Evidence map›Paper›PMID 29204884›Full record

ReviewBiophysical reviews2018

Structure and assembly mechanism of virus-associated pyramids.

Tessa E F Quax, Bertram Daum

Open access · greenAbstract readReview
In one paragraph

Review in Biophysical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Viruses of theFrontiers in microbiology · 2023
    Review
  4. Article
  5. Architecture and modular assembly ofProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. 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

2 authors at 2 institutions in 2 countries.

Tessa E F QuaxMolecular Biology of Archaea, Institute of Biology II, University of Freiburg, Freiburg, Germany. tessa.quax@biologie.uni-freiburg.de.ORCID http://orcid.org/0000-0001-5516-5871
Bertram DaumLiving Systems Institute, University of Exeter, Exeter, UK.
University of Exeter · GBUniversity of Freiburg · DE

Funding

Carl-Zeiss-Stiftung Post-doc grantFP7 People: Marie-Curie Actions PIEF-GA-2013-625316University of Exeter Research Fellow Startup Grant
6 · The paper itself

Abstract

Viruses have developed intricate molecular machines to infect, replicate within and escape from their host cells. Perhaps one of the most intriguing of these mechanisms is the pyramidal egress structure that has evolved in archaeal viruses, such as SIRV2 or STIV1. The structure and mechanism of these virus-associated pyramids (VAPs) has been studied by cryo-electron tomography and complementary biochemical techniques, revealing that VAPs are formed by multiple copies of a virus-encoded 10-kDa protein (PVAP) that integrate into the cell membrane and assemble into hollow, sevenfold symmetric pyramids. In this process, growing VAPs puncture the protective surface layer and ultimately open to release newly replicated viral particles into the surrounding medium. PVAP has the striking capability to spontaneously integrate and self-assemble into VAPs in biological membranes of the archaea, bacteria and eukaryotes. This renders the VAP a universal membrane remodelling system. In this review, we provide an overview of the VAP structure and assembly mechanism and discuss the possible use of VAPs in nano-biotechnology.

Indexed as

ArchaeaArchaeal virusCryo-electron tomographyNanostructureSulfolobusVirion egress

Identifiers

PMID29204884
PMCPMC5899717
OpenAlexW2774447237

What OpenQuestion holds

Textmetadata
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.