A Fluorescence-Based Assay to Determine PDZ-Ligand Binding Thermodynamics.

Young Joo Sun, Ernesto J Fuentes

Open access · greenAbstract read

In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. 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

–field-weighted citation impact, top 90% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

2 authors at 1 institution in 1 country.

Young Joo SunDepartment of Biochemistry, University of Iowa, Iowa City, IA, USA.

Ernesto J FuentesDepartment of Biochemistry, University of Iowa, Iowa City, IA, USA. ernesto-fuentes@uiowa.edu.

University of Iowa · US

Funding

PAS domain and redox regulation of the S. aureus SrrB sensor histidine kinaseR21AI135305 · NIAID · UNIVERSITY OF IOWA · PI FUENTES, ERNESTO JORGE · 2018 to 2019

$417k

NIAID NIH HHS R21 AI135305

6 · The paper itself

Abstract

Postsynaptic density-95, disks-large, and zonula occludens-1 (PDZ) domain interactions with cognate linear binding motifs (i.e., PDZ-binding motifs or PBMs) are important for many biological processes and can be pathological when disrupted. There are hundreds of PDZ-PBM interactions reported but few have been quantitatively determined. Moreover, PDZ-PBM interactions have been identified as potential therapeutic targets. To thoroughly understand PDZ-PBM binding energetics and their specificity, we have developed a sensitive and quantitative equilibrium binding assay. Here, we describe a protocol for determining PDZ-PBM binding energetics using fluorescence anisotropy-based methodology.

Indexed as

FluorescencePDZ DomainsThermodynamicsAmino Acid MotifsBinding SitesFluorescence PolarizationGuanylate KinasesHumansLigandsMembrane ProteinsTumor Suppressor ProteinsCASK kinasesGuanylate KinasesLigandsMembrane ProteinsSCRIB protein, humanTumor Suppressor ProteinsCASKFluorescence anisotropyPDZ-binding motifPDZ domainProtein–protein bindingScribbleSGEF

Identifiers

PMID34014520

DOI10.1007/978-1-0716-1166-1_8

PMCPMC8507397

OpenAlexW3163510022

What OpenQuestion holds

Textmetadata

LicenceTDM

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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.