Evidence map›Paper›PMID 25996897›Full record

ReviewCurrent opinion in structural biology2015

Polyproteins in structural biology.

Thibaut Crépin, Christopher Swale, Alexandre Monod, Frederic Garzoni, Maxime Chaillet, Imre Berger

Open access · bronzeAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Sample Preparation for Electron Cryo-Microscopy of Macromolecular Machines.Advances in experimental medicine and biology · 2024
    Article
  4. Article
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  6. Review
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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

6 authors at 5 institutions in 2 countries.

Thibaut CrépinUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France. Electronic address: crepin@embl.fr.
Christopher SwaleUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
Alexandre MonodUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
Frederic GarzoniUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France.
Maxime ChailletUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France.
Imre BergerUnit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, UMI 3265, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; The European Molecular Biology Laboratory, Grenoble Outstation, 71 Avenue des Martyrs, BP181, 38042 Grenoble Cedex 9, France; The School of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. Electronic address: iberger@embl.fr.
Université Grenoble Alpes · FRCentre National de la Recherche Scientifique · FREuropean Molecular Biology Laboratory · FRUniversité Joseph Fourier · FRUniversity of Bristol · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyproteins are chains of covalently conjoined smaller proteins that occur in nature as versatile means to organize the proteome of viruses including HIV. During maturation, viral polyproteins are typically cleaved into the constituent proteins with different biological functions by highly specific proteases, and structural analyses at defined stages of this maturation process can provide clues for antiviral intervention strategies. Recombinant polyproteins that use similar mechanisms are emerging as powerful tools for producing hitherto inaccessible protein targets such as the influenza polymerase, for high-resolution structure determination by X-ray crystallography. Conversely, covalent linking of individual protein subunits into single polypeptide chains are exploited to overcome sample preparation bottlenecks. Moreover, synthetic polyproteins provide a promising tool to dissect dynamic folding of polypeptide chains into three-dimensional architectures in single-molecule structure analysis by atomic force microscopy (AFM). The recent use of natural and synthetic polyproteins in structural biology and major achievements are highlighted in this contribution.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayHumansMicroscopy, Atomic ForceModels, MolecularMolecular Sequence DataPolyproteinsProtein ConformationProtein FoldingRecombinant ProteinsViral ProteinsVirusesPolyproteinsRecombinant ProteinsViral Proteins

Identifiers

PMID25996897
PMCPMC7125721
OpenAlexW272471359

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.