Evidence map›Paper›PMID 21658216›Full record

ReviewMicrobial cell factories2011

Biotechnological applications of recombinant single-domain antibody fragments.

Ario de Marco

Abstract readReview
In one paragraph

Review in Microbial cell factories, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing 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

58 citing papers in PubMed.

  1. Domain antibody-displayed phages as a novel biofilm-targeted therapy for Staphylococcus aureus.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
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  14. Advances in the Diagnosis of Foot-and-Mouth Disease.Frontiers in veterinary science · 2020
    Review
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  20. Current Conjugation Methods for Immunosensors.Nanomaterials (Basel, Switzerland) · 2018
    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

1 author.

Ario de MarcoUniversity of Nova Gorica (UNG), Vipavska 13, PO Box 301-SI-5000, Rožna Dolina (Nova Gorica), Slovenia. ario.demarco@ung.si

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundSingle-domain antibody fragments possess structural features, such as a small dimension, an elevated stability, and the singularity of recognizing epitopes non-accessible for conventional antibodies that make them interesting for several research and biotechnological applications.

resultsThe discovery of the single-domain antibody's potentials has stimulated their use in an increasing variety of fields. The rapid accumulation of articles describing new applications and further developments of established approaches has made it, therefore, necessary to update the previous reviews with a new and more complete summary of the topic.

conclusionsBeside the necessary task of updating, this work analyses in detail some applicative aspects of the single-domain antibodies that have been overseen in the past, such as their efficacy in affinity chromatography, as co-crystallization chaperones, protein aggregation controllers, enzyme activity tuners, and the specificities of the unconventional single-domain fragments.

Indexed as

BiotechnologyBacteriaBacteriophagesFungiRecombinant ProteinsSingle-Chain AntibodiesToxins, BiologicalVirusesRecombinant ProteinsSingle-Chain AntibodiesToxins, Biological

Identifiers

PMID21658216
PMCPMC3123181

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.