Results 91 to 100 of about 1,369,932 (286)

Translophagy—A potential link between autophagy impairment and translational errors

open access: yesFEBS Letters, EarlyView.
Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk   +11 more
wiley   +1 more source

Video_1_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 Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation

open access: yesFEBS Letters, EarlyView.
Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge   +6 more
wiley   +1 more source

Characterization of Pore-forming Toxin Vaginolysin from Gardnerella vaginalis. [PDF]

open access: yes, 2019
Pore formation is a powerful and widespread mechanism used by many pathogenic bacteria to attack host cells. Vaginolysin (VLY) secreted by Gardnerella vaginalis belongs to a class of bacterial pore-forming proteins, namely cholesterol-dependent ...
Zilnytė, Milda,
core  

Structures of lysenin reveal a shared evolutionary origin for pore-forming proteins and its mode of sphingomyelin recognition

open access: yes, 2012
Pore-forming proteins insert from solution into membranes to create lesions, undergoing a structural rearrangement often accompanied by oligomerization.
De Colibus, L.   +10 more
core   +1 more source

Video_4_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

RNA‐related functions of BRCA2 in transcription, replication, and genome stability

open access: yesFEBS Letters, EarlyView.
Beyond its role in homologous recombination, BRCA2 regulates R‐loop homeostasis, DNA–RNA hybrid resolution, RNA polymerase II dynamics, and transcriptional activation. Disruption of any of these functions can contribute to genome instability, inflammatory signaling, and tumorigenesis. BRCA2 is a central tumor suppressor protein best known for its roles
Lucia Alvaro‐Aranda   +2 more
wiley   +1 more source

Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor

open access: yesNature Communications
Hemolysin β-pore-forming toxins (βPFTs) are key virulence factors of Clostridium perfringens, associated with severe diseases in humans and animals. Yet, the mechanisms by which Clostridium βPFTs recognize and engage specific target cells remain poorly ...
Chang Wang   +9 more
doaj   +1 more source

Phobalysin: Fisheye View of Membrane Perforation, Repair, Chemotaxis and Adhesion

open access: yesToxins, 2019
Phobalysin P (PhlyP, for photobacterial lysin encoded on a plasmid) is a recently described small β-pore forming toxin of Photobacterium damselae subsp. damselae (Pdd).
Gisela von Hoven   +2 more
doaj   +1 more source

Supplementary Material for: Tissue-Specific Patterning of Host Innate Immune Responses by Staphylococcus aureus α-Toxin

open access: yes, 2017
Immunomodulatory cytotoxins are prominent virulence factors produced by Staphylococcus aureus, a leading cause of bacterial sepsis, skin infection, and pneumonia. S. aureus α-toxin is a pore-forming toxin that utilizes a widely expressed receptor, ADAM10,
Becker R.E.N. (4144876)   +4 more
core   +1 more source

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