ReviewInternational journal of molecular sciences2018
ConA-Like Lectins: High Similarity Proteins as Models to Study Structure/Biological Activities Relationships.
Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
25 citing papers in PubMed, 1 synthesis or guideline pooled it, 71 citations in OpenAlex.
- Tandem-repeat lectins: structural and functional insights.Glycobiology · 2024Pooled it
- Homo-oligomeric forms of lectins: their structural insights for glycan binding from the genus Canavalia.Glycoconjugate journal · 2026Article
- Immunomodulatory and Antimicrobial Effects of Pd(II)-Pincer-Type Complex.Biomedicines · 2026Article
- Altering the carbohydrate-binding specificity of the legume lectin FRIL through structure-guided engineering.Nature communications · 2026Article
- Applications of Plant Lectins in Detection and Targeted Therapy of Urological Cancers.Drug design, development and therapy · 2026Review
- Characterization of a NovelInternational journal of molecular sciences · 2025Article
- Concanavalin-A-assisted extraction-free one-pot RPA-CRISPR/Cas12a assay for rapid detection of HPV16.Mikrochimica acta · 2025Article
- Structural and Functional Analysis of the Lectin-like Protein Llp1 Secreted byJournal of fungi (Basel, Switzerland) · 2025Article
- Structural and Phylogenetic In Silico Characterization ofInternational journal of molecular sciences · 2024Article
- Adverse Food Reactions: Physiological and Ecological Perspectives.Annual review of nutrition · 2024Review
- Recent Insights into Glucose-Responsive Concanavalin A-Based Smart Hydrogels for Controlled Insulin Delivery.Gels (Basel, Switzerland) · 2024Review
- Computational insights into the circular permutation roles on ConA binding and structural stability.Current research in structural biology · 2024Article
- Structural Analysis and Characterization of an Antiproliferative Lectin fromInternational journal of molecular sciences · 2023Article
- Broadly neutralizing antibody epitopes on HIV-1 particles are exposed after virus interaction with host cells.Journal of virology · 2023Article
- The evolving biology of cross-presentation.Seminars in immunology · 2023Review
- The lectin DrfL inhibits cell migration, adhesion and triggers autophagy-dependent cell death in glioma cells.Glycoconjugate journal · 2023Article
- Concanavalin A inhibits human liver cancer cell migration by regulating F-actin redistribution and assembly via MAPK signaling pathway.Oncology letters · 2022Article
- How abiotic stress-induced socialization leads to the formation of massive aggregates in Chlamydomonas.Plant physiology · 2022Article
- Concanavalin A as a promising lectin-based anti-cancer agent: the molecular mechanisms and therapeutic potential.Cell communication and signaling : CCS · 2022Review
- Structural Prediction and Characterization ofMolecules (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Lectins are a widely studied group of proteins capable of specific and reversible binding to carbohydrates. Undoubtedly, the best characterized are those extracted from plants of the Leguminosae family. Inside this group of proteins, those from the Diocleinae subtribe have attracted attention, in particular Concanavalin A (ConA), the best-studied lectin of the group. Diocleinae lectins, also called ConA-like lectins, present a high similarity of sequence and three-dimensional structure and are known to present inflammatory, vasoactive, antibiotic, immunomodulatory and antitumor activities, among others. This high similarity of lectins inside the ConA-like group makes it possible to use them to study structure/biological activity relationships by the variability of both carbohydrate specificity and biological activities results. It is in this context the following review aims to summarize the most recent data on the biochemical and structural properties, as well as biological activities, of ConA-like lectins and the use of these lectins as models to study structure/biological activity relationships.
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What OpenQuestion holds
Registered trials
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.