Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification and characterization of a surface protein-releasing activity in Streptococcus mutans and other pathogenic streptococci.

Infection and immunity - 1 Oct 1992

Lee S F

Abstract excerpt

Surface proteins of Streptococcus mutans have been reported to be released into the culture filtrate at concentrations that vary with the growth conditions. The reason for this is not clear. The present study attempts to investigate the mechanism of the protein release. The results showed that whole cells and raffinose-stabilized protoplasts of S. mutans NG8, when incubated in buffers, were capable of releasing...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adhesins, Bacterial
Share to Bacterial Proteins
Share to Glucosyltransferases

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen-Ion Concentration

Share to Membrane Proteins

Share to Metals

Share to Mutation

Share to Streptococcus

Source

Open in PubMed Open full text

Identifiers

PMID: 1398915
DOI: 10.1128/iai.60.10.4032-4039.1992
PMCID: PMC257433

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterization of a surface protein-releasing activity in Streptococcus mutans and other pathogenic streptococci.PMID 1398915Read ↗

Requirements for surface expression and function of adhesin P1 from Streptococcus mutans.Semantic proximity Read ↗

Role of the C terminus in antigen P1 surface localization in Streptococcus mutans and two related cocci.Semantic proximity Read ↗

Inactivation of the gene encoding surface protein SspA in Streptococcus gordonii DL1 affects cell interactions with human salivary agglutinin and oral actinomyces.Semantic proximity Read ↗

Evidence that an N-terminal S-layer protein fragment triggers the release of a cell-associated high-molecular-weight amylase in Bacillus stearothermophilus ATCC 12980.Semantic proximity Read ↗

Active detachment of Streptococcus mutans cells adhered to epon-hydroxylapatite surfaces coated with salivary proteins in vitro.Semantic proximity Read ↗

Induction of surface-associated proteins of Streptococcus uberis by cultivation with extracellular matrix components and bovine mammary epithelial cells.Semantic proximity Read ↗

Secretion of Functional Salivary Peptide by Streptococcus gordonii Which Inhibits Fimbria-Mediated Adhesion of Porphyromonas gingivalisSemantic proximity Read ↗

Differentiation of salivary agglutinin-mediated adherence and aggregation of mutans streptococci by use of monoclonal antibodies against the major surface adhesin P1.Semantic proximity Read ↗

Interaction of lysozyme with a surface protein antigen of Streptococcus mutans.Semantic proximity Read ↗

VimA is part of the maturation pathway for the major gingipains of Porphyromonas gingivalis W83.Semantic proximity Read ↗

Cytoplasmic membrane-associated protein (CAP) isolated from Streptococcus pyogenes: as a new bacterial superantigen.Semantic proximity Read ↗

Molecular aspects of immunoglobulin A1 degradation by oral streptococciSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.