Evidence map›Paper›PMID 38285057›Full record

ArticleEuropean journal of histochemistry : EJH2024

Lectins as versatile tools to explore cellular glycosylation.

Susan Brooks

Open access · goldAbstract read
In one paragraph

Article in European journal of histochemistry : EJH, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. Antitumor effects of a lectin purified fromFrontiers in oncology · 2026
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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

1 author at 1 institution in 1 country.

Susan BrooksOxford Brookes University, Oxford. sbrooks@brookes.ac.uk.
Oxford Brookes University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are naturally occurring carbohydrate-binding proteins that are ubiquitous in nature and highly selective for their, often incompletely characterised, binding partners. From their discovery in the late 1880s to the present day, they have provided a broad palette of versatile tools for exploring the glycosylation of cells and tissues and for uncovering the myriad functions of glycosylation in biological systems. The technique of lectin histochemistry, used to map the glycosylation of tissues, has been instrumental in revealing the changing profile of cellular glycosylation in development, health and disease. It has been especially enlightening in revealing fundamental alterations in cellular glycosylation that accompany cancer development and metastasis, and has facilitated the identification of glycosylated biomarkers that can predict prognosis and may have utility in development of early detection and screening, Moreover, it has led to insights into the functional role of glycosylation in healthy tissues and in the processes underlying disease. Recent advances in biotechnology mean that our understanding of the precise binding partners of lectins is improving and an ever-wider range of lectins are available, including recombinant human lectins and lectins with enhanced, engineered properties. Moreover, use of traditional histochemistry to support a broad range of cutting-edge technologies and the development of high throughout microarray platforms opens the way for ever more sophisticated mapping - and understanding - of the glycome.

Indexed as

LectinsGlycosylationHistocytochemistryHumansLectins

Identifiers

PMID38285057
PMCPMC11059468
OpenAlexW4391314202

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.