ArticleGlycoconjugate journal2001
Agrocybe cylindracea lectin is a member of the galectin family.
Article in Glycoconjugate journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed, 26 citations in OpenAlex.
- Review
- Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans.International journal of molecular sciences · 2022Article
- Lectin engineering, a molecular evolutionary approach to expanding the lectin utilities.Molecules (Basel, Switzerland) · 2015Review
- Mushroom lectins: specificity, structure and bioactivity relevant to human disease.International journal of molecular sciences · 2015Review
- LEC-2, a highly variable lectin in the lichenSymbiosis (Philadelphia, Pa.) · 2012Article
- Structural basis for chitotetraose coordination by CGL3, a novel galectin-related protein from Coprinopsis cinerea.Journal of molecular biology · 2008Article
- The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A.Glycoconjugate journal · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complete amino acid sequence of Agrocybe cylindracea lectin was determined from the peptides obtained by chemical cleavages and enzymatic hydrolyses. The sequence shows 19.1% and 36.8% identity with those of human galectin-1 and Coprinus lectin-1, a fungal galectin, respectively. Seven residues, which are commonly found in carbohydrate recognizing domain (CRD) of galectins, were conserved. However, several insertions in the sequence, compared with those of human galectin-1 and Coprinus lectin-1, suggest that beta-strands S2, F3, and S4 and the loop structures between beta-strands F2 & S3 and F5 & S2 are different from those of galectins reported so far.
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Registered trials
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