Evidence map›Paper›PMID 17704915›Full record

ReviewApplied microbiology and biotechnology2007

Properties, production, and applications of camelid single-domain antibody fragments.

M M Harmsen, H J De Haard

Open access · hybridAbstract readReview
In one paragraph

Review in Applied microbiology and biotechnology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 321 papers.

0numbers the graph read from it
0cells of the map it votes in
321citing papers in PubMed
15.8field-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

321 citing papers in PubMed, 795 citations in OpenAlex.

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261 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

2 authors at 2 institutions in 2 countries.

M M HarmsenInstitute for Animal Science and Health (ID-Lelystad) of Wageningen University and Research Centre, Edelhertweg 15, Lelystad, The Netherlands. michiel.harmsen@wur.nl
H J De Haard
Ablynx (Belgium) · BEWageningen University & Research · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Camelids produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. These single-domain antibody fragments (VHHs or Nanobodies) have several advantages for biotechnological applications. They are well expressed in microorganisms and have a high stability and solubility. Furthermore, they are well suited for construction of larger molecules and selection systems such as phage, yeast, or ribosome display. This minireview offers an overview of (1) their properties as compared to conventional antibodies, (2) their production in microorganisms, with a focus on yeasts, and (3) their therapeutic applications.

Indexed as

AnimalsCamelids, New WorldImmunoglobulin FragmentsImmunoglobulin Heavy ChainsModels, BiologicalImmunoglobulin FragmentsImmunoglobulin Heavy Chains

Identifiers

PMID17704915
PMCPMC2039825
OpenAlexW2147451568

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.