Cargando…

Molecular docking analysis of P2X7 receptor with the beta toxin from Clostridium perfringens

Clostridium perfringens beta-toxin (CPB) is linked to necrotic enteritis (over proliferation of bacteria) in several species showing cytotoxic effect on primary porcine endothelial and human precursor immune cells. P2X7 receptor on THP-1 cells is known to bind CPB. This is critical to understand the...

Descripción completa

Detalles Bibliográficos
Autores principales:	Solanki, Amit Kumar, Panwar, Deepak, Kaushik, Himani, Garg, Lalit C
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Biomedical Informatics 2020
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7649019/ https://www.ncbi.nlm.nih.gov/pubmed/33214747 http://dx.doi.org/10.6026/97320630016594

Ejemplares similares

Molecular docking analysis of Clostridium perfringens beta toxin model with potential inhibitors from the ZINC database
por: Solanki, Amit Kumar, et al.
Publicado: (2021)

Immunization with recombinant fusion of LTB and linear epitope (40–62) of epsilon toxin elicits protective immune response against the epsilon toxin of Clostridium perfringens type D
por: Kaushik, Himani, et al.
Publicado: (2019)

Recombinant expression of in silico identified Bcell epitope of epsilon toxin of Clostridium perfringens in translational fusion with a carrier protein
por: Kaushik, Himani, et al.
Publicado: (2013)

Recent Insights into Clostridium perfringens Beta-Toxin
por: Nagahama, Masahiro, et al.
Publicado: (2015)

Identification and modeling of a drug target for Clostridium perfringens SM101
por: Chhabra, Gagan, et al.
Publicado: (2010)

Pyroptosis of Macrophages Induced by Clostridium perfringens Beta-1 Toxin
por: Zhang, Siyu, et al.
Publicado: (2023)

Identification of glutamate ABC-Transporter component in Clostridium perfringens as a putative drug target
por: Bhatia, Bharti, et al.
Publicado: (2014)

Regulation of Toxin Production in Clostridium perfringens
por: Ohtani, Kaori, et al.
Publicado: (2016)

The Generation and Characterization of Recombinant Protein and Antibodies of Clostridium perfringens Beta2 Toxin
por: Zeng, Jin, et al.
Publicado: (2016)

The cytotoxicity and molecular mechanisms of the Clostridium perfringens NetB toxin
por: ISLAM, AKM Azharul, et al.
Publicado: (2020)

Clostridium perfringens Iota-Toxin: Structure and Function
por: Sakurai, Jun, et al.
Publicado: (2009)

Perfringolysin O: The Underrated Clostridium perfringens Toxin?
por: Verherstraeten, Stefanie, et al.
Publicado: (2015)

Effect of Clostridium perfringens β-Toxin on Platelets
por: Thiel, Anne, et al.
Publicado: (2017)

The pore structure of Clostridium perfringens epsilon toxin
por: Savva, Christos G., et al.
Publicado: (2019)

Production, immunogenicity, stability, and safety of a vaccine against Clostridium perfringens beta toxins
por: Saadh, Mohamed J., et al.
Publicado: (2020)

Cellular Entry of Clostridium perfringens Iota-Toxin and Clostridium botulinum C2 Toxin
por: Takehara, Masaya, et al.
Publicado: (2017)

Clostridium Perfringens Toxins Involved in Mammalian Veterinary Diseases
por: Uzal, F. A., et al.
Publicado: (2010)

Membrane-Binding Mechanism of Clostridium perfringens Alpha-Toxin
por: Oda, Masataka, et al.
Publicado: (2015)

Targeted Mass Spectrometry Analysis of Clostridium perfringens Toxins
por: Duracova, Miloslava, et al.
Publicado: (2019)

Is Clostridium perfringens epsilon toxin associated with multiple sclerosis?
por: Titball, Richard W, et al.
Publicado: (2023)

Recombinant Alpha, Beta, and Epsilon Toxins of Clostridium perfringens: Production Strategies and Applications as Veterinary Vaccines
por: Ferreira, Marcos Roberto A., et al.
Publicado: (2016)

Clostridium perfringens Beta2 toxin forms highly cation-selective channels in lipid bilayers
por: Benz, Roland, et al.
Publicado: (2021)

Clostridium perfringens Delta Toxin Is Sequence Related to Beta Toxin, NetB, and Staphylococcus Pore-Forming Toxins, but Shows Functional Differences
por: Manich, Maria, et al.
Publicado: (2008)

Structural Insights into Clostridium perfringens Delta Toxin Pore Formation
por: Huyet, Jessica, et al.
Publicado: (2013)

Clostridium perfringens Delta-Toxin Induces Rapid Cell Necrosis
por: Seike, Soshi, et al.
Publicado: (2016)

Diversity of Clostridium perfringens toxin-genotypes from dairy farms
por: Fohler, Svenja, et al.
Publicado: (2016)

Targeting oncogenic Ras by the Clostridium perfringens toxin TpeL
por: Schorch, Björn, et al.
Publicado: (2018)

Mechanisms of Action and Cell Death Associated with Clostridium perfringens Toxins
por: Navarro, Mauricio A., et al.
Publicado: (2018)

Evidence of Clostridium perfringens epsilon toxin associated with multiple sclerosis
por: Wagley, Sariqa, et al.
Publicado: (2018)

Clostridium perfringens Delta-Toxin Damages the Mouse Small Intestine
por: Seike, Soshi, et al.
Publicado: (2019)

Interaction of Clostridium perfringens Iota Toxin and Lipolysis-Stimulated Lipoprotein Receptor (LSR)
por: Nagahama, Masahiro, et al.
Publicado: (2018)

Clostridium perfringens Beta-Toxin Induces Necrostatin-Inhibitable, Calpain-Dependent Necrosis in Primary Porcine Endothelial Cells
por: Autheman, Delphine, et al.
Publicado: (2013)

Immunogenicity of a Trivalent Recombinant Vaccine Against Clostridium perfringens Alpha, Beta, and Epsilon Toxins in Farm Ruminants
por: Moreira, Gustavo Marçal Schmidt Garcia, et al.
Publicado: (2016)

EGA Protects Mammalian Cells from Clostridium difficile CDT, Clostridium perfringens Iota Toxin and Clostridium botulinum C2 Toxin
por: Schnell, Leonie, et al.
Publicado: (2016)

Evidence for a Prepore Stage in the Action of Clostridium perfringens Epsilon Toxin
por: Robertson, Susan L., et al.
Publicado: (2011)

Clostridium perfringens Epsilon Toxin: A Malevolent Molecule for Animals and Man?
por: Stiles, Bradley G., et al.
Publicado: (2013)

Acid Sphingomyelinase Promotes Cellular Internalization of Clostridium perfringens Iota-Toxin
por: Nagahama, Masahiro, et al.
Publicado: (2018)

Clostridium perfringens α-toxin impairs erythropoiesis by inhibition of erythroid differentiation
por: Takagishi, Teruhisa, et al.
Publicado: (2017)

A role for the Clostridium perfringens β2 toxin in bovine enterotoxaemia?
por: Manteca, C, et al.
Publicado: (2002)

Lung endothelial cells are sensitive to epsilon toxin from Clostridium perfringens
por: Dorca-Arévalo, Jonatan, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_ik5rq5v01vsfc333n9v52m1th4