ArticleGlycoconjugate journal1997
Purification and carbohydrate-binding specificity of Agrocybe cylindracea lectin.
Article in Glycoconjugate journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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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Who cites it
10 citing papers in PubMed, 61 citations in OpenAlex.
- Nutritional, Nutraceutical, and Medicinal Potential ofFood science & nutrition · 2025Review
- Glycosylation of recombinant adeno-associated virus serotype 6.Molecular therapy. Methods & clinical development · 2024Article
- Review
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans.International journal of molecular sciences · 2022Article
- Alteration of matrix metalloproteinase-3 O-glycan structure as a biomarker for disease activity of rheumatoid arthritis.Arthritis research & therapy · 2016Article
- Mushroom lectins: specificity, structure and bioactivity relevant to human disease.International journal of molecular sciences · 2015Review
- Lectins from edible mushrooms.Molecules (Basel, Switzerland) · 2014Review
- A novel lectin with highly potent antiproliferative and HIV-1 reverse transcriptase inhibitory activities from the edible wild mushroom Russula delica.Glycoconjugate journal · 2010Article
- Agrocybe cylindracea lectin is a member of the galectin family.Glycoconjugate journal · 2001Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A lectin was isolated from fruiting bodies of Agrocybe cylindracea by two ion-exchange chromatographies and gel filtration on Toyopearl HW55F. The lectin was homogeneous on polyacrylamide gel electrophoresis and its molecular mass was determined to be 30000 by gel filtration, and 15000 by sodium dodecylsulfate polyacrylamide gel electrophoresis, signifying a dimeric protein. Its carbohydrate-binding specificity was investigated both by sugar-hapten inhibition of hemagglutination and by enzyme-linked immunosorbent assay. The inhibition tests showed the affinity of the lectin to be weakly directed toward sialic acid and lactose, and the enhanced affinity toward trisaccharides containing the NeuAc alpha2,3Gal beta-structure. Importantly, the lectin strongly interacted with glycoconjugates containing NeuAc alpha2,3Gal beta1,3GlcNAc-/GalNAc sequences.
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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.