ArticleNature chemical biology2013
A single-molecule analysis reveals morphological targets for cellulase synergy.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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
23 citing papers in PubMed, 74 citations in OpenAlex.
- Time-resolved tracking of cellulose biosynthesis and assembly during cell wall regeneration in liveScience advances · 2025Article
- Fluorescent Imaging of Extracellular Fungal Enzymes Bound onto Plant Cell Walls.International journal of molecular sciences · 2022Article
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Review
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Deconstruction and Reassembly of Renewable Polymers and Biocolloids into Next Generation Structured Materials.Chemical reviews · 2021Review
- Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose.ACS catalysis · 2021Article
- Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases.RSC chemical biology · 2020Article
- Elucidation of Changes in Cellulose Ultrastructure and Accessibility in Hardwood Fractionation Processes with Carbohydrate Binding Modules.ACS sustainable chemistry & engineering · 2020Article
- Quantifying cellulose accessibility during enzyme-mediated deconstruction using 2 fluorescence-tagged carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Enzymatic hydrolysis of cellulosic materials using synthetic mixtures of purified cellulases bioengineered at3 Biotech · 2018Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 2016Article
- Design of nanoscale enzyme complexes based on various scaffolding materials for biomass conversion and immobilization.Biotechnology journal · 2016Review
- Binding of cellulose binding modules reveal differences between cellulose substrates.Scientific reports · 2016Article
- Cellular automata modeling depicts degradation of cellulosic material by a cellulase system with single-molecule resolution.Biotechnology for biofuels · 2016Article
- The use of carbohydrate binding modules (CBMs) to monitor changes in fragmentation and cellulose fiber surface morphology during cellulase- and Swollenin-induced deconstruction of lignocellulosic substrates.The Journal of biological chemistry · 2015Article
- Cellulose surface degradation by a lytic polysaccharide monooxygenase and its effect on cellulase hydrolytic efficiency.The Journal of biological chemistry · 2014Article
- Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.The Journal of biological chemistry · 2014Article
- A distinct model of synergism between a processive endocellulase (TfCel9A) and an exocellulase (TfCel48A) from Thermobifida fusca.Applied and environmental microbiology · 2014Article
- Identification, structure, and function of a novel type VI secretion peptidoglycan glycoside hydrolase effector-immunity pair.The Journal of biological chemistry · 2013Article
Corrections and comments
- Commented on by
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanisms of enzyme activity on solid substrates are not well understood. Unlike enzyme catalysis in aqueous solutions, enzyme activity on surfaces is complicated by adsorption steps and structural heterogeneities that make enzyme-substrate interactions difficult to characterize. Cellulase enzymes, which catalyze the depolymerization of cellulose, show binding specificities for different cellulose surface morphologies, but the influence of these specificities on the activity of multienzyme mixtures has remained unclear. We developed a metric to quantify binding-target arrangements determined by photoactivated localization microscopy, and we used that metric to show that combinations of cellulases designed to bind within similar but nonidentical morphologies can have synergistic activity. This phenomenon cannot be explained with the binary crystalline or amorphous classifications commonly used to characterize cellulase-binding targets. Our results reveal a strategy for improving the activity of cellulolytic mixtures and demonstrate a versatile method for investigating protein organization on heterogeneous surfaces.
Indexed as
Identifiers
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.