Clostridium difficile toxins A and B: Receptors, pores, and translocation into cells

KE Orrell, Z Zhang, SN Sugiman-Marangos… - Critical reviews in …, 2017 - Taylor & Francis
The most potent toxins secreted by pathogenic bacteria contain enzymatic moieties that
must reach the cytosol of target cells to exert their full toxicity. Toxins such as anthrax …

Targeting acidity in diseased tissues: mechanism and applications of the membrane-inserting peptide, pHLIP

JC Deacon, DM Engelman, FN Barrera - Archives of biochemistry and …, 2015 - Elsevier
Abstract pHLIPs are a family of soluble∼ 36 amino acid peptides, which bind to membrane
surfaces. If the environment is acidic, a pHLIP folds and inserts across the membrane to form …

Role of protonation states in the stability of molecular dynamics simulations of high-resolution membrane protein structures

J Lasham, A Djurabekova, V Zickermann… - The Journal of …, 2024 - ACS Publications
Classical molecular dynamics (MD) simulations provide unmatched spatial and time
resolution of protein structure and function. However, the accuracy of MD simulations often …

Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56

J Lisboa, C Pereira, RD Pinto, IS Rodrigues… - Nature …, 2023 - nature.com
Bacterial AB toxins are secreted key virulence factors that are internalized by target cells
through receptor-mediated endocytosis, translocating their enzymatic domain to the cytosol …

The study of structure and interactions of glucose-based natural deep eutectic solvents by molecular dynamics simulation

SB Pour, JJ Sardroodi, AR Ebrahimzadeh - Journal of Molecular Liquids, 2021 - Elsevier
In the current study, molecular dynamics simulations were conducted to investigate the
structural and dynamical properties of glucose-based Deep Eutectic Solvents (DESs) at …

[HTML][HTML] pH-triggered conformational switching along the membrane insertion pathway of the diphtheria toxin T-domain

AS Ladokhin - Toxins, 2013 - mdpi.com
The translocation (T)-domain plays a key role in the action of diphtheria toxin and is
responsible for transferring the catalytic domain across the endosomal membrane into the …

Histidine protonation and conformational switching in diphtheria toxin translocation domain

MV Rodnin, V Vasques-Montes, A Kyrychenko… - Toxins, 2023 - mdpi.com
Protonation of key histidine residues has been long implicated in the acid-mediated cellular
action of the diphtheria toxin translocation (T-) domain, responsible for the delivery of the …

Fluorescent Probes and Quenchers in Studies of Protein Folding and Protein‐Lipid Interactions

A Kyrychenko, AS Ladokhin - The Chemical Record, 2024 - Wiley Online Library
Fluorescence spectroscopy provides numerous methodological tools for structural and
functional studies of biological macromolecules and their complexes. All fluorescence …

Using fluorescence for studies of biological membranes: a review

A Kyrychenko - Methods and Applications in Fluorescence, 2015 - iopscience.iop.org
Fluorescence techniques have become powerful and widely used tools for studies of
biochemical and biophysical processes occurring in biological membranes. Various …

Hydrogen–deuterium exchange and mass spectrometry reveal the pH-dependent conformational changes of diphtheria toxin T domain

J Li, MV Rodnin, AS Ladokhin, ML Gross - Biochemistry, 2014 - ACS Publications
The translocation (T) domain of diphtheria toxin plays a critical role in moving the catalytic
domain across the endosomal membrane. Translocation/insertion is triggered by a decrease …