Evidence map›Paper›PMID 29520274›Full record

ReviewFrontiers in immunology2018

Single-Domain Antibodies and the Promise of Modular Targeting in Cancer Imaging and Treatment.

María Elena Iezzi, Lucía Policastro, Santiago Werbajh, Osvaldo Podhajcer, Gabriela Alicia Canziani

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
9.5field-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

45 citing papers in PubMed, 86 citations in OpenAlex.

  1. Trial
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  4. A high-affinity CEA-targeted nanobody forJournal of nanobiotechnology · 2025
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  19. VInternational journal of molecular sciences · 2022
    Review
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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

5 authors at 3 institutions in 1 country.

María Elena IezziLaboratorio de Terapia Molecular y Celular, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
Lucía PolicastroLaboratorio de Terapia Molecular y Celular, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
Santiago WerbajhLaboratorio de Terapia Molecular y Celular, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
Osvaldo PodhajcerLaboratorio de Terapia Molecular y Celular, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
Gabriela Alicia CanzianiLaboratorio de Terapia Molecular y Celular, Fundación Instituto Leloir, Instituto de Investigaciones Bioquímicas de Buenos Aires (IIBBA-CONICET), Ciudad Autónoma de Buenos Aires, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARFundación Instituto Leloir · ARComisión Nacional de Energía Atómica · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monoclonal antibodies and their fragments have significantly changed the outcome of cancer in the clinic, effectively inhibiting tumor cell proliferation, triggering antibody-dependent immune effector cell activation and complement mediated cell death. Along with a continued expansion in number, diversity, and complexity of validated tumor targets there is an increasing focus on engineering recombinant antibody fragments for lead development. Single-domain antibodies (sdAbs), in particular those engineered from the variable heavy-chain fragment (VHH gene) found in Camelidae heavy-chain antibodies (or IgG2 and IgG3), are the smallest fragments that retain the full antigen-binding capacity of the antibody with advantageous properties as drugs. For similar reasons, growing attention is being paid to the yet smaller variable heavy chain new antigen receptor (VNAR) fragments found in Squalidae. sdAbs have been selected, mostly from immune VHH libraries, to inhibit or modulate enzyme activity, bind soluble factors, internalize cell membrane receptors, or block cytoplasmic targets. This succinct review is a compilation of recent data documenting the application of engineered, recombinant sdAb in the clinic as epitope recognition "modules" to build monomeric, dimeric and multimeric ligands that target, tag and stall solid tumor growth

Indexed as

AnimalsClinical Trials as TopicDiagnostic ImagingEpitopesHumansImmunotherapyMolecular Targeted TherapyNeoplasmsProtein EngineeringSingle-Domain AntibodiesEpitopesSingle-Domain Antibodiesbioavailabilitybroad epitope coveragecamelid heavy-chain antibodydrug-like propertiesimmunogenicitypoly-specificity

Identifiers

PMID29520274
PMCPMC5827546
OpenAlexW2789368548

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.