Evidence map›Paper›PMID 24669224›Full record

ArticleInternational journal of microbiology2014

High Level Expression and Purification of Atl, the Major Autolytic Protein of Staphylococcus aureus.

Vineet K Singh

Open access · goldAbstract read
In one paragraph

Article in International journal of microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Vineet K SinghMicrobiology and Immunology, Kirksville College of Osteopathic Medicine, A.T. Still University of Health Sciences, 800 West Jefferson Street, Kirksville, MO 63501, USA.
A.T. Still University · US

Funding

Significance of four methionine sulfoxide reductases in Staphylococcus aureusR15AI090680 · NIAID · A.T. STILL UNIVERSITY OF HEALTH SCIENCES · PI SINGH, VINEET KUMAR · 2010 to 2010
$309k
NIAID NIH HHS R15 AI090680
6 · The paper itself

Abstract

Staphylococcus aureus is a major human and animal pathogen. Autolysins regulate the growth, turnover, cell lysis, biofilm formation, and the pathogenicity of S. aureus. Atl is the major autolysin in S. aureus. The biochemical and structural studies of staphylococcal Atl have been limited due to difficulty in cloning, high level overexpression, and purification of this protein. This study describes successful cloning, high level over-expression, and purification of two forms of fully functional Atl proteins. These pure proteins can be used to study the functional and structural properties of this important protein.

Identifiers

PMID24669224
PMCPMC3941666
OpenAlexW1981043900

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.