TY  - JOUR
A1  - Scheller, Frieder W.
A1  - Wollenberger, Ursula
A1  - Lei, Chenghong
A1  - Jin, Wen
A1  - Ge, Bixia
A1  - Lehmann, Claudia
A1  - Lisdat, Fred
A1  - Fridman, Vadim
T1  - Bioelectrocatalysis by redox enzymes at modified electrodes
Y1  - 2002
UR  - www.elsevier.nl/inca/publications/6/0/1/3/4/7/index.htt
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Bioelectrocatalysis by a selenoenzyme
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Wollenberger, Ursula
A1  - Jin, Wen
A1  - Bernhardt, Rita
A1  - Lehmann, Claudia
A1  - Stöcklein, Walter F. M.
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Funktionalisierung von Elektroden für den direkten heterogenen Elektrotransfer
Y1  - 1998
ER  - 
TY  - JOUR
A1  - Lehmann, Claudia
A1  - Wollenberger, Ursula
A1  - Brigelius-Flohé, Regina
A1  - Scheller, Frieder W.
T1  - Modified gold electrodes for electrochemical studies of the reaction phospholipid hydroperoxide glutathione peroxidas with glutathione and glutathione disulfide
Y1  - 2001
ER  - 
TY  - THES
A1  - Lehmann, Claudia
T1  - Untersuchungen des Selenoenzyms Phospholipidhydroperoxid-Glutathionperoxidase an modifizierten Elektroden
Y1  - 2000
ER  - 
TY  - JOUR
A1  - Puchkov, Dmytro
A1  - Müller, Paul Markus
A1  - Lehmann, Martin
A1  - Matthäus, Claudia
T1  - Analyzing the cellular plasma membrane by fast and efficient correlative STED and platinum replica EM
JF  - Frontiers in cell and developmental biology
N2  - The plasma membrane of mammalian cells links transmembrane receptors, various structural components, and membrane-binding proteins to subcellular processes, allowing inter- and intracellular communication. Therefore, membrane-binding proteins, together with structural components such as actin filaments, modulate the cell membrane in their flexibility, stiffness, and curvature. Investigating membrane components and curvature in cells remains challenging due to the diffraction limit in light microscopy. Preparation of 5–15-nm-thin plasma membrane sheets and subsequent inspection by metal replica transmission electron microscopy (TEM) reveal detailed information about the cellular membrane topology, including the structure and curvature. However, electron microscopy cannot identify proteins associated with specific plasma membrane domains. Here, we describe a novel adaptation of correlative super-resolution light microscopy and platinum replica TEM (CLEM-PREM), allowing the analysis of plasma membrane sheets with respect to their structural details, curvature, and associated protein composition. We suggest a number of shortcuts and troubleshooting solutions to contemporary PREM protocols. Thus, implementation of super-resolution stimulated emission depletion (STED) microscopy offers significant reduction in sample preparation time and reduced technical challenges for imaging and analysis. Additionally, highly technical challenges associated with replica preparation and transfer on a TEM grid can be overcome by scanning electron microscopy (SEM) imaging. The combination of STED microscopy and platinum replica SEM or TEM provides the highest spatial resolution of plasma membrane proteins and their underlying membrane and is, therefore, a suitable method to study cellular events like endocytosis, membrane trafficking, or membrane tension adaptations.
KW  - plasma membrane
KW  - endocytosis
KW  - CLEM
KW  - STED
KW  - TEM
KW  - SEM
KW  - electron microscopy
Y1  - 2023
U6  - https://doi.org/10.3389/fcell.2023.1305680
SN  - 2296-634X
VL  - 11
PB  - Frontiers Media
CY  - Lausanne
ER  -