Evidence map›Paper›PMID 28664525›Full record

ArticleApplied biochemistry and biotechnology2018

Structure and Functional Characterisation of a Distinctive β-Lactamase from an Environmental Strain EMB20 of Bacillus cereus.

Ayesha Sadaf, Rajeshwari Sinha, S K Khare

Abstract readValidation Study
PubMed Publisher
In one paragraph

Article in Applied biochemistry and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 58% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. 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 at 1 institution in 1 country.

Ayesha SadafEnzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India.
Rajeshwari SinhaEnzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India.
S K KhareEnzyme and Microbial Biochemistry Laboratory, Department of Chemistry, Indian Institute of Technology, Hauz Khas, New Delhi, 110016, India. skhare@rocketmail.com.
Indian Institute of Technology Delhi · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rampant use and misuse of antibiotics in human medicine, agriculture and veterinary have become the key contributors to global antimicrobial resistance. One of the significant resistance mechanisms that inactivates antibiotics and impedes treatment of bacterial infections is the expression of β-lactamases. Rising evidence of newer variants of β-lactamases in the environment is therefore a serious threat to the presently available antibiotic armoury. The present work describes the purification of a variant β-lactamase isolated from a soil strain EMB20 of Bacillus cereus. The lactamase was purified using three-phase partitioning and gel filtration chromatography to a 30-fold purification and 15% recovery yield. Contrary to the general trend, the lactamase was not a metalloenzyme, but its activity was enhanced in the presence of Mg

Indexed as

Bacillus cereusbeta-Lactamase Inhibitorsbeta-LactamasesCircular DichroismElectrophoresis, Polyacrylamide GelGuanidineProtein Structure, SecondarySpectrometry, FluorescenceSubstrate SpecificityUltrafiltrationUreabeta-Lactamase Inhibitorsbeta-LactamasesGuanidineUreaAntimicrobial resistanceCircular dichroismFluorescenceLactamase inhibitorsThree-phase partitioning chromatographyβ-Lactamases

Identifiers

PMID28664525
OpenAlexW2732891977

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.