scholarly journals Structure of the membrane channel porin from Rhodopseudomonas blastica at 2.0 Å resolution

1994 ◽  
Vol 3 (1) ◽  
pp. 58-63 ◽  
Author(s):  
A. Kreusch ◽  
A. Neubüser ◽  
E. Schiltz ◽  
J. Weckesser ◽  
G.E. Schulz
Keyword(s):  
Membrane Channel ◽  
Rhodopseudomonas Blastica

scholarly journals Release mechanisms of major DAMPs

APOPTOSIS ◽  
2021 ◽  
Vol 26 (3-4) ◽  
pp. 152-162
Author(s):  
Atsushi Murao ◽  
Monowar Aziz ◽  
Haichao Wang ◽  
Max Brenner ◽  
Ping Wang
Keyword(s):  
Rna Binding ◽  
High Mobility ◽  
Live Cells ◽  
Membrane Channel ◽  
Membrane Rupture ◽  
Underlying Mechanisms ◽  
Shock Proteins ◽  
Molecular Patterns ◽  
Damage Associated Molecular Patterns ◽  
Secretory Lysosomes

AbstractDamage-associated molecular patterns (DAMPs) are endogenous molecules which foment inflammation and are associated with disorders in sepsis and cancer. Thus, therapeutically targeting DAMPs has potential to provide novel and effective treatments. When establishing anti-DAMP strategies, it is important not only to focus on the DAMPs as inflammatory mediators but also to take into account the underlying mechanisms of their release from cells and tissues. DAMPs can be released passively by membrane rupture due to necrosis/necroptosis, although the mechanisms of release appear to differ between the DAMPs. Other types of cell death, such as apoptosis, pyroptosis, ferroptosis and NETosis, can also contribute to DAMP release. In addition, some DAMPs can be exported actively from live cells by exocytosis of secretory lysosomes or exosomes, ectosomes, and activation of cell membrane channel pores. Here we review the shared and DAMP-specific mechanisms reported in the literature for high mobility group box 1, ATP, extracellular cold-inducible RNA-binding protein, histones, heat shock proteins, extracellular RNAs and cell-free DNA.

scholarly journals Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Uday Tak ◽  
Terje Dokland ◽  
Michael Niederweis
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Pore Formation ◽  
Molecular Switches ◽  
Water Soluble ◽  
Host Cells ◽  
Solvent Exposure ◽  
Membrane Channel ◽  
Toxin Secretion ◽  
Outer Membrane Channel ◽  
Membrane Spanning

AbstractMycobacterium tuberculosis secretes the tuberculosis necrotizing toxin (TNT) to kill host cells. Here, we show that the WXG100 proteins EsxE and EsxF are essential for TNT secretion. EsxE and EsxF form a water-soluble heterodimer (EsxEF) that assembles into oligomers and long filaments, binds to membranes, and forms stable membrane-spanning channels. Electron microscopy of EsxEF reveals mainly pentameric structures with a central pore. Mutations of both WXG motifs and of a GXW motif do not affect dimerization, but abolish pore formation, membrane deformation and TNT secretion. The WXG/GXW mutants are locked in conformations with altered thermostability and solvent exposure, indicating that the WXG/GXW motifs are molecular switches controlling membrane interaction and pore formation. EsxF is accessible on the bacterial cell surface, suggesting that EsxEF form an outer membrane channel for toxin export. Thus, our study reveals a protein secretion mechanism in bacteria that relies on pore formation by small WXG proteins.

scholarly journals Solution NMR Studies of Antiamoebin, a Membrane Channel-Forming Polypeptide

2003 ◽  
Vol 84 (1) ◽  
pp. 185-194 ◽  
Author(s):  
T.P. Galbraith ◽  
R. Harris ◽  
P.C. Driscoll ◽  
B.A. Wallace
Keyword(s):  
Solution Nmr ◽  
Membrane Channel ◽  
Nmr Studies

Real-time monitoring of the oxidative response of a membrane–channel biomimetic system to free radicals

2013 ◽  
Vol 49 (59) ◽  
pp. 6584 ◽  
Author(s):  
Yu Liu ◽  
Yi-Lun Ying ◽  
Hai-Yan Wang ◽  
Chan Cao ◽  
Da-Wei Li ◽  
...  
Keyword(s):  
Free Radicals ◽  
Real Time ◽  
Real Time Monitoring ◽  
Membrane Channel ◽  
Oxidative Response
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