Evidence map›Paper›PMID 37999394›Full record

ReviewMarine drugs2023

Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential.

Andrei Grinchenko, Ivan Buriak, Vadim Kumeiko

Open access · goldAbstract readReview
In one paragraph

Review in Marine drugs, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

2 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Proteomic Analysis ofAntibiotics (Basel, Switzerland) · 2024
    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

3 authors at 1 institution in 1 country.

Andrei GrinchenkoSchool of Medicine and Life Sciences, Far Eastern Federal University, 690922 Vladivostok, Russia.ORCID 0000-0002-0276-013X
Ivan BuriakSchool of Medicine and Life Sciences, Far Eastern Federal University, 690922 Vladivostok, Russia.ORCID 0000-0003-3485-8024
Vadim KumeikoSchool of Medicine and Life Sciences, Far Eastern Federal University, 690922 Vladivostok, Russia.ORCID 0000-0002-1639-664X
Far Eastern Federal University · RU

Funding

Ministry of Science and Higher Education of the Russian Federation FZNS-2023-0017Russian Federal Academic Leadership Program Priority 2030
6 · The paper itself

Abstract

C1q domain-containing proteins (C1qDC proteins) unexpectedly turned out to be widespread molecules among a variety of invertebrates, despite their lack of an integral complement system. Despite the wide distribution in the genomes of various invertebrates, data on the structure and properties of the isolated and characterized C1qDC proteins, which belong to the C1q/TNF superfamily, are sporadic, although they hold great practical potential for the creation of new biotechnologies. This review not only summarizes the current data on the properties of already-isolated or bioengineered C1qDC proteins but also projects further strategies for their study and biomedical application. It has been shown that further broad study of the carbohydrate specificity of the proteins can provide great opportunities, since for many of them only interactions with pathogen-associated molecular patterns (PAMPs) was evaluated and their antimicrobial, antiviral, and fungicidal activities were studied. However, data on the properties of C1qDC proteins, which researchers originally discovered as lectins and therefore studied their fine carbohydrate specificity and antitumor activity, intriguingly show the great potential of this family of proteins for the creation of targeted drug delivery systems, vaccines, and clinical assays for the differential diagnosis of cancer. The ability of invertebrate C1qDC proteins to recognize patterns of aberrant glycosylation of human cell surfaces and interact with mammalian immunoglobulins indicates the great biomedical potential of these molecules.

Indexed as

Complement C1qInvertebratesAmino Acid SequenceAnimalsCarbohydratesHumansMammalsMolecular StructureCarbohydratesComplement C1qC1q/TNF superfamilycancercarbohydrate-binding proteinsclinical diagnosticsdrug deliveryglycosylationlectin

Identifiers

PMID37999394
PMCPMC10672478
OpenAlexW4388019551

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.