ArticleMolecular oral microbiology2010
Identification and characterization of amylase-binding protein C from Streptococcus mitis NS51.
Article in Molecular oral microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
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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.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Amylases: Biofilm Inducer or Biofilm Inhibitor?Frontiers in cellular and infection microbiology · 2021Review
- The Predominant Oral Microbiota Is Acquired Early in an Organized Pattern.Scientific reports · 2019Article
- Comparative genomics and evolution of the amylase-binding proteins of oral streptococci.BMC microbiology · 2017Article
- Salivary Alpha-Amylase Enzyme, Psychological Disorders, and Life Quality in Patients with Recurrent Aphthous Stomatitis.International journal of dentistry · 2017Article
- Draft genome sequences of 18 oral streptococcus strains that encode amylase-binding proteins.Genome announcements · 2015Article
- Article
- Taking the starch out of oral biofilm formation: molecular basis and functional significance of salivary α-amylase binding to oral streptococci.Applied and environmental microbiology · 2013Review
- Response of fatty acid synthesis genes to the binding of human salivary amylase by Streptococcus gordonii.Applied and environmental microbiology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A substantial proportion of the streptococcal species found in dental plaque biofilms are able to interact with the abundant salivary enzyme alpha-amylase. These streptococci produce proteins that specifically bind amylase. An important plaque species, Streptococcus mitis, secretes a 36-kDa amylase-binding protein into the extracellular milieu. Proteins precipitated from S. mitis NS51 cell culture supernatant by the addition of purified salivary amylase were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to a membrane, and a prominent 36-kDa band was cut from the membrane and sequenced to yield the N-terminal amino acid sequence DSQAQYSNGV. Searching the S. mitis genome sequence database revealed a single open reading frame containing this sequence, and the gene was amplified by the S. mitis genomic DNA polymerase chain reaction. The coding region of this open reading frame, designated amylase-binding protein C (AbpC), was cloned into an Escherichia coli expression vector and the recombinant AbpC (rAbpC) was purified from the soluble fraction of the E. coli cell lysate. Purified AbpC was found to interact with immobilized amylase, confirming AbpC as a new streptococcal amylase-binding protein.
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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.