Evidence map›Paper›PMID 42663952›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

A Selective Activity-Based Approach for Analysis of Enzymes with an OmpG Nanopore.

Monifa A V Fahie, Bach Pham, Fanjun Li, Min Chen

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Monifa A V FahieMolecular and Cellular Biology Program; University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Bach PhamDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Fanjun LiDepartment of Chemistry, University of Massachusetts Amherst, Amherst, MA, 01003, USA.
Min ChenMolecular and Cellular Biology Program; University of Massachusetts Amherst, Amherst, MA, 01003, USA. mchen1@umass.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many enzymatic activity assays are based on either (i) identifying and quantifying the enzyme with methods such as western blot or enzyme linked substrate assay (ELISA) or (ii) quantifying the enzymatic reaction by monitoring the changing levels of either product or substrate with techniques such as mass spectrometry, absorption or fluorescence spectroscopy, thin layer chromatography, luminescence, and more. We have generated outer membrane protein G (OmpG)-based nanopore approaches to distinguish enzyme identity and analyze the enzyme's catalytic activity. Here, we engineered an OmpG nanopore with a peptide cut site inserted into one of its loops to detect proteolytic behavior. In addition, we generated an OmpG nanopore with a single-stranded DNA attached to a loop for analyzing nucleolytic cleavage. These OmpG nanopore approaches may be highly useful in analyzing specific enzymes in complex biological samples, or in directly determining kinetics of enzyme-substrate complex association and dissociation.

Indexed as

Bacterial Outer Membrane ProteinsEnzyme AssaysEscherichia coli ProteinsNanoporesPorinsEscherichia coliKineticsProtein EngineeringSubstrate SpecificityBacterial Outer Membrane ProteinsEscherichia coli ProteinsOmpG protein, E coliPorinsCaspaseDNA ligandEnzyme activity sensorENzyme-substrate complexNanopore engineering/designNucleaseOmpGPeptide substrateProteaseSingle channel recording

Identifiers

PMID42663952

What OpenQuestion holds

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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.