α-Amylase is a potential growth inhibitor of Porphyromonas gingivalis, a periodontal pathogenic bacterium

scientific article

α-Amylase is a potential growth inhibitor of Porphyromonas gingivalis, a periodontal pathogenic bacterium is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1111/JRE.12079
P698PubMed publication ID23550921

P50authorToshiaki MitsuiQ41412877
P2093author name stringK Hashimoto
K Harada
T Tanaka
K Shibata
M Taniguchi
A Ochiai
Y Ishiyama
P2860cites workDetermination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalisQ22066058
Porphyromonas gingivalis-host interactions: open war or intelligent guerilla tactics?Q24655246
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Q25938983
Measurement of protein using bicinchoninic acidQ26778491
Probability-based protein identification by searching sequence databases using mass spectrometry dataQ27860736
Structure of human salivary alpha-amylase at 1.6 A resolution: implications for its role in the oral cavityQ28276076
Antimicrobial and host-defense peptides as new anti-infective therapeutic strategiesQ29617810
Structural and sequence-based classification of glycoside hydrolasesQ29618507
Utility of mass spectrometry for proteome analysis: part I. Conceptual and experimental approachesQ33393366
Identification and characterization of amylase-binding protein C from Streptococcus mitis NS51.Q33821557
Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recoveryQ34648504
Molecular interaction of Porphyromonas gingivalis with host cells: implication for the microbial pathogenesis of periodontal diseaseQ35068815
Dental plaque as a microbial biofilmQ35778371
Amylase-binding protein B of Streptococcus gordonii is an extracellular dipeptidyl-peptidase.Q36898563
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary alpha-amylase in substrate hydrolysis and bacterial bindingQ37101576
Host defense peptides in the oral cavity and the lung: similarities and differencesQ37276479
Oligosaccharide binding to barley alpha-amylase 1.Q38323448
Structural relationship between the enzymatic and streptococcal binding sites of human salivary alpha-amylaseQ38337700
Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva.Q39509656
Bacteroides gingivalis, Bacteroides intermedius and Actinobacillus actinomycetemcomitans in human periodontal diseasesQ39631665
Porphyromonas gingivalis invades oral epithelial cells in vitroQ41556268
Identification and analysis of the amylase-binding protein B (AbpB) and gene (abpB) from Streptococcus gordoniiQ42680215
Cyclodextrins improve the antimicrobial activity of the chloride salt of Ruthenium(II) chloro-phenanthroline-trithiacyclononaneQ44268373
The rice alpha-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastidsQ46535295
P433issue1
P921main subjectPorphyromonas gingivalisQ3214147
P304page(s)62-68
P577publication date2013-04-01
P1433published inJournal of Periodontal ResearchQ15759338
P1476titleα-Amylase is a potential growth inhibitor of Porphyromonas gingivalis, a periodontal pathogenic bacterium
P478volume49

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cites work (P2860)
Q52656528Antimicrobial activity and mechanism of action of a novel cationic α-helical octadecapeptide derived from α-amylase of rice.
Q51183291Characterization and production of multifunctional cationic peptides derived from rice proteins.
Q33587557Comparative genomics and evolution of the amylase-binding proteins of oral streptococci
Q35877623Comparison of salivary levels of mucin and amylase and their relation with clinical parameters obtained from patients with aggressive and chronic periodontal disease
Q58720978Construction of a high-density genetic map and fine QTL mapping for growth and nutritional traits of Crassostrea gigas
Q52319488Revealing the Amylase Interactome in Whole Saliva Using Proteomic Approaches.

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