Evidence map›Paper›PMID 32814367›Full record

ReviewAnnals of the New York Academy of Sciences2020

Enhancing organophosphate hydrolase efficacy via protein engineering and immobilization strategies.

Priya Katyal, Stanley Chu, Jin Kim Montclare

Abstract readReview
In one paragraph

Review in Annals of the New York Academy of Sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
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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

3 authors.

Priya KatyalDepartment of Chemical and Biomolecular Engineering, New York University, Tandon School of Engineering, Brooklyn, New York.
Stanley ChuDepartment of Chemical and Biomolecular Engineering, New York University, Tandon School of Engineering, Brooklyn, New York.
Jin Kim MontclareDepartment of Chemical and Biomolecular Engineering, New York University, Tandon School of Engineering, Brooklyn, New York.ORCID 0000-0001-6857-3591

Funding

Computationally Designed Stable Artificial Phosphotriesterases for Detoxification of Organophosphorus AgentsR21NS103831 · NINDS · NEW YORK UNIVERSITY · PI MONTCLARE, JIN KIM · 2017 to 2018
$349k
NINDS NIH HHS R21 NS103831
6 · The paper itself

Abstract

Organophosphorus compounds (OPs), developed as pesticides and chemical warfare agents, are extremely toxic chemicals that pose a public health risk. Of the different detoxification strategies, organophosphate-hydrolyzing enzymes have attracted much attention, providing a potential route for detoxifying those exposed to OPs. Phosphotriesterase (PTE), also known as organophosphate hydrolase (OPH), is one such enzyme that has been extensively studied as a catalytic bioscavenger. In this review, we will discuss the protein engineering of PTE aimed toward improving the activity and stability of the enzyme. In order to make enzyme utilization in OP detoxification more favorable, enzyme immobilization provides an effective means to increase enzyme activity and stability. Here, we present several such strategies that enhance the storage and operational stability of PTE/OPH.

Indexed as

Enzymes, ImmobilizedPhosphoric Monoester HydrolasesProtein EngineeringCatalysisChemical Warfare AgentsHumansHydrolysisOrganophosphorus CompoundsPesticidesChemical Warfare AgentsEnzymes, ImmobilizedOrganophosphorus CompoundsPesticidesPhosphoric Monoester Hydrolasesphosphorylphosphatasechemical warfare agentsorganophosphate hydrolaseorganophosphatesorganophosphorus compoundspesticidesphosphotriesterase

Identifiers

PMID32814367
PMCPMC7771632

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Registered trials

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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.