Madden,Dean R., Cheng,Qing, Thiran,Shalita, Rajan,Shanti, Rigo,Frank, Keinanen,Kari, ...
Upon agonist binding, the bilobate ligand-binding domains of the ionotropic glutamate receptors (iGluR) undergo a cleft closure whose magnitude correlates broadly with the efficacy of the agonist....
Madden,Dean R., Cheng,Qing, Thiran,Shalita, Rajan,Shanti, Rigo,Frank, Keinanen,Kari, ...
Upon agonist binding, the bilobate ligand−binding domains of the ionotropic glutamate receptors (iGluR) undergo a cleft closure whose magnitude correlates broadly with the efficacy of the agonist....
Madden, Dean R., Cheng, Qing, Thiran, Shalita, Rajan, Shanti, Rigo, Frank, Keinanen, Kari, ...
Upon agonist binding, the bilobate ligand-binding domains of the ionotropic glutamate receptors (iGluR) undergo a cleft closure whose magnitude correlates broadly with the efficacy of the agonist....
Madden, Dean R., Cheng, Qing, Thiran, Shalita, Rajan, Shanti, Rigo, Frank, Keinanen, Kari, ...
Upon agonist binding, the bilobate ligand−binding domains of the ionotropic glutamate receptors (iGluR) undergo a cleft closure whose magnitude correlates broadly with the efficacy of the agonist....
Reinelt,Stefan, Hofmann,Eckhard, Gerharz,Tanja, Bott,Michael, Madden,Dean R.
The integral membrane sensor kinase CitA of Klebsiella pneumoniae is part of a two-component signal transduction system that regulates the transport and metabolism of citrate in response to its...
Reinelt, Stefan, Hofmann, Eckhard, Gerharz, Tanja, Bott, Michael, Madden, Dean R.
The integral membrane sensor kinase CitA of Klebsiella pneumoniae is part of a two-component signal transduction system that regulates the transport and metabolism of citrate in response to its...
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...
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 structure and function of glutamate receptor ion channels (2002)
As in the case of many ligand-gated ion channels, the biochemical and electrophysiological properties of the ionotropic glutamate receptors have been studied extensively. Nevertheless, we still do...
The inner workings of AMPA receptors (2002)
As with all ligand-gated ion channels, ionotropic glutamate receptors (iGluRs) convert the free energy of agonist-binding into a sequence of conformational changes that allow regulated ion flux...
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...
Madden,Dean R., Thiran,Shalita, Zimmermann,Herbert, Romm,Jonathan, Jayaraman,Vasanthi
The stereochemistry of the interactions between quinoxaline antagonists and the ligand-binding domain of the glutamate receptor 4 (GluR4) have been investigated by probing their vibrational modes...
Madden,Dean R., Thiran,Shalita, Zimmermann,Herbert, Romm,Jonathan, Jayaraman,Vasanthi
The stereochemistry of the interactions between quinoxaline antagonists and the ligand-binding domain of the glutamate receptor 4 (GluR4) have been investigated by probing their vibrational modes...
Madden, Dean R., Thiran, Shalita, Zimmermann, Herbert, Romm, Jonathan, Jayaraman, Vasanthi
The stereochemistry of the interactions between quinoxaline antagonists and the ligand-binding domain of the glutamate receptor 4 (GluR4) have been investigated by probing their vibrational modes...
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...
Madden, Dean R., Thiran, Shalita, Zimmermann, Herbert, Romm, Jonathan, Jayaraman, Vasanthi
The stereochemistry of the interactions between quinoxaline antagonists and the ligand-binding domain of the glutamate receptor 4 (GluR4) have been investigated by probing their vibrational modes...
Madden,Dean R., Abele,Rupert, Andersson,Arnold, Keinänen,Kari
The ionotropic glutamate receptors (GluR) are the primary mediators of excitatory synaptic transmission in the brain. GluR agonist binding has been localized to an extracellular domain whose core is...
Jayaraman,Vasanthi, Thiran,Shalita, Madden,Dean R.
Recently, it has been demonstrated that Fourier transform infrared spectroscopy (FTIR) detects conformational changes in the glutamate receptor ligand-binding domain that are associated with agonist...
Madden, Dean R., Abele, Rupert, Andersson, Arnold, Keinänen, Kari
The ionotropic glutamate receptors (GluR) are the primary mediators of excitatory synaptic transmission in the brain. GluR agonist binding has been localized to an extracellular domain whose core is...
Jayaraman, Vasanthi, Thiran, Shalita, Madden, Dean R.
Recently, it has been demonstrated that Fourier transform infrared spectroscopy (FTIR) detects conformational changes in the glutamate receptor ligand-binding domain that are associated with agonist...
Kuusinen,Arja, Abele,Rupert, Madden,Dean R., Keinänen,Kari
The extracellular part of ionotropic glutamate receptor (iGluR) subunits can be divided into a conserved two-lobed ligand-binding domain (S1S2) and an N-terminal ~400-residue segment of unknown...
Abele,Rupert, Svergun,D., Keinänen,Kari, Koch,H. J., Madden,Dean R.
Solution scattering studies were performed on a ligand-binding domain (S1S2) of a glutamate receptor ion channel (GluR) in order to study GluR-binding and signal-transduction mechanisms. The core of...
Kuusinen, Arja, Abele, Rupert, Madden, Dean R., Keinänen, Kari
The extracellular part of ionotropic glutamate receptor (iGluR) subunits can be divided into a conserved two-lobed ligand-binding domain (S1S2) and an N-terminal ~400-residue segment of unknown...
Abele, Rupert, Svergun, D., Keinänen, Kari, Koch, H. J., Madden, Dean R.
Solution scattering studies were performed on a ligand-binding domain (S1S2) of a glutamate receptor ion channel (GluR) in order to study GluR-binding and signal-transduction mechanisms. The core of...
Abele,Rupert, Lampinen,Milla, Keinänen,Kari, Madden,Dean R.
Redox agents elicit a wide variety of effects on the ligand affinity and channel properties of ionotropic glutamate receptors and have been proposed as potential therapeutic agents for...
Abele, Rupert, Lampinen, Milla, Keinänen, Kari, Madden, Dean R.
Redox agents elicit a wide variety of effects on the ligand affinity and channel properties of ionotropic glutamate receptors and have been proposed as potential therapeutic agents for...
Characterization of the functional role of the N-glycans in the AMPA receptor ligand-binding domain
Pasternack,Amos, Coleman,Suzanne K., Féthière,James, Madden,Dean R., LeCaer,Jean Paul, Rossier,Jean, ...
Crystal structure of the ligand binding domain of CitA
Reinelt,Stephan, Hofmann,Eckhard, Gerharz,Tanja, Bott,Michael, Madden,Dean R.
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...