ReviewCellular and molecular life sciences : CMLS2010
β-Glucosidases.
Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 196 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
196 citing papers in PubMed, 601 citations in OpenAlex.
- Characterization of aFoods (Basel, Switzerland) · 2026Article
- Perlolyrine Formation and Isoflavones Hydrolysis During Miso Fermentation Affected by Tryptophan and Tryptamine.Journal of food science · 2026Article
- Identifying and characterising a plant GH1 β-glucosidase that exhibits hydrolytic activity on N-linked glucopyranoside.FEBS open bio · 2026Article
- Characterization of an alkali- and glucose-tolerant β-glucosidase from Karamay saline-alkali soil and its structural basis for glucose tolerance.BMC biotechnology · 2026Article
- Genome-wide characterization and expression analysis of glycoside hydrolase family 1 in Morus alba.BMC plant biology · 2026Article
- Temperature-Dependent Conformational Dynamics of Substrate Entrance Loops in β-Glucosidase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Multi-omics analysis of soy isoflavone-induced responses in rumen fermentation, endocrine status and milk production in cows with varying milk yields.Journal of animal science and biotechnology · 2026Article
- Intracellular β-glucosidase regulates cellulase expression and development in Aspergillus nidulans.Applied microbiology and biotechnology · 2026Article
- Investigating the functions of glycosyl hydrolase family 1 in foxtail millet through an integrated genome-wide survey, expression profiling, and variation analysis.BMC plant biology · 2026Article
- Structural insights into glycoside hydrolase family 1 β-glucosidase: Selective oligosaccharide hydrolysis, synthesis, and product profiling.The Journal of biological chemistry · 2026Article
- Characterization of Recombinant GH 43 β-Xylosidases and a GH 3 β-Glucosidase fromJournal of microbiology and biotechnology · 2026Article
- Alternative Splicing Analysis Revealed That the Transcription Factor PacC Shapes the Virulence of the DermatophyteInternational journal of molecular sciences · 2026Article
- Transcriptomic insights into the role of CmLec4 in infection and development of Cordyceps militaris.AMB Express · 2026Article
- Integrative analyses of the transcriptome and metabolome of Huzhang (Pinellia pedatisecta Schott) uncover the molecular genetic basis of its medicinal properties.BMC genomics · 2026Article
- Unravelling the molecular mechanisms of vegetative-to-reproductive transition in Cynara cardunculus by RNA-Seq analysis.Plant molecular biology · 2026Article
- Comparative transcriptomics of anthocyanin accumulation in the pericarp of pigmented purple corn.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
- Multiomics profiling of transcriptional and metabolic responses ofFrontiers in microbiology · 2026Article
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- Flavor compounds regulation in rice-flavor Baijiu byFrontiers in microbiology · 2026Article
136 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Glucosidases (3.2.1.21) are found in all domains of living organisms, where they play essential roles in the removal of nonreducing terminal glucosyl residues from saccharides and glycosides. β-Glucosidases function in glycolipid and exogenous glycoside metabolism in animals, defense, cell wall lignification, cell wall β-glucan turnover, phytohormone activation, and release of aromatic compounds in plants, and biomass conversion in microorganisms. These functions lead to many agricultural and industrial applications. β-Glucosidases have been classified into glycoside hydrolase (GH) families GH1, GH3, GH5, GH9, and GH30, based on their amino acid sequences, while other β-glucosidases remain to be classified. The GH1, GH5, and GH30 β-glucosidases fall in GH Clan A, which consists of proteins with (β/α)(8)-barrel structures. In contrast, the active site of GH3 enzymes comprises two domains, while GH9 enzymes have (α/α)(6) barrel structures. The mechanism by which GH1 enzymes recognize and hydrolyze substrates with different specificities remains an area of intense study.
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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.