ArticleRSC advances2019
Thermal unfolding and refolding of a lytic polysaccharide monooxygenase from
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 31 citations in OpenAlex.
- Machine learning for enzyme catalytic activity: current progress and future horizons.Briefings in bioinformatics · 2026Review
- Seq2Topt: a sequence-based deep learning predictor of enzyme optimal temperature.Briefings in bioinformatics · 2025Article
- Improving the Enzymatic Activity and Stability of a Lytic Polysaccharide Monooxygenase.International journal of molecular sciences · 2023Article
- Protonation State of an Important Histidine from High Resolution Structures of Lytic Polysaccharide Monooxygenases.Biomolecules · 2022Article
- Lytic Polysaccharide Monooxygenase fromInternational journal of molecular sciences · 2021Article
- Colorimetric LPMO assay with direct implication for cellulolytic activity.Biotechnology for biofuels · 2021Article
- Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species.Biotechnology for biofuels · 2021Article
- LPMOInternational journal of molecular sciences · 2020Article
- A thermostable bacterial lytic polysaccharide monooxygenase with high operational stability in a wide temperature range.Biotechnology for biofuels · 2020Article
- Water-soluble chlorophyll-binding proteins from Brassica oleracea allow for stable photobiocatalytic oxidation of cellulose by a lytic polysaccharide monooxygenase.Biotechnology for biofuels · 2020Article
- Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis.Biomolecules · 2020Article
- A simple enzymatic assay for the quantification of C1-specific cellulose oxidation by lytic polysaccharide monooxygenases.Biotechnology letters · 2020Article
- Influence of Lytic Polysaccharide Monooxygenase Active Site Segments on Activity and Affinity.International journal of molecular sciences · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes which promote the degradation of recalcitrant polysaccharides like cellulose or chitin. Here, we have investigated the thermostability of an LPMO from
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.