Evidence map›Paper›PMID 20140750›Full record

ArticleCellular and molecular life sciences : CMLS2010

A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.

Anske Van den Abbeele, Sarah De Clercq, Ariane De Ganck, Veerle De Corte, Berlinda Van Loo, Sameh Hamdy Soror, Vasundara Srinivasan, Jan Steyaert, Joël Vandekerckhove, Jan Gettemans

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 67 citations in OpenAlex.

  1. A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026
    Review
  2. Article
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  7. Review
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  9. Review
  10. Resolving the topological enigma in CaThe Journal of biological chemistry · 2019
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Advances in targeted degradation of endogenous proteins.Cellular and molecular life sciences : CMLS · 2019
    Review
  16. Article
  17. Article
  18. Reporter-nanobody fusions (RANbodies) as versatile, small, sensitive immunohistochemical reagents.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Structural basis for GABANature structural & molecular biology · 2017
    Article
  20. Single domain antibodies for the knockdown of cytosolic and nuclear proteins.Protein science : a publication of the Protein Society · 2017
    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

10 authors at 3 institutions in 1 country.

Anske Van den AbbeeleDepartment of Medical Protein Research, VIB, 9000 Ghent, Belgium.
Sarah De Clercq
Ariane De Ganck
Veerle De Corte
Berlinda Van Loo
Sameh Hamdy Soror
Vasundara Srinivasan
Jan Steyaert
Joël Vandekerckhove
Jan Gettemans
VIB-UGent Center for Medical Biotechnology · BEVIB-VUB Center for Structural Biology · BEGhent University · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA interference has tremendously advanced our understanding of gene function but recent reports have exposed undesirable side-effects. Recombinant Camelid single-domain antibodies (VHHs) provide an attractive means for studying protein function without affecting gene expression. We raised VHHs against gelsolin (GsnVHHs), a multifunctional actin-binding protein that controls cellular actin organization and migration. GsnVHH-induced delocalization of gelsolin to mitochondria or the nucleus in mammalian cells reveals distinct subpopulations including free gelsolin and actin-bound gelsolin complexes. GsnVHH 13 specifically recognizes Ca(2+)-activated gelsolin (K (d) approximately 10 nM) while GsnVHH 11 binds gelsolin irrespective of Ca(2+) (K (d) approximately 5 nM) but completely blocks its interaction with G-actin. Both GsnVHHs trace gelsolin in membrane ruffles of EGF-stimulated MCF-7 cells and delay cell migration without affecting F-actin severing/capping or actin nucleation activities by gelsolin. We conclude that VHHs represent a potent way of blocking structural proteins and that actin nucleation by gelsolin is more complex than previously anticipated.

Indexed as

Protein Structure, TertiaryActinsAnimalsCalciumCamelids, New WorldCell LineCell MovementCrystallography, X-RayEpitopesGelsolinHumansMitochondriaModels, MolecularMolecular Sequence DataRecombinant Fusion ProteinsSingle-Chain AntibodiesActinsCalciumEpitopesGelsolinRecombinant Fusion ProteinsSingle-Chain Antibodies

Identifiers

PMID20140750
PMCPMC11115616
OpenAlexW2097884340

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.