Evidence map›Paper›PMID 19529959›Full record

ReviewMedical microbiology and immunology2009

Single domain antibodies: promising experimental and therapeutic tools in infection and immunity.

Janusz Wesolowski, Vanina Alzogaray, Jan Reyelt, Mandy Unger, Karla Juarez, Mariela Urrutia, Ana Cauerhff, Welbeck Danquah, Björn Rissiek, Felix Scheuplein and 9 more

Open access · hybridAbstract readReview
In one paragraph

Review in Medical microbiology and immunology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed
22.2field-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

246 citing papers in PubMed, 501 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Article
  5. Adaptive Disorder as the Hallmark of Nanobodies Antigen-Binding Loops.Journal of chemical information and modeling · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. VNpj viruses · 2025
    Article
  14. Article
  15. Review
  16. Article
  17. Modulating ion channels with nanobodies.Synthetic and systems biotechnology · 2025
    Review
  18. Article
  19. Article
  20. Article

186 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

19 authors at 8 institutions in 5 countries.

Janusz WesolowskiInstitute of Immunology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
Vanina Alzogaray
Jan Reyelt
Mandy Unger
Karla Juarez
Mariela Urrutia
Ana Cauerhff
Welbeck Danquah
Björn Rissiek
Felix Scheuplein
Nicole Schwarz
Sahil Adriouch
Olivier Boyer
Michel Seman
Alexei Licea
David V Serreze
Fernando A Goldbaum
Friedrich Haag
Friedrich Koch-Nolte
University Medical Center Hamburg-Eppendorf · DEUniversität Hamburg · DEConsejo Nacional de Investigaciones Científicas y Técnicas · ARJackson Laboratory · USUniversité de Rouen Normandie · FRCenter for Scientific Research and Higher Education at Ensenada · MXFundación Instituto Leloir · ARInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibodies are important tools for experimental research and medical applications. Most antibodies are composed of two heavy and two light chains. Both chains contribute to the antigen-binding site which is usually flat or concave. In addition to these conventional antibodies, llamas, other camelids, and sharks also produce antibodies composed only of heavy chains. The antigen-binding site of these unusual heavy chain antibodies (hcAbs) is formed only by a single domain, designated VHH in camelid hcAbs and VNAR in shark hcAbs. VHH and VNAR are easily produced as recombinant proteins, designated single domain antibodies (sdAbs) or nanobodies. The CDR3 region of these sdAbs possesses the extraordinary capacity to form long fingerlike extensions that can extend into cavities on antigens, e.g., the active site crevice of enzymes. Other advantageous features of nanobodies include their small size, high solubility, thermal stability, refolding capacity, and good tissue penetration in vivo. Here we review the results of several recent proof-of-principle studies that open the exciting perspective of using sdAbs for modulating immune functions and for targeting toxins and microbes.

Indexed as

Amino Acid SequenceAnimalsAntibodiesCamelids, New WorldComplementarity Determining RegionsImmunoglobulin Heavy ChainsMolecular ConformationMolecular Sequence DataRecombinant ProteinsSequence AlignmentSharksAntibodiesComplementarity Determining RegionsImmunoglobulin Heavy ChainsRecombinant Proteins

Identifiers

PMID19529959
PMCPMC2714450
OpenAlexW2120929471

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.