Evidence map›Paper›PMID 32610042›Full record

ArticleCell chemical biology2020

Monitoring Allosteric Interactions with CXCR4 Using NanoBiT Conjugated Nanobodies.

Mark Soave, Raimond Heukers, Barrie Kellam, Jeanette Woolard, Martine J Smit, Stephen J Briddon, Stephen J Hill

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. NanoBCell reports methods · 2023
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Probing GPCR Dimerization Using Peptides.Frontiers in endocrinology · 2022
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  17. 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

7 authors at 3 institutions in 2 countries.

Mark SoaveDivision of Physiology, Pharmacology and Neuroscience, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK; Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, The Midlands, UK.
Raimond HeukersDivision of Medicinal Chemistry, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University of Amsterdam, De Boelelaan 1108, 1081 HZ Amsterdam, the Netherlands; QVQ Holding B.V., Yalelaan 1, 3584 CL Utrecht, the Netherlands.
Barrie KellamCentre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, The Midlands, UK; School of Pharmacy, Biodiscovery Institute, University of Nottingham, Nottingham NG7 2RD, UK.
Jeanette WoolardDivision of Physiology, Pharmacology and Neuroscience, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK; Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, The Midlands, UK.
Martine J SmitDivision of Medicinal Chemistry, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University of Amsterdam, De Boelelaan 1108, 1081 HZ Amsterdam, the Netherlands.
Stephen J BriddonDivision of Physiology, Pharmacology and Neuroscience, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK; Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, The Midlands, UK.
Stephen J HillDivision of Physiology, Pharmacology and Neuroscience, School of Life Sciences, University of Nottingham, Nottingham NG7 2UH, UK; Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, The Midlands, UK. Electronic address: stephen.hill@nottingham.ac.uk.
University of Nottingham · GBQserve Group (Netherlands) · NLVrije Universiteit Amsterdam · NL

Funding

Medical Research Council MR/N020081/1
6 · The paper itself

Abstract

Camelid single-domain antibody fragments (nanobodies) offer the specificity of an antibody in a single 15-kDa immunoglobulin domain. Their small size allows for easy genetic manipulation of the nanobody sequence to incorporate protein tags, facilitating their use as biochemical probes. The nanobody VUN400, which recognizes the second extracellular loop of the human CXCR4 chemokine receptor, was used as a probe to monitor specific CXCR4 conformations. VUN400 was fused via its C terminus to the 11-amino-acid HiBiT tag (VUN400-HiBiT) which complements LgBiT protein, forming a full-length functional NanoLuc luciferase. Here, complemented luminescence was used to detect VUN400-HiBiT binding to CXCR4 receptors expressed in living HEK293 cells. VUN400-HiBiT binding to CXCR4 could be prevented by orthosteric and allosteric ligands, allowing VUN400-HiBiT to be used as a probe to detect allosteric interactions with CXCR4. These data demonstrate that the high specificity offered by extracellular targeted nanobodies can be utilized to probe receptor pharmacology.

Indexed as

Allosteric RegulationCells, CulturedHumansLuciferasesLuminescent MeasurementsNanoparticlesReceptors, CXCR4Single-Domain AntibodiesCXCR4 protein, humanLuciferasesReceptors, CXCR4Single-Domain Antibodiesallosterismchemokine receptorCXCR4extracellular loop 2NanoBiTnanobodiesNanoLuciferase

Identifiers

PMID32610042
PMCPMC7573392
OpenAlexW3037419359

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.