Evidence map›Paper›PMID 27685368›Full record

ReviewCritical reviews in biochemistry and molecular biology2016

Oligomeric viral proteins: small in size, large in presence.

Bhargavi Jayaraman, Amber M Smith, Jason D Fernandes, Alan D Frankel

Abstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
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  6. Review
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  12. Melatonin and mitochondrial function during ischemia/reperfusion injury.Cellular and molecular life sciences : CMLS · 2017
    Review
  13. Review
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

4 authors.

Bhargavi Jayaramana Department of Biochemistry and Biophysics , University of California , San Francisco , CA , USA.
Amber M Smitha Department of Biochemistry and Biophysics , University of California , San Francisco , CA , USA.
Jason D Fernandesb UC Santa Cruz Genomics Institute , Santa Cruz , CA , USA.
Alan D Frankela Department of Biochemistry and Biophysics , University of California , San Francisco , CA , USA.

Funding

X-ray Screening and Rapid Structure DeterminationP50GM082250 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FRANKEL, ALAN D · 2007 to 2018
$48.8M
NIGMS NIH HHS P50 GM082250
6 · The paper itself

Abstract

Viruses are obligate parasites that rely heavily on host cellular processes for replication. The small number of proteins typically encoded by a virus is faced with selection pressures that lead to the evolution of distinctive structural properties, allowing each protein to maintain its function under constraints such as small genome size, high mutation rate, and rapidly changing fitness conditions. One common strategy for this evolution is to utilize small building blocks to generate protein oligomers that assemble in multiple ways, thereby diversifying protein function and regulation. In this review, we discuss specific cases that illustrate how oligomerization is used to generate a single defined functional state, to modulate activity via different oligomeric states, or to generate multiple functional forms via different oligomeric states.

Indexed as

Protein MultimerizationAnimalsCapsidEbolavirusFlavivirusFlavivirus InfectionsHemorrhagic Fever, EbolaHIVHIV InfectionsHumansModels, MolecularProtein ConformationViral ProteinsVirus DiseasesVirusesVirus ReplicationViral ProteinsEbolavirus VP40Flavivirus NS1HIV-1 CapsidHIV-1 Revmultifunctionaloligomeric statesViral proteins

Identifiers

PMID27685368
PMCPMC5088105

What OpenQuestion holds

Textmetadata
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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.