Structure and assembly of the pseudopilin PulG (2004)
Köhler, Rolf, Schäfer, Karsten, Müller, Shirley, Vignon, Guillaume, Diederichs, Kay, Philippsen, Ansgar, ...
The pseudopilin PulG is one of several essential components of the type II pullulanase secretion machinery (the Pul secreton) of the Gram-negative bacterium Klebsiella oxytoca. The sequence of the...
Philippsen, Ansgar, Im, Wonpil, Engel, Andreas, Schirmer, Tilman, Roux, Benoit, Müller, Daniel J.
The atomic force microscope (AFM) was used to image native OmpF porin and to detect the electrostatic potential generated by the protein. To this end the OmpF porin trimers from Escherichia coli was...
Identification and structure of a putative Ca2+-binding domain at the C terminus of AQP1 (2002)
Fotiadis, Dimitrios, Suda, Kitaru, Tittmann, Peter, Jeno, Paul, Philippsen, Ansgar, Müller, Daniel J., ...
um in translocation of AQP1 in cholangiocytes from intracellular vesicles to the plasma membrane and in triggering its fusion is discussed. Functional studies are now required to identify the...
Sugar Transport through Maltoporin of Escherichia coli: Role of the Greasy Slide
Van Gelder, Patrick, Dumas, Fabrice, Bartoldus, Ingrid, Saint, Nathalie, Prilipov, Alexei, Winterhalter, Mathias, ...
The lining of the maltodextrin-specific maltoporin (LamB) channel exhibits a string of aromatic residues, the greasy slide, part of which has been shown previously by crystallography to be involved...
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, ...
GlpF, the glycerol facilitator protein of Escherichia coli, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine-tagged protein was overexpressed,...
Philippsen, Ansgar, Im, Wonpil, Engel, Andreas, Schirmer, Tilman, Roux, Benoit, Müller, Daniel J
The atomic force microscope (AFM) was used to image native OmpF porin and to detect the electrostatic potential generated by the protein. To this end the OmpF porin trimers from Escherichia coli was...
Sugar Transport through Maltoporin of Escherichia coli: Role of the Greasy Slide
Van Gelder, Patrick, Dumas, Fabrice, Bartoldus, Ingrid, Saint, Nathalie, Prilipov, Alexei, Winterhalter, Mathias, ...
The lining of the maltodextrin-specific maltoporin (LamB) channel exhibits a string of aromatic residues, the greasy slide, part of which has been shown previously by crystallography to be involved...
The 3.7 Å projection map of the glycerol facilitator GlpF: a variant of the aquaporin tetramer
Braun, Thomas, Philippsen, Ansgar, Wirtz, Sabine, Borgnia, Mario J., Agre, Peter, Kühlbrandt, Werner, ...
GlpF, the glycerol facilitator protein of Escherichia coli, is an archetypal member of the aquaporin superfamily. To assess its structure, recombinant histidine-tagged protein was overexpressed,...
Philippsen, Ansgar, Im, Wonpil, Engel, Andreas, Schirmer, Tilman, Roux, Benoit, Müller, Daniel J
The atomic force microscope (AFM) was used to image native OmpF porin and to detect the electrostatic potential generated by the protein. To this end the OmpF porin trimers from Escherichia coli was...
Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state
Eifler, Nora, Vetsch, Michael, Gregorini, Marco, Ringler, Philippe, Chami, Mohamed, Philippsen, Ansgar, ...
ClyA is a pore-forming toxin from virulent Escherichia coli and Salmonella enterica strains. Here, we show that the intrinsic hemolytic activity of ClyA is independent of its redox state, and that...