Results 101 to 110 of about 1,369,932 (286)

Video_7_Molecular and Functional Analysis of Pore-Forming Toxin Monalysin From Entomopathogenic Bacterium Pseudomonas entomophila.MOV

open access: yes, 2020
Pseudomonas entomophila is a highly pathogenic bacterium that infects insects. It is also used as a suitable model pathogen to analyze Drosophila's innate immunity. P.
Emil Salim (8627832)   +10 more
core   +1 more source

The heterodimeric amino acid transporters (HAT) of the SLC7/SLC3 family: A structure−function relationships and relevance to human pathology

open access: yesFEBS Letters, EarlyView.
Heterodimeric amino acid transporters consist of SLC7 and SLC3 family proteins arranged in a conserved structural organization. They regulate nutrient transport across cell membranes, supporting essential cellular functions. These transporters also contribute to xenobiotic/drug uptake and distribution.
Mariafrancesca Scalise   +5 more
wiley   +1 more source

CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin

open access: yeseLife, 2017
Many pathogenic bacteria produce pore-forming toxins to attack and kill human cells. We have determined the 4.5 Å structure of the ~2.2 MDa pore complex of pneumolysin, the main virulence factor of Streptococcus pneumoniae, by cryoEM.
Katharina van Pee   +5 more
doaj   +1 more source

All in the family: the toxic activity of pore-forming colicins

open access: yes
Colicins are unusual bacterial toxins because they are directed against close relatives of the producing strain. They kill their targets in one of three distinct ways; via a ribonuclease or deoxyribonuclease activity or by forming pores in the target ...
van der Goot, F. G.   +2 more
core   +1 more source

Video_9_Molecular and Functional Analysis of Pore-Forming Toxin Monalysin From Entomopathogenic Bacterium Pseudomonas entomophila.MOV

open access: yes, 2020
Pseudomonas entomophila is a highly pathogenic bacterium that infects insects. It is also used as a suitable model pathogen to analyze Drosophila's innate immunity. P.
Emil Salim (8627832)   +10 more
core   +1 more source

Leucine‐rich glioma inactivated 1 (LGI1) is a ganglioside‐binding protein

open access: yesFEBS Letters, EarlyView.
Neuronal hyperexcitability associated with a decrease/absence of the extracellular protein LGI1 has been suggested to be primarily due to the downregulation of Kv1 channel expression. The molecular mechanisms underlying this decrease have not yet been elucidated.
Kévin Debreux   +7 more
wiley   +1 more source

Potentiation Effect Of 5FU by Fragaceatoxin C Pore-Forming Toxin in MCF-7 Cell Line

open access: yesMajallah-i Dānishgāh-i ’Ulūm-i Pizishkī-i Shahīd Ṣadūqī Yazd, 2019
Introduction: Chemotherapy has been restricted due to the high-dose side effects. In the present study, acceleration of the chemotherapeutic drug (5FU) entrance into MCF-7 cells has been explored by using a recombinant form of Fragaceatoxin C (FraC) pore-
Mohammad Hassan Kheirandish   +2 more
doaj  

The Effect of Cholesterol on the Long-Range Network of Interactions Established among Sea Anemone Sticholysin II Residues at the Water-Membrane Interface

open access: yesMarine Drugs, 2015
Actinoporins are α-pore forming proteins with therapeutic potential, produced by sea anemones. Sticholysin II (StnII) from Stichodactyla helianthus is one of its most extensively characterized members.
Sara García-Linares   +5 more
doaj   +1 more source

Replication Data for: Support Vector Machine-based Prediction of Pore-forming Toxins (PFT) using Distributed Representation of Reduced Alphabets

open access: yes
Curated dataset used for developing sequence-based SVM classifier for predicting pore-forming ...
Valadi K. Jayaraman   +2 more
core   +1 more source

Structure and function of bacterial pore-forming toxins [PDF]

open access: yes, 2015
The pore-forming bacterial toxins are crutial virulence factors of pathogenic bacteria. Their essential feature is the capacity to form hydrophilic transmembrane pores in cytoplasmic membrane of target cells.
Suková, Anna
core  

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