Review3 Biotech2017
A review on chimeric xylanases: methods and conditions.
Review in 3 Biotech, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 24 citations in OpenAlex.
- High-quality de novo genome assembly and functional genomic insights into Thermobifida alba DSM43795Biologia futura · 2025Article
- Embedding a feruloyl esterase active site into a thermophilic endoxylanase scaffold for the degradation of feruloylated xylans.Computational and structural biotechnology journal · 2025Article
- Plant cell wall architecture guided design of CBM3-GH11 chimeras with enhanced xylanase activity using a tandem repeat left-handed β-3-prism scaffold.Computational and structural biotechnology journal · 2021Article
- Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multi-functional enzymes are one of the nature's solutions to facilitate metabolic pathways, thus several reactions are regulated and performed simultaneously on one polypeptide chain. Inspired by nature, artificial chimeric proteins have been designed to reduce the production costs and improve the performance. One of the interesting applications of this method is in the plant-based industries such as feed additive, waste treatment, biofuel production, and pulp and paper bleaching. In fact, the heterogeneous texture of plants needs using a combination of different enzymes to achieve an optimal quality in the manufacturing process. Given that xylans are the most abundant non-cellulosic polysaccharides in nature, xylanases are widely utilized in the mentioned industries. In this regard, several studies have been conducted to develop the relevant chimeric enzymes. Despite the successes that have been attained in this field, misfolding, functional or structural interference, and linker breakage have been reported in some cases. The present paper reviews the research to introduce the prerequisites to design an appropriate chimeric xylanase.
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.