ArticleThe Plant cell2014
The structure of the catalytic domain of a plant cellulose synthase and its assembly into dimers.
Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 64 citations in OpenAlex.
- Plant-Based Scaffolds in Tissue Engineering: Structure-Function, Processing, and Clinical Outlook-A Review.Annals of biomedical engineering · 2026Review
- Cellulose Synthesis in Cyanobacteria: Shared Pathways and Distinct Features with Bacteria and Plants.Plants (Basel, Switzerland) · 2025Review
- Cellulose synthase TaCESA7 negatively regulates wheat resistance to stripe rust by reducing cell wall lignification.Stress biology · 2025Article
- The knockout of ClaCSLH1 induced dwarfing in watermelon.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- The plant cell wall-dynamic, strong, and adaptable-is a natural shapeshifter.The Plant cell · 2024Review
- Discovery and Characterization of Fluopipamine, a Putative Cellulose Synthase 1 Antagonist withinJournal of agricultural and food chemistry · 2024Article
- Cellulose: A Review of Water Interactions, Applications in Composites, and Water Treatment.Chemical reviews · 2023Review
- Essential amino acids in the Plant-Conserved and Class-Specific Regions of cellulose synthases.Plant physiology · 2023Article
- Molecular studies of cellulose synthase supercomplex from cotton fiber reveal its unique biochemical properties.Science China. Life sciences · 2022Article
- ENB1 encodes a cellulose synthase 5 that directs synthesis of cell wall ingrowths in maize basal endosperm transfer cells.The Plant cell · 2022Article
- Updating Insights into the Catalytic Domain Properties of PlantMolecules (Basel, Switzerland) · 2021Review
- Anther dehiscence is regulated by gibberellic acid in yellow lupine (Lupinus luteus L.).BMC plant biology · 2021Article
- Structure ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Polysaccharide Biosynthesis: Glycosyltransferases and Their Complexes.Frontiers in plant science · 2021Article
- Characterisation of Cellulose Synthase Like F6 (Frontiers in plant science · 2020Article
- Insights into the cellulose degradation mechanism of the thermophilic fungusBiotechnology for biofuels · 2020Article
- Heterologous overexpression, purification and functional analysis of plant cellulose synthase from green bamboo.Plant methods · 2019Article
- Differences in protein structural regions that impact functional specificity in GT2 family β-glucan synthases.PloS one · 2019Article
- Domain swaps of Arabidopsis secondary wall cellulose synthases to elucidate their class specificity.Plant direct · 2018Article
- Cellulose synthase complex organization and cellulose microfibril structure.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2018Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
Cellulose microfibrils are para-crystalline arrays of several dozen linear (1→4)-β-d-glucan chains synthesized at the surface of the cell membrane by large, multimeric complexes of synthase proteins. Recombinant catalytic domains of rice (Oryza sativa) CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. Specificity of binding to UDP and UDP-Glc indicates a properly folded protein, and binding kinetics indicate that each monomer independently synthesizes single glucan chains of cellulose, i.e., two chains per dimer pair. In contrast to structure modeling predictions, solution x-ray scattering studies demonstrate that the monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain. This configuration is in stark contrast to the domain organization obtained in predicted structures of plant CesA. The arrangement of the catalytic domain within the CesA monomer and dimer provides a foundation for constructing structural models of the synthase complex and defining the relationship between the rosette structure and the cellulose microfibrils they synthesize.
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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.