveira E Santos, Melanie Ott, Verena Raschbichler, Susanne M Bailer

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 40% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Christina FunkFraunhofer Institute for Interfacial Engineering and Biotechnology IGB, 70569 Stuttgart, Germany.ORCID 0000-0002-4160-0147
Débora Marques da Silveira E SantosFraunhofer Institute for Interfacial Engineering and Biotechnology IGB, 70569 Stuttgart, Germany.
Melanie OttMax von Pettenkofer-Institute, Ludwig-Maximilians-University Munich, 80539 Munich, Germany.
Verena RaschbichlerMax von Pettenkofer-Institute, Ludwig-Maximilians-University Munich, 80539 Munich, Germany.
Susanne M BailerFraunhofer Institute for Interfacial Engineering and Biotechnology IGB, 70569 Stuttgart, Germany.
Ludwig-Maximilians-Universität München · DEUniversity of Stuttgart · DEFraunhofer Institute for Interfacial Engineering and Biotechnology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at the inner nuclear membrane, which is critical for this process. The nuclear import of both proteins ensues separately from each other: pUL31 is actively imported through the central pore channel, while pUL34 is transported along the peripheral pore membrane. With this study, we identified a functional bipartite NLS between residues 178 and 194 of pUL34. pUL34 lacking its NLS is mislocalized to the TGN but retargeted to the ER upon insertion of the authentic NLS or a mimic NLS, independent of the insertion site. If co-expressed with pUL31, either of the pUL34-NLS variants is efficiently, although not completely, targeted to the nuclear rim where co-localization with pUL31 and membrane budding seem to occur, comparable to the wild-type. The viral mutant HSV1(17

Indexed as

Virus ReleaseActive Transport, Cell NucleusAmino Acid MotifsAnimalsCell LineCell NucleusChlorocebus aethiopsHeLa CellsHerpesvirus 1, HumanHumansMutationVero CellsViral ProteinsVirus ReplicationUL34 protein, Human herpesvirus 1Viral ProteinsHSV1importinsinner nuclear membrane (INM)NECnuclear egressnuclear importpUL31pUL34TA membrane proteinstargeting integral membrane proteins

Identifiers

PMID34452409
PMCPMC8402719
OpenAlexW3192395233

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.