Evidence map›Paper›PMID 21812660›Full record

ReviewAssay and drug development technologies2011

Molecular interaction studies using microscale thermophoresis.

Moran Jerabek-Willemsen, Chistoph J Wienken, Dieter Braun, Philipp Baaske, Stefan Duhr

Open access · hybridAbstract readReview
In one paragraph

Review in Assay and drug development technologies, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 399 papers.

0numbers the graph read from it
0cells of the map it votes in
399citing papers in PubMed
29.3field-weighted citation impact, top 1% 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

399 citing papers in PubMed, 798 citations in OpenAlex.

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  13. Precision Aptamers Against a Native GPCR through Ligand-Guided Selection.bioRxiv : the preprint server for biology · 2026
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339 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Moran Jerabek-WillemsenSystems Biophysics, Center for Nanoscience, Munich, Germany.
Chistoph J Wienken
Dieter Braun
Philipp Baaske
Stefan Duhr
Center for NanoScience · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abstract The use of infrared laser sources for creation of localized temperature fields has opened new possibilities for basic research and drug discovery. A recently developed technology, Microscale Thermophoresis (MST), uses this temperature field to perform biomolecular interaction studies. Thermophoresis, the motion of molecules in temperature fields, is very sensitive to changes in size, charge, and solvation shell of a molecule and thus suited for bioanalytics. This review focuses on the theoretical background of MST and gives a detailed overview on various applications to demonstrate the broad applicability. Experiments range from the quantification of the affinity of low-molecular-weight binders using fluorescently labeled proteins, to interactions between macromolecules and multi-component complexes like receptor containing liposomes. Information regarding experiment and experimental setup is based on the Monolith NT.115 instrument (NanoTemper Technologies GmbH).

Indexed as

Biophysical PhenomenaChemistry Techniques, AnalyticalHumansInfrared RaysMolecular ConformationMotionProteinsSurface Plasmon ResonanceTemperatureProteins

Identifiers

PMID21812660
PMCPMC3148787
OpenAlexW2114160655

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.