ArticleProceedings of the National Academy of Sciences of the United States of America2007
A glycosyltransferase with a length-controlling activity as a mechanism to regulate the size of polysaccharides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 57 citations in OpenAlex.
- LARGE1 processively polymerizes length-controlled matriglycan on prodystroglycan.Nature communications · 2025Article
- A β-1,2-glucan-associated glycoside hydrolase family 1 β-glucosidase from Streptomyces griseus.Protein science : a publication of the Protein Society · 2025Article
- New glycoside hydrolase families of β-1,2-glucanases.Protein science : a publication of the Protein Society · 2025Article
- Degree of polymerization and spatial distributions of acyclic and cyclic oligohexoses in soybean root nodules uncovered by MALDI and nanophotonic laser desorption ionization mass spectrometry.Materials today. Bio · 2025Article
- Enzymes that catalyze cyclization of β-1,2-glucans.Applied microbiology and biotechnology · 2025Review
- Development of a scalable recombinant system for cyclic beta-1,2-glucans production.Microbial cell factories · 2024Article
- Structure-function analysis of the cyclic β-1,2-glucan synthase from Agrobacterium tumefaciens.Nature communications · 2024Article
- Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase.Applied microbiology and biotechnology · 2024Article
- Discovery of solabiose phosphorylase and its application for enzymatic synthesis of solabiose from sucrose and lactose.Scientific reports · 2022Article
- A Novel Three-Step Extraction Strategy for High-Value Products from Red AlgaeFoods (Basel, Switzerland) · 2021Article
- Identification, characterization, and structural analyses of a fungal endo-β-1,2-glucanase reveal a new glycoside hydrolase family.The Journal of biological chemistry · 2019Article
- Comparative genomics and phylogenomic analyses of lysine riboswitch distributions in bacteria.PloS one · 2017Article
- Generation and characterization of β1,2-gluco-oligosaccharide probes from Brucella abortus cyclic β-glucan and their recognition by C-type lectins of the immune system.Glycobiology · 2016Article
- Bacterial Molecular Signals in the Sinorhizobium fredii-Soybean Symbiosis.International journal of molecular sciences · 2016Article
- Interaction network and localization of Brucella abortus membrane proteins involved in the synthesis, transport, and succinylation of cyclic β-1,2-glucans.Journal of bacteriology · 2015Article
- Enzymatic synthesis using glycoside phosphorylases.Carbohydrate research · 2015Review
- 1,2-β-Oligoglucan phosphorylase from Listeria innocua.PloS one · 2014Article
- Brucella β 1,2 cyclic glucan is an activator of human and mouse dendritic cells.PLoS pathogens · 2012Article
- Importance of Lipopolysaccharide and Cyclic β-1,2-Glucans in Brucella-Mammalian Infections.International journal of microbiology · 2010Article
- Characterization of the lipid linkage region and chain length of the cellubiuronic acid capsule of Streptococcus pneumoniae.The Journal of biological chemistry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclic beta-1,2-glucans (CbetaG) are osmolyte homopolysaccharides with a cyclic beta-1,2-backbone of 17-25 glucose residues present in the periplasmic space of several bacteria. Initiation, elongation, and cyclization, the three distinctive reactions required for building the cyclic structure, are catalyzed by the same protein, the CbetaG synthase. The initiation activity catalyzes the transference of the first glucose from UDP-glucose to a yet-unidentified amino acid residue in the same protein. Elongation proceeds by the successive addition of glucose residues from UDP-glucose to the nonreducing end of the protein-linked beta-1,2-oligosaccharide intermediate. Finally, the protein-linked intermediate is cyclized, and the cyclic glucan is released from the protein. These reactions do not explain, however, the mechanism by which the number of glucose residues in the cyclic structure is controlled. We now report that control of the degree of polymerization (DP) is carried out by a beta-1,2-glucan phosphorylase present at the CbetaG synthase C-terminal domain. This last activity catalyzes the phosphorolysis of the beta-1,2-glucosidic bond at the nonreducing end of the linear protein-linked intermediate, releasing glucose 1-phosphate. The DP is thus regulated by this "length-controlling" phosphorylase activity. To our knowledge, this is the first description of a control of the DP of homopolysaccharides.
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.