Role of pore-forming toxins in bacterial infectious diseases. - Wikidata - awgldk - TriplyDB

Role of pore-forming toxins in bacterial infectious diseases.

Role of pore-forming toxins in bacterial infectious diseases.

http://www.wikidata.org/entity/Q34346202

about

Bacterial Control of Pores Induced by the Type III Secretion System: Mind the Gap Cell Membrane-Coated Nanoparticles As an Emerging Antibacterial Vaccine Platform Signaling beyond Punching Holes: Modulation of Cellular Responses by Vibrio cholerae Cytolysin Insights into phagocytosis-coupled activation of pattern recognition receptors and inflammasomes Rational manipulation of mRNA folding free energy allows rheostat control of pneumolysin production by Streptococcus pneumoniae Revisiting the membrane interaction mechanism of a membrane-damaging β-barrel pore-forming toxin Vibrio cholerae cytolysin.Transmembrane oligomeric form of Vibrio cholerae cytolysin triggers TLR2/TLR6-dependent proinflammatory responses in monocytes and macrophages.The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.Host-derived, pore-forming toxin-like protein and trefoil factor complex protects the host against microbial infection.Bio-inspired detoxification using 3D-printed hydrogel nanocomposites.A Novel Role of Listeria monocytogenes Membrane Vesicles in Inhibition of Autophagy and Cell Death.Prevalence and characteristics of Staphylococcus aureus and methicillin-resistant Staphylococcus aureus nasal colonization among a community-based diabetes population in Foshan, China.A Novel ESAT-6 Secretion System-Secreted Protein EsxX of Community-Associated Staphylococcus aureus Lineage ST398 Contributes to Immune Evasion and Virulence.Pseudomonas aeruginosa Exolysin promotes bacterial growth in lungs, alveolar damage and bacterial dissemination.Antibiotic Resistance and Virulence Phenotypes of Recent Bacterial Strains Isolated from Urinary Tract Infections in Elderly Patients with Prostatic Disease.Channel-forming bacterial toxins in biosensing and macromolecule delivery Mouse, but not human, ApoB-100 lipoprotein cholesterol is a potent innate inhibitor of Streptococcus pneumoniae pneumolysin.Human-specific bacterial pore-forming toxins induce programmed necrosis in erythrocytes Nanotoxoid Vaccines Candidalysin is a fungal peptide toxin critical for mucosal infection Aggregatibacter actinomycetemcomitans-induced hypercitrullination links periodontal infection to autoimmunity in rheumatoid arthritis.Genomic and transcriptomic differences in community acquired methicillin resistant Staphylococcus aureus USA300 and USA400 strains.The cytolytic activity of vaginolysin strictly depends on cholesterol and is potentiated by human CD59.The assembly dynamics of the cytolytic pore toxin ClyA.Binding studies on isolated porcine small intestinal mucosa and in vitro toxicity studies reveal lack of effect of C. perfringens beta-toxin on the porcine intestinal epithelium.PC, a Novel Oral Insecticidal Toxin from Bacillus bombysepticus Involved in Host Lethality via APN and BtR-175.Hydrogel Retaining Toxin-Absorbing Nanosponges for Local Treatment of Methicillin-Resistant Staphylococcus aureus Infection On the translocation of bacteria and their lipopolysaccharides between blood and peripheral locations in chronic, inflammatory diseases: the central roles of LPS and LPS-induced cell death.Pore-Forming Toxins Induce Macrophage Necroptosis during Acute Bacterial Pneumonia.eIF2α Confers Cellular Tolerance to S. aureus α-Toxin.Phylogenetic Distribution of Virulence Genes Among ESBL-producing Uropathogenic Escherichia coli Isolated from Long-term Hospitalized Patients.A Partially Purified Acinetobacter baumannii Phage Preparation Exhibits no Cytotoxicity in 3T3 Mouse Fibroblast Cells.Membrane Repair: Mechanisms and Pathophysiology.The Association of Panton-Valentine leukocidin and mecA Genes in Methicillin-Resistant Staphylococcus aureus Isolates From Patients Referred to Educational Hospitals in Ahvaz, Iran The Streptococcus pyogenes NAD(+) glycohydrolase modulates epithelial cell PARylation and HMGB1 release Lipid raft-dependent plasma membrane repair interferes with the activation of B lymphocytes Molecular Characterization of Nonhemolytic and Nonpigmented Group B Streptococci Responsible for Human Invasive Infections.The NADase-Negative Variant of the Streptococcus pyogenes Toxin NAD⁺ Glycohydrolase Induces JNK1-Mediated Programmed Cellular Necrosis.Statin-conferred enhanced cellular resistance against bacterial pore-forming toxins in airway epithelial cells Editorial: Bacterial Exotoxins: How Bacteria Fight the Immune System.

P2860

Q26751034-F72E4D95-0565-4A73-B78B-C1603522BD6C Q26784233-54EAD8C9-5843-4FAC-804B-281ED2D0E714 Q26797319-E6E77827-4F35-4866-8F0C-324BB3610DBD Q26865044-801EDACC-A532-4864-9E29-ECB745729A93 Q28544890-A5DE9D8D-8DA2-4596-8BC6-6FC7C1CBB4E8 Q30152909-1F40671E-E189-4C69-8803-26904F2138CC Q30153292-3982E0C7-4815-4E4C-ADCB-0E89278BCA45 Q30379698-6D9B17A1-B634-40A1-AE76-86C60E0652AE Q33607035-D681DC0C-3270-4D12-AB11-9C4973331FCF Q33626659-D692A93B-1289-415E-BBFE-6A60CFCBF4EB Q33627783-05DC03C6-7A9C-47BE-B44C-75C3136794DD Q33633695-11751A32-8319-434B-B513-E4395D261F24 Q33639550-5801C1E9-E36E-4D72-88A9-FC8DCB2BF9BF Q33704962-66BF1F65-528E-4001-A691-FEB6F3E1F218 Q33847272-37169E6F-3E89-496C-8F09-D7600E496BCA Q34101821-D5CA5BD8-DD34-4BAF-9340-14CF3F89B60A Q34134769-0374A483-87DC-4A97-966A-9B7CF42A5011 Q34237796-139A9C50-955C-4A9B-8740-F83E128F2CE1 Q34268613-05E6CDAF-2740-4039-B6F0-F7D3B4201E0E Q34520268-68AC3A37-68B7-40CC-9FF5-37E9FF4E697A Q34547370-D57EC38F-71E3-435B-B968-7F8C963821AB Q34984553-2E8480FE-D5C1-4711-AC00-F9F0F80DD839 Q35003661-65A887C9-556B-40B7-8D46-328E81D4776F Q35139429-C50DD48D-0587-4C49-9CA3-557172406AC9 Q35564052-549A9D70-4797-4105-A401-2A7B58D1B7D0 Q35701708-0777321A-8952-43A4-8530-0D3AC48DEBF5 Q35706529-0B25408B-70A6-4D58-B646-EB85E427F405 Q35765830-1CBC2A24-95D0-4300-A148-E54CB1B70492 Q35867134-0EFA3CEC-3BA9-47A9-BD6E-1435B08A5E9E Q35890679-39C26D92-50A0-4A8E-97E3-2806150EDF1D Q36068040-51CDB711-61DE-4B4B-8037-C83B18C3FBC4 Q36106493-B63449D2-27B0-437F-B283-5E816AA1AB04 Q36146335-49886573-470C-4DC1-A241-32B8879434FB Q36146866-260CF75C-66D4-4734-8A3F-D65DEF41B5CF Q36219154-AEC07078-02D9-4532-9F07-3EF33635378D Q36395119-CFD7EBFB-741D-4350-B562-C7348D4D79E1 Q36434355-C8A529DE-EBCB-45D5-802F-80A50D53D293 Q36548272-251AC2C2-92AB-42DE-AAE7-74E3C6053838 Q36549172-B3CC8B0F-CCFC-4E6A-929D-BAF8F869E39D Q37146118-E6379DCD-6562-4A02-B008-37400AB8CD2A

P2860

Role of pore-forming toxins in bacterial infectious diseases.

http://www.wikidata.org/entity/Q34346202

description

2013 nî lūn-bûn

@nan

2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Role of pore-forming toxins in bacterial infectious diseases.

@ast

Role of pore-forming toxins in bacterial infectious diseases.

@en

Role of pore-forming toxins in bacterial infectious diseases.

@nl

type

label

Role of pore-forming toxins in bacterial infectious diseases.

@ast

Role of pore-forming toxins in bacterial infectious diseases.

@en

Role of pore-forming toxins in bacterial infectious diseases.

@nl

prefLabel

Role of pore-forming toxins in bacterial infectious diseases.

@ast

Role of pore-forming toxins in bacterial infectious diseases.

@en

Role of pore-forming toxins in bacterial infectious diseases.

@nl

P1433

Q34346202-7B9CA9FD-791A-4475-9217-EE34CC232783

P1476

Q34346202-4B0DAAE2-9B81-4FA3-8786-3232113A9D48

P2093

Q34346202-A4DB547E-6F7E-4CA4-8E37-4AB61B50006F

Q34346202-F42C703E-581D-4C0D-8562-A467EDB2BD52

P2860

Q34346202-0040AFEE-7669-4344-89E0-D6E6FE1F835B

Q34346202-01161130-3524-4B2B-9F7E-B3653B55842C

Q34346202-02A445DD-A108-4A44-89C7-A51E2E76A5E0

Q34346202-02F23976-ADF4-4D30-80E8-E7CACD4CE7DF

Q34346202-038F46C2-1690-4429-BC6D-A2B98021DA16

Q34346202-061E91B7-52EA-486F-B4DF-99E34DD8F956

Q34346202-07C1B74E-23DE-4F45-9E8A-59D661FB606C

Q34346202-08B37419-78AA-4F94-8C05-4AD1E7BB7F44

Q34346202-090E86AB-DA9B-449E-B8EC-872B27F0B77A

Q34346202-096B5584-0D3C-4574-BE0B-C296DE052D9B

P304

Q34346202-E89D2770-7781-4E20-915D-8B6CF8879406

P31

Q34346202-9B27946E-0D8F-40AD-AE7C-6763D6BB57CB

P356

Q34346202-5A8EBAFE-2B10-464E-81B4-56EE1D6565CD

P433

Q34346202-4539B0B8-47CA-492D-989B-A57D7311F000

P478

Q34346202-D194B2BD-AEC2-4A88-A00F-8DBB4F6685C7

P50

Q34346202-41A83D12-AAE9-4066-A4F0-0D09666AC8F5

Q34346202-50A5D7CF-EE29-40C2-B915-845EA32AF993

P577

Q34346202-D9E2117C-5921-46EB-8507-45AC6D39A298

P5875

Q34346202-C478F712-E777-4677-8D25-BF78906ED39B

P698

Q34346202-A136EE6E-2BD9-4BB4-B287-17BA3DE4AAD1

P932

Q34346202-85D6A7EA-ADD7-46E9-911A-938489342B74

P356

P1433

Microbiology and Molecular Biology Reviews

P1476

Role of pore-forming toxins in bacterial infectious diseases.

@en

P2093

Ferdinand C O Los

http://www.w3.org/2001/XMLSchema#string

Raffi V Aroian

http://www.w3.org/2001/XMLSchema#string

P2860

The role of innate immune responses in the outcome of interspecies competition for colonization of mucosal surfaces

STUDIES ON THE CHEMICAL NATURE OF THE SUBSTANCE INDUCING TRANSFORMATION OF PNEUMOCOCCAL TYPES: INDUCTION OF TRANSFORMATION BY A DESOXYRIBONUCLEIC ACID FRACTION ISOLATED FROM PNEUMOCOCCUS TYPE III

Streptococcus pneumoniae : Epidemiology, Risk Factors, and Clinical Features

Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins

Cytotoxic effects of streptolysin o and streptolysin s enhance the virulence of poorly encapsulated group a streptococci

Bacillus thuringiensis and its pesticidal crystal proteins

Synergistic effects of alpha-toxin and perfringolysin O in Clostridium perfringens-mediated gas gangrene

Identification, cloning, and expression of the CAMP factor gene (cfa) of group A streptococci

Bacillus thuringiensis crystal proteins that target nematodes

Staphylococcus aureus α-hemolysin mediates virulence in a murine model of severe pneumonia through activation of the NLRP3 inflammasome

P304

173-207

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1128/MMBR.00052-12

http://www.w3.org/2001/XMLSchema#string

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

77

http://www.w3.org/2001/XMLSchema#string

P50

P577

2013-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

236933160

http://www.w3.org/2001/XMLSchema#string

P698

23699254

http://www.w3.org/2001/XMLSchema#string

P932

3668673

http://www.w3.org/2001/XMLSchema#string