Evidence map›Paper›PMID 28293074›Full record

ArticleBioinformation2016

An analysis of horseradish peroxidase enzyme for effluent treatment.

Hanumalal Nunavath, Chandrasekhar Banoth, Venkateswar Rao Talluri, Bhima Bhukya

Open access · hybridAbstract read
In one paragraph

Article in Bioinformation, 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
0.7field-weighted citation impact, top 14% 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, 9 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

4 authors at 1 institution in 1 country.

Hanumalal NunavathDepartment of Microbiology, Osmania University, Hyderabad - 500 007, India.
Chandrasekhar BanothDepartment of Microbiology, Osmania University, Hyderabad - 500 007, India.
Venkateswar Rao TalluriProfessor TNA Innovation Center, VBTIPL, Sy. No.253/A, Jiblakpally, Pochampally - 508284, Nalgonda (Dist.), Telangana, India.
Bhima BhukyaDepartment of Microbiology, Osmania University, Hyderabad - 500 007, India.
Osmania University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The present study explains computational methods to design thermostable horseradish peroxidase enzyme using the crystal structure available from Protein Data Bank (PDB ID: 6ATJ). Multiple mutations were introduced to the original enzyme and developed a model by using Modeler9.14. After designing the model functional effect was confirmed in terms of protein ligand binding by molecular docking using Autodock 4.2. The implementation of modeling steps is demonstrated in the context of performing mutations for particular amino acid residue on the ligand pocket of the horseradish peroxidase, to derive the desired ligand binding properties. The docking investigation of modelled HRP with Quercetindihydroxide using Autodock 4.2 software that six amino acid residues, P139, H42, A31, L174, A38, and G169 are involved in hydrogen bonding. More importantly, it provides insight into understanding and properly interpreting the data produced by these methods. The 3D model was docked with Quercetindihydroxide (a known horseradish modulator) to understand molecular interactions at the active site region.

Indexed as

de-colourizationhomology modelinghorseradish peroxidaseindustrial effluents

Identifiers

PMID28293074
PMCPMC5322315
OpenAlexW2583810913

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.