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Molecular Oral Microbiology, ISSN 2041-1006, 10/2017, Volume 32, Issue 5, pp. 375 - 389
Summary Treponema denticola is an oral spirochete strongly associated with severe periodontal disease. A prominent virulence factor, the major outer sheath... 
migration | immune | signaling | host‐pathogen | spirochete | lipid | host-pathogen | POLYMICROBIAL SYNERGY | COMPLEX | SURFACE PROTEIN | SUBGINGIVAL PLAQUE | PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE | PTEN | MICROBIOLOGY | PERIODONTAL-DISEASE | IN-VITRO | DENTISTRY, ORAL SURGERY & MEDICINE | TUMOR-SUPPRESSOR | BINDING-PROPERTIES | Porins - genetics | Neutrophils - drug effects | Treponema denticola - immunology | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Neutrophils - immunology | Neutrophils - physiology | Porins - metabolism | Neuropeptides - metabolism | Recombinant Proteins - pharmacology | Treponema denticola - drug effects | Virulence Factors | Host-Pathogen Interactions | Porins - pharmacology | Bacterial Proteins - pharmacology | Animals | Treponema denticola - metabolism | Chemotaxis, Leukocyte - drug effects | Signal Transduction - drug effects | Porins - chemistry | Bacterial Proteins - metabolism | Mice | Proto-Oncogene Proteins c-akt - metabolism | rac1 GTP-Binding Protein - metabolism | Spirochetes | Periodontics | Incubation | Virulence | Neutrophils | Impairment | Antibodies | Amino acids | Rac1 protein | Stimulation | AKT protein | Activation | Leukocytes (neutrophilic) | Kinases | Chemotaxis | Proteins | Signal transduction | Periodontal disease | Actin | Inhibition | Recombinant
Journal Article
ChemMedChem, ISSN 1860-7179, 07/2014, Volume 9, Issue 7, pp. 1501 - 1511
Cystalysin from Treponema denticola is a pyridoxal 5′‐phosphate dependent lyase that catalyzes the formation of pyruvate, ammonia, and sulfide from cysteine.... 
in silico screening | cystalysin | crystal microspectrophotometry | antibiotic agents | enzyme inhibitors | CHEMISTRY, MEDICINAL | O-ACETYLSERINE SULFHYDRYLASE | SITE-DIRECTED MUTAGENESIS | PK(A) PREDICTION | PYRIDOXAL 5'-PHOSPHATE | CYSTEINE DESULFHYDRASE | SMALL-MOLECULE INHIBITORS | HUMAN ERYTHROCYTES | FORCE-FIELD | PHARMACOLOGY & PHARMACY | WATER-MOLECULES | BINDING-SITES | Small Molecule Libraries - pharmacology | Catalytic Domain | Gram-Positive Bacteria - drug effects | Humans | Enzyme Inhibitors - pharmacology | Small Molecule Libraries - therapeutic use | Treponema denticola - enzymology | Recombinant Proteins - chemistry | Cystathionine gamma-Lyase - metabolism | Recombinant Proteins - genetics | Recombinant Proteins - biosynthesis | Treponema denticola - drug effects | Cystathionine gamma-Lyase - antagonists & inhibitors | Enzyme Inhibitors - therapeutic use | Microbial Sensitivity Tests | Gram-Negative Bacteria - drug effects | Small Molecule Libraries - chemistry | Periodontitis - drug therapy | Anti-Bacterial Agents - chemistry | Enzyme Inhibitors - chemistry | Anti-Bacterial Agents - pharmacology | Molecular Docking Simulation | Cystathionine gamma-Lyase - genetics | Binding Sites | Phosphates | Enzymes | Ammonia | Cysteine | Enzyme inhibitors | Periodontitis | Ionization | Crystals | Virulence (Microbiology) | Structure | Glycine
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2013, Volume 8, Issue 6, p. e66209
The major outer sheath protein (Msp) of Treponema denticola inhibits neutrophil polarization and directed chemotaxis together with actin dynamics in vitro in... 
LOCALIZATION | ACTIVATION | SURFACE PROTEIN | POLARITY | PHOSPHATASE | MULTIDISCIPLINARY SCIENCES | PTEN | PTDINSP | TUMOR-SUPPRESSOR | RAC1 | MOTILITY | Phosphatidylinositol Phosphates - metabolism | Gelsolin - metabolism | CapZ Actin Capping Protein - genetics | Male | Phosphatidylinositol 3-Kinases - metabolism | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Proto-Oncogene Proteins c-akt - genetics | Porins - pharmacology | Treponema denticola - chemistry | Chemotactic Factors - pharmacology | Chemotaxis, Leukocyte - genetics | Chemotaxis, Leukocyte - drug effects | N-Formylmethionine Leucyl-Phenylalanine - pharmacology | Porins - isolation & purification | Cell Polarity - drug effects | Neuropeptides - genetics | Proto-Oncogene Proteins c-akt - metabolism | Neutrophils - metabolism | Neutrophils - pathology | PTEN Phosphohydrolase - agonists | PTEN Phosphohydrolase - genetics | Signal Transduction | Mice, Inbred C57BL | Neutrophils - drug effects | PTEN Phosphohydrolase - metabolism | Neuropeptides - metabolism | CapZ Actin Capping Protein - metabolism | Gene Expression Regulation - drug effects | Phosphatidylinositol 3-Kinases - genetics | Bacterial Proteins - pharmacology | Animals | Gelsolin - genetics | Mice | Primary Cell Culture | Bacterial Proteins - isolation & purification | rac1 GTP-Binding Protein - metabolism | rac1 GTP-Binding Protein - genetics | Physiological aspects | Genetic aspects | Research | Actin | Chemotaxis | Treponema | Polarization | Lipids | Homology | Stimulation | AKT protein | Activation | Feedback loops | Phospholipids | Leucine | Kinases | Phosphatase | Recruitment | Proteins | Signal transduction | Cell activation | Chromosome 10 | Bone marrow | Formyl peptides | Fibroblasts | Inhibition | Gelsolin | Localization | Downstream | Immune system | Tensin | Phosphatidylinositol 3,4,5-triphosphate | Neutrophils | Methionine | Rac1 protein | Leukocytes (neutrophilic) | 1-Phosphatidylinositol 3-kinase | Signaling | Dental research | Laboratory animals | PTEN protein
Journal Article
by Shin, J and Choi, Y
Molecular Oral Microbiology, ISSN 2041-1006, 12/2012, Volume 27, Issue 6, pp. 471 - 482
Journal Article
Journal Article
Journal of Microbiological Methods, ISSN 0167-7012, 10/2010, Volume 83, Issue 1, pp. 66 - 68
Journal Article