Evidence map›Paper›PMID 32106676›Full record

ArticleAnalytical chemistry2020

Homogeneous Dual-Parametric-Coupled Assay for Simultaneous Nucleotide Exchange and KRAS/RAF-RBD Interaction Monitoring.

Kari Kopra, Emmiliisa Vuorinen, Maria Abreu-Blanco, Qi Wang, Ville Eskonen, William Gillette, Arto T Pulliainen, Matthew Holderfield, Harri Härmä

Open access · hybridAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  6. NMRBiomolecular NMR assignments · 2025
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  18. Review
  19. Production of Isotopically Labeled KRAS4b.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  20. 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

9 authors at 2 institutions in 2 countries.

Kari KopraMaterials Chemistry and Chemical Analysis, University of Turku, Vatselankatu 2, 20500 Turku, Finland.ORCID 0000-0001-7585-6020
Emmiliisa VuorinenMaterials Chemistry and Chemical Analysis, University of Turku, Vatselankatu 2, 20500 Turku, Finland.
Maria Abreu-BlancoLeidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, 8560 Progress Dr., Frederick, Maryland 21702, United States.
Qi WangInstitute of Biomedicine, University of Turku, Kiinamyllynkatu 10, 20520 Turku, Finland.
Ville EskonenMaterials Chemistry and Chemical Analysis, University of Turku, Vatselankatu 2, 20500 Turku, Finland.ORCID 0000-0001-5214-5904
William GilletteLeidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, 8560 Progress Dr., Frederick, Maryland 21702, United States.
Arto T PulliainenInstitute of Biomedicine, University of Turku, Kiinamyllynkatu 10, 20520 Turku, Finland.ORCID 0000-0002-9361-8963
Matthew HolderfieldLeidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, 8560 Progress Dr., Frederick, Maryland 21702, United States.
Harri HärmäMaterials Chemistry and Chemical Analysis, University of Turku, Vatselankatu 2, 20500 Turku, Finland.ORCID 0000-0002-8936-039X
University of Turku · FILeidos (United States) · US

Funding

CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

We have developed a rapid and sensitive single-well dual-parametric method introduced in linked RAS nucleotide exchange and RAS/RAF-RBD interaction assays. RAS mutations are frequent drivers of multiple different human cancers, but the development of therapeutic strategies has been challenging. Traditionally, efforts to disrupt the RAS function have focused on nucleotide exchange inhibitors, GTP-RAS interaction inhibitors, and activators increasing GTPase activity of mutant RAS proteins. As the amount of biological knowledge grows, targeted biochemical assays enabling high-throughput screening have become increasingly interesting. We have previously introduced a homogeneous quenching resonance energy transfer (QRET) assay for nucleotide binding studies with RAS and heterotrimeric G proteins. Here, we introduce a novel homogeneous signaling technique called QTR-FRET, which combine QRET technology and time-resolved Förster resonance energy transfer (TR-FRET). The dual-parametric QTR-FRET technique enables the linking of guanine nucleotide exchange factor-induced Eu

Indexed as

Fluorescence Resonance Energy TransferGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHumansProto-Oncogene Proteins c-rafProto-Oncogene Proteins p21(ras)Guanine Nucleotide Exchange FactorsGuanosine TriphosphateKRAS protein, humanProto-Oncogene Proteins c-rafProto-Oncogene Proteins p21(ras)

Identifiers

PMID32106676
PMCPMC7143314
OpenAlexW3007721372

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.