Evidence map›Paper›PMID 37340471›Full record

ArticleBMC research notes2023

Extreme thermal stability of the antiGFP nanobody - GFP complex.

Balázs Kakasi, Eszter Gácsi, Hajnalka Jankovics, Ferenc Vonderviszt

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC research notes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
  2. Review
  3. Tuning Polyacrylate Composition to Recognize and Modulate Fluorescent Proteins.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Review
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

4 authors.

Balázs KakasiBio-Nanosystems Laboratory, Research Institute of Biomolecular and Chemical Engineering, Faculty of Engineering, University of Pannonia, Veszprém, Hungary.
Eszter GácsiBio-Nanosystems Laboratory, Research Institute of Biomolecular and Chemical Engineering, Faculty of Engineering, University of Pannonia, Veszprém, Hungary.
Hajnalka JankovicsBio-Nanosystems Laboratory, Research Institute of Biomolecular and Chemical Engineering, Faculty of Engineering, University of Pannonia, Veszprém, Hungary.
Ferenc VondervisztBio-Nanosystems Laboratory, Research Institute of Biomolecular and Chemical Engineering, Faculty of Engineering, University of Pannonia, Veszprém, Hungary. vonderviszt.ferenc@mk.uni-pannon.hu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveThe green fluorescent protein (GFP) and its derivatives are widely used in biomedical research. The manipulation of GFP-tagged proteins by GFP-specific binders, e.g. single-domain antibodies (nanobodies), is of increasing significance. It is therefore important to better understand the properties of antiGFP-GFP interaction in order to establish methodological applications. In this work the interaction of superfolder GFP (sfGFP) and its enhancer nanobody (aGFP

resultsPrevious calorimetric experiments demonstrated that the aGFP

Indexed as

Green Fluorescent ProteinsSingle-Domain AntibodiesProtein StabilityTemperatureGreen Fluorescent ProteinsSingle-Domain AntibodiesCDFluorescenceGFP enhancer nanobodyStructural stabilitySuperfolder GFP

Identifiers

PMID37340471
PMCPMC10283196

What OpenQuestion holds

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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.