Evidence map›Paper›PMID 30707898›Full record

ArticleAnalytical biochemistry2019

A simple fluorescent assay for the discovery of protein-protein interaction inhibitors.

Mona Al-Mugotir, Carol Kolar, Krysten Vance, David L Kelly, Amarnath Natarajan, Gloria E O Borgstahl

Open access · hybridAbstract read
In one paragraph

Article in Analytical biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

8 citing papers in PubMed, 11 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

6 authors at 2 institutions in 1 country.

Mona Al-MugotirUniversity of Nebraska Medical Center, Department of Biochemistry and Molecular Biology, 985870 Nebraska Medical Center, Omaha, NE, 68198-5870, USA.
Carol KolarUniversity of Nebraska Medical Center, The Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA.
Krysten VanceUniversity of Nebraska Medical Center, The Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA.
David L KellyUniversity of Nebraska Medical Center, The Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA.
Amarnath NatarajanUniversity of Nebraska Medical Center, The Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA.
Gloria E O BorgstahlUniversity of Nebraska Medical Center, Department of Biochemistry and Molecular Biology, 985870 Nebraska Medical Center, Omaha, NE, 68198-5870, USA; University of Nebraska Medical Center, The Eppley Institute for Research in Cancer and Allied Diseases, Fred & Pamela Buffett Cancer Center, 986805 Nebraska Medical Center, Omaha, NE, 68198-6805, USA. Electronic address: gborgstahl@unmc.edu.
University of Nebraska Medical Center · USNebraska Medical Center · US

Funding

UNMC/EPPLEY CANCER CENTER SUPPORT GRANTP30CA036727 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Joann B. Sweasy · 1985 to 2026
$55.0M
TRAINING PROGRAM IN CANCER RESEARCHT32CA009035 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHERNOFF, JONATHAN · 1985 to 2020
$10.5M
CHEMICAL CARCINOGENESIS &CANCER BIOLOGYT32CA009476 · NCI · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI Jennifer D. Black · 1988 to 2026
$6.2M
NCI NIH HHS P30 CA036727NCI NIH HHS T32 CA009035NCI NIH HHS T32 CA009476
6 · The paper itself

Abstract

Due to the therapeutic potential of targeting protein-protein interactions (PPIs) there is a need for easily executed assays to perform high throughput screening (HTS) of inhibitors. We have developed and optimized an innovative and robust fluorescence-based assay for detecting PPI inhibitors, called FluorIA (Fluorescence-based protein-protein Interaction Assay). Targeting the PPI of RAD52 with replication protein A (RPA) was used as an example, and the FluorIA protocol design, optimization and successful application to HTS of large chemical libraries are described. Here enhanced green fluorescent protein (EGFP)-tagged RAD52 detected the PPI using full-length RPA heterotrimer coated, black microtiter plates and loss in fluorescence intensity identified small molecule inhibitors (SMIs) that displaced the EGFP-tagged RAD52. The FluorIA design and protocol can be adapted and applied to detect PPIs for other protein systems. This should push forward efforts to develop targeted therapeutics against protein complexes in pathological processes.

Indexed as

Protein Interaction MapsGreen Fluorescent ProteinsHigh-Throughput Screening AssaysHumansHydrogen-Ion ConcentrationProtein BindingRad52 DNA Repair and Recombination ProteinSmall Molecule LibrariesSpectrometry, Fluorescenceenhanced green fluorescent proteinGreen Fluorescent ProteinsRad52 DNA Repair and Recombination ProteinSmall Molecule LibrariesFluorescent assayHigh throughput screeningProtein-protein interactionSmall molecule inhibitor

Identifiers

PMID30707898
PMCPMC7968734
OpenAlexW2913598915

What OpenQuestion holds

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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.