NMR assignments for the insertion domain of bacteriophage Sf6 coat protein.

Therese N Tripler, Carolyn M Teschke, Andrei T Alexandrescu

Abstract read

In one paragraph

Article in Biomolecular NMR assignments, 2017. 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

–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

1 citing paper in PubMed.

Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.Journal of virology · 2019
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

3 authors.

Therese N TriplerDepartment of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Road, Storrs, CT, 06269-3125, USA.

Carolyn M TeschkeDepartment of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Road, Storrs, CT, 06269-3125, USA. Carolyn.teschke@uconn.edu.

Andrei T AlexandrescuDepartment of Molecular and Cell Biology, University of Connecticut, 91 N. Eagleville Road, Storrs, CT, 06269-3125, USA. andrei@uconn.edu.

Funding

Understanding the Protein:Protein Interactions Required for Virus AssemblyR01GM076661 · NIGMS · UNIVERSITY OF CONNECTICUT STORRS · PI TESCHKE, CAROLYN M · 2007 to 2022

$7.2M

NIGMS NIH HHS R01 GM076661

6 · The paper itself

Abstract

The P22 bacteriophage group is a subgroup of the λ phage supercluster, comprised of the three major sequence types Sf6, P22, and CUS-3, based on their capsid proteins. Our goal is to investigate the extent to which structure-function relationships are conserved for the viral coat proteins and I-domains in this subgroup. Sf6 is a phage that infects the human pathogen Shigella flexneri. The coat protein of Sf6 assembles into a procapsid, which further undergoes maturation during DNA packaging into an infectious virion. The Sf6 coat protein contains a genetically inserted domain, termed the I-domain, similar to the ones present in the P22 and CUS-3 coat proteins. Based on the P22 example, I-domains play important functional roles in capsid assembly, stability, viability, and size-determination. Here we report the

Indexed as

Nuclear Magnetic Resonance, BiomolecularAmino Acid SequenceBacteriophage P22Capsid ProteinsProtein DomainsCapsid ProteinsConserved folding motifsIcosahedral particlesIntrinsically disordered proteinsProtein dynamicsStructure homology

Identifiers

PMID27798771

DOI10.1007/s12104-016-9716-5

PMCPMC5344723

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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.