Evidence map›Paper›PMID 33671302›Full record

ReviewBiomolecules2021

Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies.

Alessandra Zarantonello, Henrik Pedersen, Nick S Laursen, Gregers R Andersen

Open access · goldAbstract readReview
In one paragraph

Review in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Acquired drivers of C3 glomerulopathy.Clinical kidney journal · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
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

4 authors at 1 institution in 1 country.

Alessandra ZarantonelloDepartment of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark.ORCID 0000-0002-9769-2271
Henrik PedersenDepartment of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark.ORCID 0000-0003-4911-5119
Nick S LaursenDepartment of Biomedicine, Aarhus University, 8000 Aarhus, Denmark.
Gregers R AndersenDepartment of Molecular Biology and Genetics, Aarhus University, 8000 Aarhus, Denmark.
Aarhus University · DK

Funding

Lundbeckfonden R155-2015-2666Lundbeckfonden R192-2015-726Novo Nordisk Fonden NNF16OC0022058
6 · The paper itself

Abstract

The complement system is part of the innate immune response, where it provides immediate protection from infectious agents and plays a fundamental role in homeostasis. Complement dysregulation occurs in several diseases, where the tightly regulated proteolytic cascade turns offensive. Prominent examples are atypical hemolytic uremic syndrome, paroxysmal nocturnal hemoglobinuria and Alzheimer's disease. Therapeutic intervention targeting complement activation may allow treatment of such debilitating diseases. In this review, we describe a panel of complement targeting nanobodies that allow modulation at different steps of the proteolytic cascade, from the activation of the C1 complex in the classical pathway to formation of the C5 convertase in the terminal pathway. Thorough structural and functional characterization has provided a deep mechanistic understanding of the mode of inhibition for each of the nanobodies. These complement specific nanobodies are novel powerful probes for basic research and offer new opportunities for in vivo complement modulation.

Indexed as

Complement ActivationComplement System ProteinsAnimalsAntibodies, Monoclonal, HumanizedAtypical Hemolytic Uremic SyndromeComplement C1Complement C3-C5 ConvertasesEpitopesHemoglobinuria, ParoxysmalHumansImmunity, InnateImmunoglobulin GInflammationMolecular ConformationNanomedicineProtein BindingAntibodies, Monoclonal, HumanizedComplement C1Complement C3-C5 ConvertasesComplement System ProteinsEpitopesImmunoglobulin GSingle-Domain Antibodiescomplement systemconvertaseinhibitormolecular mechanismproteolytic cascadestructural biology

Identifiers

PMID33671302
PMCPMC7922070
OpenAlexW3132155949

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.