ReviewFrontiers in plant science2018
Functional Roles of Starch Binding Domains and Surface Binding Sites in Enzymes Involved in Starch Biosynthesis.
Review in Frontiers in plant science, 2018. 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, 29 citations in OpenAlex.
- Mechanistic insights into substrate-targeting modification effects on interfacial kinetics of raw starch-degrading amylases.Applied and environmental microbiology · 2026Article
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Article
- Dietary Conversion from All-Concentrate to All-Roughage Alters Rumen Bacterial Community Composition and Function in Yak, Cattle-Yak, Tibetan Yellow Cattle and Yellow Cattle.Animals : an open access journal from MDPI · 2024Article
- OsLESV and OsESV1 promote transitory and storage starch biosynthesis to determine rice grain quality and yield.Plant communications · 2024Article
- Structure, function, and evolution of plant ADP-glucose pyrophosphorylase.Plant molecular biology · 2022Review
- BETA-AMYLASE9 is a plastidial nonenzymatic regulator of leaf starch degradation.Plant physiology · 2022Article
- In Silico Analysis of Fungal and Chloride-Dependent α-Amylases within the Family GH13 with Identification of Possible Secondary Surface-Binding Sites.Molecules (Basel, Switzerland) · 2021Article
- Understanding Starch Metabolism in Pea Seeds towards Tailoring Functionality for Value-Added Utilization.International journal of molecular sciences · 2021Review
- Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase).Journal of bioscience and bioengineering · 2021Article
- A specific oligosaccharide-binding site in the alternansucrase catalytic domain mediates alternan elongation.The Journal of biological chemistry · 2020Article
- Comparative Genomic Data Provide New Insight on the Evolution of Pathogenicity inFrontiers in microbiology · 2020Article
- Phosphorylation of ADP-Glucose Pyrophosphorylase During Wheat Seeds Development.Frontiers in plant science · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biosynthesis of starch is catalyzed by a cascade of enzymes. The activity of a large number of these enzymes depends on interaction with polymeric substrates via carbohydrate binding sites, which are situated outside of the catalytic site and its immediate surroundings including the substrate-binding crevice. Such secondary binding sites can belong to distinct starch binding domains (SBDs), classified as carbohydrate binding modules (CBMs), or be surface binding sites (SBSs) exposed on the surface of catalytic domains. Currently in the Carbohydrate-Active enZYmes (CAZy) database SBDs are found in 13 CBM families. Four of these families; CBM20, CBM45, CBM48, and CBM53 are represented in enzymes involved in starch biosynthesis, namely starch synthases, branching enzymes, isoamylases, glucan, water dikinases, and α-glucan phosphatases. A critical role of the SBD in activity has not been demonstrated for any of these enzymes. Among the well-characterized SBDs important for starch biosynthesis are three CBM53s of
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.