Evidence map›Paper›PMID 27050257›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 Å resolution.

Pierce O'Neil, Scott Lovell, Nurjahan Mehzabeen, Kevin Battaile, Indranil Biswas

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  2. HU ofFrontiers in microbiology · 2018
    Article
  3. 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

5 authors at 3 institutions in 1 country.

Pierce O'NeilDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA.
Scott LovellProtein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Kansas City, KS 66047, USA.
Nurjahan MehzabeenProtein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Kansas City, KS 66047, USA.
Kevin BattaileIMCA-CAT, Hauptman-Woodward Medical Research Institute, APS, Argonne National Laboratory, Argonne, IL 60439, USA.
Indranil BiswasDepartment of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA.
University of Kansas · USUniversity of Kansas Medical Center · USHauptman-Woodward Medical Research Institute · US

Funding

TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI HOLYOAK, TODD · 2002 to 2011
$20.1M
Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
Protein Structure and FunctionP20GM103420 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2012 to 2012
$2.0M
Expression of clp genes in Streptococcus mutansR01DE021664 · NIDCR · UNIVERSITY OF KANSAS MEDICAL CENTER · PI BISWAS, INDRANIL · 2011 to 2015
$1.8M
NCRR NIH HHS 5P20RR017708NCRR NIH HHS P20 RR017708NIDCR NIH HHS DE021664NIDCR NIH HHS R01 DE021664NIGMS NIH HHS 8P20GM103420NIGMS NIH HHS P20 GM103420NIGMS NIH HHS P30 GM110761
6 · The paper itself

Abstract

Nucleoid-associated proteins (NAPs) in prokaryotes play an important architectural role in DNA bending, supercoiling and DNA compaction. In addition to architectural roles, some NAPs also play regulatory roles in DNA replication and repair, and act as global transcriptional regulators in many bacteria. Bacteria encode multiple NAPs and some of them are even essential for survival. Streptococcus mutans, a dental pathogen, encodes one such essential NAP called histone-like protein (HLP). Here, the three-dimensional structure of S. mutans HLP has been determined to 1.9 Å resolution. The HLP structure is a dimer and shares a high degree of similarity with other bacterial NAPs, including HU. Since HLPs are essential for the survival of pathogenic streptococci, this structure determination is potentially beneficial for future drug development against these pathogens.

Indexed as

Amino Acid SequenceBacterial ProteinsDimerizationGenes, BacterialHistonesModels, MolecularProtein ConformationSequence Homology, Amino AcidStreptococcus mutansBacterial ProteinsHistoneshistone-like proteinHLPnucleoid-associated proteinStreptococcus mutans

Identifiers

PMID27050257
PMCPMC4822980
OpenAlexW2319967807

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.