Evidence map›Paper›PMID 26745729›Full record

ArticlePloS one2016

Development and Application of a High Throughput Protein Unfolding Kinetic Assay.

Qiang Wang, Nicklas Waterhouse, Olusegun Feyijinmi, Matthew J Dominguez, Lisa M Martinez, Zoey Sharp, Rachel Service, Jameson R Bothe, Elliott J Stollar

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. How a highly acidic SH3 domain folds in the absence of its charged peptide target.Protein science : a publication of the Protein Society · 2023
    Article
  3. 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 1 country.

Qiang WangDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Nicklas WaterhouseDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Olusegun FeyijinmiDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Matthew J DominguezDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Lisa M MartinezDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Zoey SharpDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Rachel ServiceDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Jameson R BotheNMRFAM, University of Wisconsin-Madison, Madison, Wisconsin, United States of America.
Elliott J StollarDepartment of Physical Sciences, Eastern New Mexico University, Portales, New Mexico, United States of America.
Eastern New Mexico University · USUniversity of Wisconsin–Madison · US

Funding

NM-INBRE Sequencing and Bioinformatics CoreP20GM103451 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI Charlotte C. Gard · 2012 to 2026
$61.2M
TR&D 3: TECHNOLOGY DEVELOPMENT FOR NMR STUDIES OF SMALL MOLECULES (METABOLOMICS, NATURAL PRODUCTS, METABOLITE-PROTEIN INTERACTIONS) pp.537-585 P41GM103399 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2012 to 2019
$9.4M
Small Angle X-ray Scattering InstrumentS10RR027000 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI BUTCHER, SAMUEL E · 2011 to 2011
$307k
NCRR NIH HHS S10 RR027000NCRR NIH HHS S10RR027000NIGMS NIH HHS 8P20GM103451NIGMS NIH HHS P20 GM103451NIGMS NIH HHS P41 GM103399NIGMS NIH HHS P41GM103399
6 · The paper itself

Abstract

The kinetics of folding and unfolding underlie protein stability and quantification of these rates provides important insights into the folding process. Here, we present a simple high throughput protein unfolding kinetic assay using a plate reader that is applicable to the studies of the majority of 2-state folding proteins. We validate the assay by measuring kinetic unfolding data for the SH3 (Src Homology 3) domain from Actin Binding Protein 1 (AbpSH3) and its stabilized mutants. The results of our approach are in excellent agreement with published values. We further combine our kinetic assay with a plate reader equilibrium assay, to obtain indirect estimates of folding rates and use these approaches to characterize an AbpSH3-peptide hybrid. Our high throughput protein unfolding kinetic assays allow accurate screening of libraries of mutants by providing both kinetic and equilibrium measurements and provide a means for in-depth ϕ-value analyses.

Indexed as

Chromatography, GelGuanidineHigh-Throughput Screening AssaysKineticsMicrofilament ProteinsModels, MolecularProtein DenaturationProtein StabilityProteolysisScattering, Small AngleSolutionssrc Homology DomainsThermodynamicsX-Ray DiffractionGuanidineMicrofilament ProteinsSolutions

Identifiers

PMID26745729
PMCPMC4706425
OpenAlexW2238146247

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.