scholarly journals KLIKK proteases of Tannerella forsythia: putative virulence factors with a unique domain structure

2015 ◽  
Vol 6 ◽  
Author(s):  
Miroslaw Ksiazek ◽  
Danuta Mizgalska ◽  
Sigrum Eick ◽  
Ida B. Thøgersen ◽  
Jan J. Enghild ◽  
...  
Keyword(s):  
Domain Structure ◽  
Virulence Factors ◽  
Tannerella Forsythia ◽  
Unique Domain

scholarly journals Analysis of oral microbiome from fossil human remains revealed the significant differences in virulence factors of modern and ancient Tannerella forsythia

BMC Genomics ◽  
2020 ◽  
Vol 21 (1) ◽  
Author(s):  
Anna Philips ◽  
Ireneusz Stolarek ◽  
Luiza Handschuh ◽  
Katarzyna Nowis ◽  
Anna Juras ◽  
...  
Keyword(s):  
Virulence Factors ◽  
Human Remains ◽  
Oral Microbiome ◽  
Tannerella Forsythia

scholarly journals A novel NADPH-dependent oxidoreductase with a unique domain structure in the hyperthermophilic Archaeon,Thermococcus litoralis

2008 ◽  
Vol 282 (1) ◽  
pp. 8-14 ◽  
Author(s):  
András Tóth ◽  
Mária Takács ◽  
Géza Groma ◽  
Gábor Rákhely ◽  
Kornél L. Kovács
Keyword(s):  
Domain Structure ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
Unique Domain

Unique domain structure of π-conjugated tolanethioacetate self-assembled monolayers on Au(111)

2007 ◽  
Vol 107 (10-11) ◽  
pp. 1000-1003 ◽  
Author(s):  
Youngdo Jeong ◽  
Seungwook Kwon ◽  
Yongku Kang ◽  
Changjin Lee ◽  
Eisuke Ito ◽  
...  
Keyword(s):  
Domain Structure ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled ◽  
Unique Domain

scholarly journals An in silico Analysis of Protein Targeted by Glycyrrhizin in Common Dental Pathogens

2020 ◽  
pp. 170-178
Author(s):  
S. Balamithra ◽  
Smiline Girija ◽  
J. Vijayashree Priyadharsini
Keyword(s):  
Virulence Factors ◽  
In Silico ◽  
In Silico Analysis ◽  
Subcellular Location ◽  
Functional Class ◽  
Treponema Denticola ◽  
Peptic Ulcers ◽  
Upper Respiratory Tract ◽  
Tannerella Forsythia ◽  
Medicinal Uses

Glycyrrhizin is a phytocompound which is derived from Glycyrrhiza glabra. It is used in treating the upper respiratory tract disease like cough, bronchitis, laryngitis, sore throat, etc. It has various medicinal uses in rheumatism, peptic ulcers, asthma, allergies, and inflammation. Glycyrrhizin has been reported to possess antibacterial, antiviral, antioxidant, anti inflammatory properties. In view of the above facts, the present in silico study was designed to demonstrate the molecular mechanism underlying the antimicrobial activity of glycyrrhizin against common dental pathogens such as Streptococcus mutans, Porphyromonas gingivalis, Treponema denticola, Enterococcus faecalis and Tannerella forsythia. The STITCH tool was used to identify the drug-protein interaction. The functional class of the protein was deduced using VICMPred, followed by the identification of epitopes on the virulence factors using BepiPred. Further, the subcellular location of the virulence factors were also studied using PSORTb software. The computational analysis performed identified several virulence factors viz., short chain dehydrogenase/reductase family oxidoreductase of Treponema denticola and D-mannonate oxidoreductase of Tannerella forsythia which were found to interact with glycyrrhizin. Interestingly, phosphopyruvate hydratase was found to be the protein present in all the five genera was shown to interact with glycyrrhizin. Thus the present study reveals the target proteins on the dental pathogens which were shown to interact with glycyrrhizin. Furthermore, experimental validation of the results are warranted to provide substantial details on the anti-microbial activity of glycyrrhizin against common dental pathogens.

scholarly journals Bacillus subtilis YhcR, a High-Molecular-Weight, Nonspecific Endonuclease with a Unique Domain Structure

2004 ◽  
Vol 186 (16) ◽  
pp. 5376-5383 ◽  
Author(s):  
Irina A. Oussenko ◽  
Roberto Sanchez ◽  
David H. Bechhofer
Keyword(s):  
Molecular Weight ◽  
Bacillus Subtilis ◽  
High Molecular Weight ◽  
Domain Structure ◽  
Micrococcal Nuclease ◽  
Structural Domain ◽  
Protein Extract ◽  
Triple Mutant ◽  
Rnase R ◽  
Unique Domain

ABSTRACT In a continuing effort to identify ribonucleases that may be involved in mRNA decay in Bacillus subtilis, fractionation of a protein extract from a triple-mutant strain that was missing three previously characterized 3′-to-5′ exoribonucleases (polynucleotide phosphorylase [PNPase], RNase R, and YhaM) was undertaken. These experiments revealed the presence of a high-molecular-weight nuclease encoded by the yhcR gene that was active in the presence of Ca2+ and Mn2+. YhcR is a sugar-nonspecific nuclease that cleaves endonucleolytically to yield nucleotide 3′-monophosphate products, similar to the well-characterized micrococcal nuclease of Staphylococcus aureus. YhcR appears to be located principally in the cell wall and is likely to be a substrate for a B. subtilis sortase. Zymogram analysis suggests that YhcR is the major Ca2+-activated nuclease of B. subtilis. In addition to having a unique overall domain structure, YhcR contains a hitherto unknown structural domain that we have named “NYD,” for “new YhcR domain.”

Unique Domain Structure of Two-Dimensional α-Mo2C Superconducting Crystals

Nano Letters ◽  
2016 ◽  
Vol 16 (7) ◽  
pp. 4243-4250 ◽  
Author(s):  
Zhibo Liu ◽  
Chuan Xu ◽  
Ning Kang ◽  
Libin Wang ◽  
Yixiao Jiang ◽  
...  
Keyword(s):  
Domain Structure ◽  
Two Dimensional ◽  
Unique Domain

Domains and domain nucleation in magnetron-sputtered CoCr thin films

1993 ◽  
Vol 51 ◽  
pp. 1046-1047
Author(s):  
B. G. Demczyk
Keyword(s):  
Thin Films ◽  
Domain Structure ◽  
Magnetic Domain ◽  
Domain Size ◽  
Film Plane ◽  
Magnetic Domain Structure ◽  
Perpendicular Magnetization ◽  
Columnar Grains ◽  
Reversal Mechanism ◽  
Lorentz Transmission Electron Microscopy

CoCr thin films have been of interest for a number of years due to their strong perpendicular anisotropy, favoring magnetization normal to the film plane. The microstructure and magnetic properties of CoCr films prepared by both rf and magnetron sputtering have been examined in detail. By comparison, however, relatively few systematic studies of the magnetic domain structure and its relation to the observed film microstructure have been reported. In addition, questions still remain as to the operative magnetization reversal mechanism in different film thickness regimes. In this work, the magnetic domain structure in magnetron sputtered Co-22 at.%Cr thin films of known microstructure were examined by Lorentz transmission electron microscopy. Additionally, domain nucleation studies were undertaken via in-situ heating experiments.It was found that the 50 nm thick films, which are comprised of columnar grains, display a “dot” type domain configuration (Figure 1d), characteristic of a perpendicular magnetization. The domain size was found to be on the order of a few structural columns in diameter.

Ferroelectric Domain Structure of Pb(Zr.52Ti.48)03

1980 ◽  
Vol 38 ◽  
pp. 214-215
Author(s):  
E.K. Goo ◽  
R.K. Mishra
Keyword(s):  
Phase Transformation ◽  
Domain Structure ◽  
Tetragonal Phase ◽  
Ferroelectric Domain ◽  
Cubic Phase ◽  
Ion Milling ◽  
Thin Foils ◽  
Ferroelectric Domain Structure ◽  
Ferroelectric Domains

Ferroelectric domains are twins that are formed when PZT undergoes a phase transformation from a non-ferroelectric cubic phase to a ferroelectric tetragonal phase upon cooling below ∼375°C.,1 The tetragonal phase is spontaneously polarized in the direction of c-axis, making each twin a ferroelectric domain. Thin foils of polycrystalline Pb (Zr.52Ti.48)03 were made by ion milling and observed in the Philips EM301 with a double tilt stage.

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