Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors. - Wikidata - awgldk - TriplyDB

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

http://www.wikidata.org/entity/Q44922742

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Calcium binding by the PKD1 domain regulates interdomain flexibility inVibrio choleraemetalloprotease PrtV Iron and zinc exploitation during bacterial pathogenesis Novel and unique diagnostic biomarkers for Bacillus anthracis infection.Updating perspectives on the initiation of Bacillus anthracis growth and dissemination through its host.Degradation of circulating von Willebrand factor and its regulator ADAMTS13 implicates secreted Bacillus anthracis metalloproteases in anthrax consumptive coagulopathy.Bacillus anthracis protease InhA increases blood-brain barrier permeability and contributes to cerebral hemorrhages.Bacillus anthracis interacts with plasmin(ogen) to evade C3b-dependent innate immunity.Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of invertebrates.Linking temporal changes in bacterial community structures with the detection and phylogenetic analysis of neutral metalloprotease genes in the sediments of a hypereutrophic lake.Necrotrophism is a quorum-sensing-regulated lifestyle in Bacillus thuringiensis.Whole proteome analysis of mouse lymph nodes in cutaneous anthrax Bacillus anthracis sin locus and regulation of secreted proteases.Identification of stringent response-related and potential serological proteins released from Bacillus anthracis overexpressing the RelA/SpoT homolog, Rsh Bant.A Bacillus anthracis strain deleted for six proteases serves as an effective host for production of recombinant proteins Bacillus anthracis Overcomes an Amino Acid Auxotrophy by Cleaving Host Serum Proteins Proteomic analysis of Bacillus thuringiensis at different growth phases by using an automated online two-dimensional liquid chromatography-tandem mass spectrometry strategy Molecular and cellular mechanisms of ectodomain shedding Protease-dependent mechanisms of complement evasion by bacterial pathogens.Structural Basis for Latency and Function of Immune Inhibitor A Metallopeptidase, a Modulator of the Bacillus anthracis Secretome Activated protein C ameliorates Bacillus anthracis lethal toxin-induced lethal pathogenesis in rats.Bacillus thuringiensis metalloproteinase Bmp1 functions as a nematicidal virulence factor.Syndecan-1 is an in vivo suppressor of Gram-positive toxic shock Bacillus anthracis: interactions with the host and establishment of inhalational anthrax.The metalloprotease PrtV from Vibrio cholerae.Spatial localization of bacteria controls coagulation of human blood by 'quorum acting'Anthrax infection inhibits the AKT signaling involved in the E-cadherin-mediated adhesion of lung epithelial cells.Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.Proteomic studies of Bacillus anthracis.New insights into the biological effects of anthrax toxins: linking cellular to organismal responses Molecular functions of syndecan-1 in disease.Shedding of cell membrane-bound proteoglycans.Metallothionein: a Potential Link in the Regulation of Zinc in Nutritional Immunity.InhA1, NprA, and HlyII as candidates for markers to differentiate pathogenic from nonpathogenic Bacillus cereus strains.Syndecan-1 ectodomain shedding is regulated by the small GTPase Rab5 Potential dissemination of Bacillus anthracis utilizing human lung epithelial cells.The InhA metalloproteases of Bacillus cereus contribute concomitantly to virulence.Thermolysin damages animal life through degradation of plasma proteins enhanced by rapid cleavage of serpins and activation of proteases.Communication of γ phage lysin plyG enzymes binding toward SrtA for inhibition of Bacillus anthracis: protein-protein interaction and molecular dynamics study.Staphylococcus aureus proteins SSL6 and SElX interact with neutrophil receptors as identified using secretome phage display.Bacillus anthracis protease InhA regulates BslA-mediated adhesion in human endothelial cells.

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P2860

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

http://www.wikidata.org/entity/Q44922742

description

2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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2006年學術文章

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name

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@en

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@nl

type

label

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@en

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@nl

prefLabel

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@en

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@nl

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P1433

Journal of Biological Chemistry

P1476

Secreted neutral metalloproteases of Bacillus anthracis as candidate pathogenic factors.

@en

P2093

Bryan A Millis

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Charles Bailey

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Dhritiman V Mukherjee

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Emanuel F Petricoin

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Lance A Liotta

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Myung-Chul Chung

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Serguei G Popov

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Taissia G Popova

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Vikas Chandhoke

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Weidong Zhou

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P2860

The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria

Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels

Investigation of bioterrorism-related anthrax, United States, 2001: epidemiologic findings

Effective antiprotease-antibiotic treatment of experimental anthrax

Acceleration of epithelial cell syndecan-1 shedding by anthrax hemolytic virulence factors.

The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor

Quantitative pathology of inhalational anthrax I: quantitative microscopic findings

Repetitive Ser-Gly sequences enhance heparan sulfate assembly in proteoglycans

Pathology and pathogenesis of bioterrorism-related inhalational anthrax

Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNFalpha

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31408-31418

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10.1074/JBC.M605526200

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P433

42

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281

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2006-08-22T00:00:00Z

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16926147

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