Evidence map›Paper›PMID 20236676›Full record

ReviewVirology2010

'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.

Carolyn M Teschke, Kristin N Parent

Abstract readReview
In one paragraph

Review in Virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

57 citing papers in PubMed, 85 citations in OpenAlex.

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  13. Ecology, Structure, and Evolution ofAnnual review of virology · 2020
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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

2 authors at 2 institutions in 1 country.

Carolyn M TeschkeDepartment of Molecular and Cell Biology, 91 N. Eagleville Rd., U-3125, University of Connecticut, Storrs, CT 06269-3125, USA. Teschke@uconn.edu
Kristin N Parent
University of California San Diego · USUniversity of Connecticut · US

Funding

VIRUS ASSEMBLY AND TRANSMISSIONP01AI045976 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI ROSSMANN, MICHAEL G · 1999 to 2008
$8.8M
Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022
$7.2M
Microscopy &Image Analysis of Unstained MacromoleculesR37GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2013
$5.6M
NIAID NIH HHS P01 AI045976NIGMS NIH HHS R01 GM076661NIGMS NIH HHS R01 GM76661NIGMS NIH HHS R37 GM033050NIGMS NIH HHS R37 GM33050PHS HHS F32A1078624
6 · The paper itself

Abstract

The amino acid sequence of viral capsid proteins contains information about their folding, structure and self-assembly processes. While some viruses assemble from small preformed oligomers of coat proteins, other viruses such as phage P22 and herpesvirus assemble from monomeric proteins (Fuller and King, 1980; Newcomb et al., 1999). The subunit assembly process is strictly controlled through protein:protein interactions such that icosahedral structures are formed with specific symmetries, rather than aberrant structures. dsDNA viruses commonly assemble by first forming a precursor capsid that serves as a DNA packaging machine (Earnshaw, Hendrix, and King, 1980; Heymann et al., 2003). DNA packaging is accompanied by a conformational transition of the small precursor procapsid into a larger capsid for isometric viruses. Here we highlight the pseudo-atomic structures of phage P22 coat protein and rationalize several decades of data about P22 coat protein folding, assembly and maturation generated from a combination of genetics and biochemistry.

Indexed as

Protein FoldingProtein MultimerizationBacteriophage P22Capsid ProteinsModels, BiologicalMutant ProteinsVirus AssemblyCapsid ProteinsMutant Proteins

Identifiers

PMID20236676
PMCPMC2862144
OpenAlexW2088389799

What OpenQuestion holds

Textmetadata
LicenceTDM
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.