Evidence map›Paper›PMID 29054528›Full record

ArticleAnalytical biochemistry2018

Using two-site binding models to analyze microscale thermophoresis data.

Shih-Chia Tso, Qiuyan Chen, Sergey A Vishnivetskiy, Vsevolod V Gurevich, T M Iverson, Chad A Brautigam

Abstract read
In one paragraph

Article in Analytical biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

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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.

Shih-Chia TsoDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA.
Qiuyan ChenDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, USA.
Sergey A VishnivetskiyDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, USA.
Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, USA.
T M IversonDepartment of Pharmacology, Vanderbilt University Medical Center, Nashville, TN, USA; Department of Biochemistry, Vanderbilt University Medical Center, Nashville, TN, USA.
Chad A BrautigamDepartment of Biophysics, The University of Texas Southwestern Medical Center, Dallas, TX, USA; Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas, TX, USA. Electronic address: chad.brautigam@utsouthwestern.edu.

Funding

Shop Module CoreP30EY008126 · NEI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Kevin L Schey · 1989 to 2026
$19.6M
STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
Structure/Function of Complex ll OxidoreductasesR01GM061606 · NIGMS · NORTHERN CALIFORNIA INSTITUTE RES &EDUC · PI CECCHINI, GARY, IVERSON, T M · 2001 to 2022
$9.1M
Mechanisms for ligand binding by serine-rich adhesins of Gram-positive pathogensR01AI106987 · NIAID · NORTHERN CALIFORNIA INSTITUTE/RES/EDU · PI IVERSON, T M, SULLAM, PAUL M. · 2014 to 2018
$3.4M
Targeted Engineering of Designer Arrestins to Regulate Cell SignalingR35GM122491 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2017 to 2021
$2.6M
Arrestin interactions with non-receptor binding partnersR01GM077561 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2007 to 2015
$2.3M
Molecular basis for arrestin-mediated signalingR01GM120569 · NIGMS · VANDERBILT UNIVERSITY · PI T M Iverson · 2016 to 2026
$1.9M
Regulation of GPCR signaling with receptor-specific arrestinsR01GM109955 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2015 to 2017
$1.1M
Mechanisms of signal bias in arrestinsR21DA043680 · NIDA · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V., IVERSON, T M · 2017 to 2018
$432k
NanoTemper Monolith NT.115 Microscale Thermophoresis (MST) instrumentS10OD021483 · OD · VANDERBILT UNIVERSITY · PI SPILLER, BENJAMIN W · 2016 to 2016
$136k
NEI NIH HHS P30 EY008126NEI NIH HHS R01 EY011500NIAID NIH HHS R01 AI106987NIDA NIH HHS R21 DA043680NIGMS NIH HHS R01 GM061606NIGMS NIH HHS R01 GM077561NIGMS NIH HHS R01 GM109955NIGMS NIH HHS R01 GM120569NIGMS NIH HHS R35 GM122491
6 · The paper itself

Abstract

The emergence of microscale thermophoresis (MST) as a technique for determining the dissociation constants for bimolecular interactions has enabled these quantities to be measured in systems that were previously difficult or impracticable. However, most models for analyses of these data featured the assumption of a simple 1:1 binding interaction. The only model widely used for multiple binding sites was the Hill equation. Here, we describe two new MST analytic models that assume a 1:2 binding scheme: the first features two microscopic binding constants (K

Indexed as

AlgorithmsModels, MolecularAdenosine MonophosphateAnimalsAptamers, Nucleotidebeta-Arrestin 2Binding SitesCattleKineticsMonte Carlo MethodMutagenesis, Site-DirectedPhytic AcidProtein BindingRecombinant ProteinsAdenosine MonophosphateAptamers, Nucleotidebeta-Arrestin 2Phytic AcidRecombinant ProteinsArrestin-3DNA aptamerMicroscale thermophoresisProtein-ligand interactionsProtein-protein interactions

Identifiers

PMID29054528
PMCPMC5906060

What OpenQuestion holds

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LicenceTDM
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.