ArticleProceedings of the National Academy of Sciences of the United States of America1999
A nod factor binding lectin with apyrase activity from legume roots.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 176 citations in OpenAlex.
- Apyrase in horticultural crops: insights into growth, stress adaptation and quality regulation.Molecular horticulture · 2025Review
- Nitrogen fixation in maize: breeding opportunities.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Review
- Structure-function and application of plant lectins in disease biology and immunity.Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association · 2019Review
- AProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Protein science : a publication of the Protein Society · 2017Article
- Lipo-chitooligosaccharidic nodulation factors and their perception by plant receptors.Glycoconjugate journal · 2015Review
- Populus euphratica APYRASE2 Enhances Cold Tolerance by Modulating Vesicular Trafficking and Extracellular ATP in Arabidopsis Plants.Plant physiology · 2015Article
- Extracellular ATP acts as a damage-associated molecular pattern (DAMP) signal in plants.Frontiers in plant science · 2014Review
- The nodulation factor hydrolase of Medicago truncatula: characterization of an enzyme specifically cleaving rhizobial nodulation signals.Plant physiology · 2013Article
- Rhizobial and mycorrhizal symbioses in Lotus japonicus require lectin nucleotide phosphohydrolase, which acts upstream of calcium signaling.Plant physiology · 2013Article
- The Arabidopsis apyrase AtAPY1 is localized in the Golgi instead of the extracellular space.BMC plant biology · 2012Article
- Purification and biochemical characterization of a novel ecto-apyrase, MP67, from Mimosa pudica.Plant physiology · 2011Article
- Enzymatic role for soybean ecto-apyrase in nodulation.Plant signaling & behavior · 2011Article
- Enzymatic activity of the soybean ecto-apyrase GS52 is essential for stimulation of nodulation.Plant physiology · 2011Article
- The GDA1_CD39 superfamily: NTPDases with diverse functions.Purinergic signalling · 2011Article
- Extracellular ATP signaling in plants.Trends in cell biology · 2010Review
- Extracellular nucleotides elicit cytosolic free calcium oscillations in Arabidopsis.Plant physiology · 2010Article
- Review
- Immunohistochemical localization of apyrase during initial differentiation and germination of pea seeds.Planta · 2009Article
- Plant lectins: the ties that bind in root symbiosis and plant defense.Molecular genetics and genomics : MGG · 2009Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A lectin isolated from the roots of the legume, Dolichos biflorus, binds to Nod factors produced by rhizobial strains that nodulate this plant and has a deduced amino acid sequence with no significant homology to any lectin reported to date. This lectin also is an enzyme that catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside di- and triphosphates; the enzyme activity is increased in the presence of carbohydrate ligands. This lectin-nucleotide phosphohydrolase (LNP) has a substrate specificity characteristic of the apyrase category of phosphohydrolases, and its sequence contains four motifs characteristic of this category of enzymes. LNP is present on the surface of the root hairs, and treatment of roots with antiserum to LNP inhibits their ability to undergo root hair deformation and to form nodules on exposure to rhizobia. These properties suggest that this protein may play a role in the rhizobium-legume symbiosis and/or in a related carbohydrate recognition event endogenous to the plant.
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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.