Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions

JL Popot - Annual review of biochemistry, 2010 - annualreviews.org
Membrane proteins (MPs) are usually handled in aqueous solutions as protein/detergent
complexes. Detergents, however, tend to be inactivating. This situation has prompted the …

Site-directed fluorescence approaches for dynamic structural biology of membrane peptides and proteins

H Raghuraman, S Chatterjee, A Das - Frontiers in Molecular …, 2019 - frontiersin.org
Membrane proteins mediate a number of cellular functions and are associated with several
diseases and also play a crucial role in pathogenicity. Due to their importance in cellular …

Mutant pores

J Clarke, AJ Heron, L Jayasinghe, EJ Wallace… - US Patent …, 2017 - Google Patents
US9751915B2 - Mutant pores - Google Patents US9751915B2 - Mutant pores - Google
Patents Mutant pores Download PDF Info Publication number US9751915B2 …

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 …

Amphipols and Fluorinated Surfactants: Two Alternatives to Detergents for Studying Membrane Proteins In vitro

C Breyton, B Pucci, JL Popot - Heterologous expression of membrane …, 2010 - Springer
Handling integral membrane proteins in aqueous solutions traditionally relies on the use of
detergents, which are surfactants capable of dispersing the components of biological …

Conformational switching of the diphtheria toxin T domain

MV Rodnin, A Kyrychenko, P Kienker, O Sharma… - Journal of molecular …, 2010 - Elsevier
The diphtheria toxin T domain translocates the catalytic C domain across the endosomal
membrane in response to acidification. To elucidate the role of histidine protonation in …

Kinetic intermediate reveals staggered pH-dependent transitions along the membrane insertion pathway of the diphtheria toxin T-domain

A Kyrychenko, YO Posokhov, MV Rodnin… - Biochemistry, 2009 - ACS Publications
The pH-triggered membrane insertion pathway of the T-domain of diphtheria toxin was
studied using site-selective fluorescence labeling with subsequent application of several …

Mega-stokes pyrene ceramide conjugates for STED imaging of lipid droplets in live cells

O Darragh, A Byrne, GB Berselli, C Long, TE Keyes - Analyst, 2019 - pubs.rsc.org
Lipid droplets are dynamic subcellular organelles that participate in a range of physiological
processes including metabolism, regulation and lipid storage. Their role in disease, such as …

Role of acidic residues in helices TH8–TH9 in membrane interactions of the diphtheria toxin T domain

C Ghatak, MV Rodnin, M Vargas-Uribe, AJ McCluskey… - Toxins, 2015 - mdpi.com
The pH-triggered membrane insertion of the diphtheria toxin translocation domain (T
domain) results in transferring the catalytic domain into the cytosol, which is relevant to …

Conformational switching, refolding and membrane insertion of the diphtheria toxin translocation domain

AS Ladokhin, A Kyrychenko, MV Rodnin… - Methods in …, 2021 - Elsevier
Diphtheria toxin is among many bacterial toxins that utilize the endosomal pathway of
cellular entry, which is ensured by the bridging of the endosomal membrane by the toxin's …