Cargando…

Inhibition of Pore-Forming Proteins

Perforation of cellular membranes by pore-forming proteins can affect cell physiology, tissue integrity, or immune response. Since many pore-forming proteins are toxins or highly potent virulence factors, they represent an attractive target for the development of molecules that neutralize their acti...

Descripción completa

Detalles Bibliográficos
Autores principales:	Omersa, Neža, Podobnik, Marjetka, Anderluh, Gregor
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2019
Materias:	Review
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6784129/ https://www.ncbi.nlm.nih.gov/pubmed/31546810 http://dx.doi.org/10.3390/toxins11090545

Ejemplares similares

Pore-forming moss protein bryoporin is structurally and mechanistically related to actinoporins from evolutionarily distant cnidarians
por: Šolinc, Gašper, et al.
Publicado: (2022)

Design of Protein Logic Gate System Operating on Lipid Membranes
por: Omersa, Neža, et al.
Publicado: (2020)

More than one way to bind to cholesterol: atypical variants of membrane-binding domain of perfringolysin O selected by ribosome display
por: Šakanović, Aleksandra, et al.
Publicado: (2020)

Engineering a pH responsive pore forming protein
por: Kisovec, Matic, et al.
Publicado: (2017)

Plasticity of Listeriolysin O Pores and its Regulation by pH and Unique Histidine
por: Podobnik, Marjetka, et al.
Publicado: (2015)

Corrigendum: Plasticity of Listeriolysin O Pores and its Regulation by pH and Unique Histidine
por: Podobnik, Marjetka, et al.
Publicado: (2015)

An oomycete NLP cytolysin forms transient small pores in lipid membranes
por: Pirc, Katja, et al.
Publicado: (2022)

Binding of the transcription activator-like effector augments transcriptional regulation by another transcription factor
por: Leben, Katja, et al.
Publicado: (2022)

Molecular basis for functional diversity among microbial Nep1-like proteins
por: Lenarčič, Tea, et al.
Publicado: (2019)

Lipid-Binding Aegerolysin from Biocontrol Fungus Beauveria bassiana
por: Kraševec, Nada, et al.
Publicado: (2021)

Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes
por: Petrišič, Nejc, et al.
Publicado: (2023)

Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly
por: Podobnik, Marjetka, et al.
Publicado: (2016)

Expansion and Neofunctionalization of Actinoporin-like Genes in Mediterranean Mussel (Mytilus galloprovincialis)
por: Koritnik, Neža, et al.
Publicado: (2022)

Crystal structure of RahU, an aegerolysin protein from the human pathogen Pseudomonas aeruginosa, and its interaction with membrane ceramide phosphorylethanolamine
por: Kočar, Eva, et al.
Publicado: (2021)

Cytotoxic Activity of LLO Y406A Is Targeted to the Plasma Membrane of Cancer Urothelial Cells
por: Resnik, Nataša, et al.
Publicado: (2021)

Pore formation by human stefin B in its native and oligomeric states and the consequent amyloid induced toxicity
por: Anderluh, Gregor, et al.
Publicado: (2012)

Structures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin Recognition
por: De Colibus, Luigi, et al.
Publicado: (2012)

Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging
por: Margheritis, Eleonora, et al.
Publicado: (2023)

Challenges and approaches to studying pore-forming proteins
por: Benton, Joshua T., et al.
Publicado: (2021)

(19)F NMR studies provide insights into lipid membrane interactions of listeriolysin O, a pore forming toxin from Listeria monocytogenes
por: Kozorog, Mirijam, et al.
Publicado: (2018)

pH-triggered endosomal escape of pore-forming Listeriolysin O toxin-coated gold nanoparticles
por: Plaza-GA, Ismael, et al.
Publicado: (2019)

Bacterial pore-forming toxins
por: Ulhuq, Fatima R., et al.
Publicado: (2022)

Structural basis for the multitasking nature of the potato virus Y coat protein
por: Kežar, Andreja, et al.
Publicado: (2019)

Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming Toxin Vibrio cholerae Cytolysin
por: Singh, Mahendra, et al.
Publicado: (2022)

Gasdermins: novel mitochondrial pore-forming proteins
por: Rogers, Corey, et al.
Publicado: (2019)

Diarylthiophenes as inhibitors of the pore-forming protein perforin
por: Miller, Christian K., et al.
Publicado: (2016)

Nep1-like proteins as a target for plant pathogen control
por: Pirc, Katja, et al.
Publicado: (2021)

Role of Pore-Forming Toxins in Neonatal Sepsis
por: Sonnen, Andreas F.-P., et al.
Publicado: (2013)

Structural Features of Apicomplexan Pore-Forming Proteins and Their Roles in Parasite Cell Traversal and Egress
por: Guerra, Alfredo J., et al.
Publicado: (2017)

The Pore-Forming Haemolysins of Bacillus Cereus: A Review
por: Ramarao, Nalini, et al.
Publicado: (2013)

Structural Basis of the Pore-Forming Toxin/Membrane Interaction
por: Li, Yajuan, et al.
Publicado: (2021)

Ostreolysin A/Pleurotolysin B and Equinatoxins: Structure, Function and Pathophysiological Effects of These Pore-Forming Proteins
por: Frangež, Robert, et al.
Publicado: (2017)

Characterization and Pharmacological Inhibition of the Pore-Forming Clostridioides difficile CDTb Toxin
por: Ernst, Katharina, et al.
Publicado: (2021)

Ceramide Aminoethylphosphonate as a New Molecular Target for Pore-Forming Aegerolysin-Based Protein Complexes
por: Balbi, Teresa, et al.
Publicado: (2022)

Staphylococcal Bicomponent Pore-Forming Toxins: Targets for Prophylaxis and Immunotherapy
por: Aman, M. Javad, et al.
Publicado: (2014)

Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
por: Etxaniz, Asier, et al.
Publicado: (2018)

Response of Cellular Innate Immunity to Cnidarian Pore-Forming Toxins
por: Yap, Wei Yuen, et al.
Publicado: (2018)

A label-free approach for measuring interactions of proteins with lipid membranes
por: Anderluh, Gregor
Publicado: (2023)

The MACPF/CDC family of pore-forming toxins
por: Rosado, Carlos J, et al.
Publicado: (2008)

Listeriolysin O Affects the Permeability of Caco-2 Monolayer in a Pore-Dependent and Ca(2+)-Independent Manner
por: Cajnko, Miša Mojca, et al.
Publicado: (2015)

Cannot write session to /tmp/vufind_sessions/sess_4bt2nsd201e6fj75amnle3horq