Willem Tichelaar

The dynamin A ring complex: molecular organisation and nucleotide-dependent conformational changes (2002)

Klockow,Boris, Tichelaar,Willem, Madden,Dean R., Niemann,Hartmut H., Akiba,Toshihiko, Hirose,Keiko, ...

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human...

The dynamin A ring complex: molecular organisation and nucleotide-dependent conformational changes (2002)

Klockow, Boris, Tichelaar, Willem, Madden, Dean R., Niemann, Hartmut H., Akiba, Toshihiko, Hirose, Keiko, ...

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human...

First Images of a Glutamate Receptor Ion Channel: Oligomeric State and Molecular Dimensions of GluRB Homomers (2001)

Safferling,Markus, Tichelaar,Willem, Kümmerle,Günther, Jouppila,Annukka, Kuusinen,Arja, Keinänen,Kari, ...

We have expressed, purified, and characterized glutamate receptor ion channels (GluR) assembled as homomers of the subunit GluRB. For the first time, single-milligram quantities of biochemically...

First Images of a Glutamate Receptor Ion Channel: Oligomeric State and Molecular Dimensions of GluRB Homomers (2001)

Safferling, Markus, Tichelaar, Willem, Kümmerle, Günther, Jouppila, Annukka, Kuusinen, Arja, Keinänen, Kari, ...

We have expressed, purified, and characterized glutamate receptor ion channels (GluR) assembled as homomers of the subunit GluRB. For the first time, single-milligram quantities of biochemically...

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein (1999)

Jekow,Petra, Behlke,Joachim, Tichelaar,Willem, Lurz,Rudi, Regalla,Manuela, Hinrichs,Winfried, ...

Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was...

Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the bilayer (1999)

Ulrich,S. A., Tichelaar,Willem, Förster,G., Zschörnig,O., Weinkauf,S., Meyer,H. W.

Effect of the ionic environment on the molecular structure of bacteriophage SPP1 portal protein (1999)

Jekow, Petra, Behlke, Joachim, Tichelaar, Willem, Lurz, Rudi, Regalla, Manuela, Hinrichs, Winfried, ...

Bacteriophage SPP1 portal protein is a large cyclical homo-oligomer composed of 13 subunits. The solution structure and assembly behavior of this protein with high-point rotational symmetry was...

Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in the bilayer (1999)

Ulrich, S. A., Tichelaar, Willem, Förster, G., Zschörnig, O., Weinkauf, S., Meyer, H. W.

Perforated support foils with pre-defined hole size, shape and arrangement (1998)

Tichelaar,Willem, Ermantraut,E., Wohlfart,K.

Perforated support foils with pre-defined hole size, shape and arrangement (1998)

Tichelaar, Willem, Ermantraut, E., Wohlfart, K.

Scanning transmission electron microscopy of biomacromolecules (1984)

Tichelaar, Willem

Dit proefschrift handelt over structuuronderzoek aan biologische makromolekulen met behulp van transmissie-elektronenmikroskopie, waarbij het gebruik van de scanning transmissie-elektronenmikroskoop...

The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes

Klockow, Boris, Tichelaar, Willem, Madden, Dean R., Niemann, Hartmut H., Akiba, Toshihiko, Hirose, Keiko, ...

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human...

The dynamin A ring complex: molecular organization and nucleotide-dependent conformational changes

Klockow, Boris, Tichelaar, Willem, Madden, Dean R., Niemann, Hartmut H., Akiba, Toshihiko, Hirose, Keiko, ...

Here we show that Dictyostelium discoideum dynamin A is a fast GTPase, binds to negatively charged lipids, and self-assembles into rings and helices in a nucleotide-dependent manner, similar to human...