Bacterial Pore-Forming Toxins Promote the Activation of Caspases in Parallel to Necroptosis to Enhance Alarmin Release and Inflammation During Pneumonia
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Bacterial Pore-Forming Toxins Promote the Activation of Caspases in Parallel to Necroptosis to Enhance Alarmin Release and Inflammation During Pneumonia ; volume:8 ; number:1 ; day:11 ; month:4 ; year:2018 ; pages:1-10 ; date:12.2018
Scientific reports ; 8, Heft 1 (11.4.2018), 1-10, 12.2018
- Creator
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Gonzalez-Juarbe, Norberto
- Contributor
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Bradley, Kelley M.
Riegler, Ashleigh N.
Reyes, Luis F.
Brissac, Terry
Park, Sang-Sang
Restrepo, Marcos I.
Orihuela, Carlos J.
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-24210-8
- URN
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urn:nbn:de:101:1-2018061023504259709339
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:39 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Gonzalez-Juarbe, Norberto
- Bradley, Kelley M.
- Riegler, Ashleigh N.
- Reyes, Luis F.
- Brissac, Terry
- Park, Sang-Sang
- Restrepo, Marcos I.
- Orihuela, Carlos J.
- SpringerLink (Online service)
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Cell‐free production of pore forming toxins: Functional analysis of thermostable direct hemolysin from Vibrio parahaemolyticus
Single Particle Tracking to Characterize the Mechanism of Pore Formation by Pore Forming Proteins
Primary and secondary membrane damage by small β-barrel pore forming toxins and their implications for membrane repair
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Endogenous pore-forming protein complex targets acidic glycosphingolipids in lipid rafts to initiate endolysosome regulation
Pore forming toxins : with 1 table
Mechanisms protecting host cells against bacterial pore-forming toxins
The pesticidal Cry6Aa toxin from Bacillus thuringiensis is structurally similar to HlyE-family alpha pore-forming toxins
Mannose receptor‐derived peptides neutralize pore‐forming toxins and reduce inflammation and development of pneumococcal disease
Cell‐free production of pore forming toxins: Functional analysis of thermostable direct hemolysin from Vibrio parahaemolyticus
Single Particle Tracking to Characterize the Mechanism of Pore Formation by Pore Forming Proteins
Primary and secondary membrane damage by small β-barrel pore forming toxins and their implications for membrane repair
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Injectable, Pore‐Forming, Perfusable Double‐Network Hydrogels Resilient to Extreme Biomechanical Stimulations
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