ReviewFrontiers in immunology2017
F-Type Lectins: A Highly Diversified Family of Fucose-Binding Proteins with a Unique Sequence Motif and Structural Fold, Involved in Self/Non-Self-Recognition.
Review in Frontiers in immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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.
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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.
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Who cites it
20 citing papers in PubMed.
- Distinct cell states define larval and adult body plans in a hemichordate.Nature communications · 2026Article
- SpEchinoidin, a C-type lectin and a member of an expanded CTL family, is up-regulated by phagocytes in sea urchins responding to immune challenge.Developmental and comparative immunology · 2026Article
- Coral color morphs exhibit distinct microbial and proteomic profiles linked to stress and immune mechanisms in a changing ocean.Microbiome · 2026Article
- L-Fucose: a dietary sugar with multifaceted potential in the biology and therapy of cancer.Nature reviews. Cancer · 2026Review
- Exploring the Structural Diversity and Biotechnological Potential of the Rhodophyte Phycolectome.Marine drugs · 2024Review
- Fucose-binding lectins: purification, characterization and potential biomedical applications.Molecular biology reports · 2023Review
- Mass Spectrometry Analysis of Shark Skin Proteins.International journal of molecular sciences · 2023Review
- Proteome-wide prediction of bacterial carbohydrate-binding proteins as a tool for understanding commensal and pathogen colonisation of the vaginal microbiome.NPJ biofilms and microbiomes · 2021Article
- Review
- Human Lectins, Their Carbohydrate Affinities and Where to Find Them.Biomolecules · 2021Review
- LectomeXplore, an update of UniLectin for the discovery of carbohydrate-binding proteins based on a new lectin classification.Nucleic acids research · 2021Article
- Article
- Novel Avian Pathogenic Escherichia coli Genes Responsible for Adhesion to Chicken and Human Cell Lines.Applied and environmental microbiology · 2020Article
- Functional reprogramming ofThe Journal of biological chemistry · 2020Article
- ASGR1 and Its Enigmatic Relative, CLEC10A.International journal of molecular sciences · 2020Review
- Pregnancy Galectinology: Insights Into a Complex Network of Glycan Binding Proteins.Frontiers in immunology · 2019Review
- Theft and Reception of Host Cell's Sialic Acid: Dynamics ofFrontiers in immunology · 2019Review
- Article
- An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.Glycobiology · 2018Article
- From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.Histochemistry and cell biology · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The F-type lectin (FTL) family is one of the most recent to be identified and structurally characterized. Members of the FTL family are characterized by a fucose recognition domain [F-type lectin domain (FTLD)] that displays a novel jellyroll fold ("F-type" fold) and unique carbohydrate- and calcium-binding sequence motifs. This novel lectin family comprises widely distributed proteins exhibiting single, double, or greater multiples of the FTLD, either tandemly arrayed or combined with other structurally and functionally distinct domains, yielding lectin subunits of pleiotropic properties even within a single species. Furthermore, the extraordinary variability of FTL sequences (isoforms) that are expressed in a single individual has revealed genetic mechanisms of diversification in ligand recognition that are unique to FTLs. Functions of FTLs in self/non-self-recognition include innate immunity, fertilization, microbial adhesion, and pathogenesis, among others. In addition, although the F-type fold is distinctive for FTLs, a structure-based search revealed apparently unrelated proteins with minor sequence similarity to FTLs that displayed the FTLD fold. In general, the phylogenetic analysis of FTLD sequences from viruses to mammals reveals clades that are consistent with the currently accepted taxonomy of extant species. However, the surprisingly discontinuous distribution of FTLDs within each taxonomic category suggests not only an extensive structural/functional diversification of the FTLs along evolutionary lineages but also that this intriguing lectin family has been subject to frequent gene duplication, secondary loss, lateral transfer, and functional co-option.
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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.