Michael Hollmann

ORCID: 0000-0001-8000-7787
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About
Contact & Profiles
Research Areas
  • Neuroscience and Neuropharmacology Research
  • Ion channel regulation and function
  • Receptor Mechanisms and Signaling
  • Nicotinic Acetylcholine Receptors Study
  • Photoreceptor and optogenetics research
  • Chemical Synthesis and Analysis
  • Molecular Sensors and Ion Detection
  • Lipid Membrane Structure and Behavior
  • Photochromic and Fluorescence Chemistry
  • Autoimmune Neurological Disorders and Treatments
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Neurogenesis and neuroplasticity mechanisms
  • Law and Political Science
  • Amino Acid Enzymes and Metabolism
  • Neuroscience of respiration and sleep
  • Genetics and Neurodevelopmental Disorders
  • Memory and Neural Mechanisms
  • Marine Biology and Ecology Research
  • Neurobiology and Insect Physiology Research
  • Neural dynamics and brain function
  • RNA regulation and disease
  • Aquatic Invertebrate Ecology and Behavior
  • Neuroscience and Neural Engineering
  • Marine Ecology and Invasive Species
  • Pharmacological Receptor Mechanisms and Effects

Ruhr University Bochum
2014-2023

Zentrum für Pathologie und Zytodiagnostik
2023

Institut für Zeitgeschichte München–Berlin
2020

University of Freiburg
2020

Deutsche Nationalbibliothek
2014-2020

University of Würzburg
2019

Ford Motor Company (United States)
2019

John D. and Catherine T. MacArthur Foundation
2019

Deutsche Forschungsgemeinschaft
2007

Max Planck Society
1986-2005

NMDA ( N -methyl -D-aspartate) receptors and non-NMDA represent the two major classes of ion channel-linked glutamate receptors. Unlike receptor channels, channels have usually been thought to conduct monovalent cations only. Non-NMDA that can be gated by kainic acid (KA) α-amino-3-hydroxy-5-methyl-4-isoxazole propionic (AMPA) are formed subunits GluR1, GluR2, GluR3. These were expressed in various combinations Xenopus oocytes so their permeability divalent could studied. At physiological...

10.1126/science.1709304 article EN Science 1991-05-10

Three closely related genes, GluR1, GluR2, and GluR3, encode receptor subunits for the excitatory neurotransmitter glutamate. The proteins encoded by individual genes form homomeric ion channels in Xenopus oocytes that are sensitive to glutamatergic agonists such as kainate quisqualate but not N -methyl-D-aspartate, indicating binding sites exist on single polypeptides. In addition, kainate-evoked conductances potentiated expressing two or more of cloned subunits. Electrophysiological...

10.1126/science.2168579 article EN Science 1990-08-31

Extracellular ATP exerts pronounced biological actions in virtually every organ or tissue that has been studied. In the central and peripheral nervous system, acts as a fast excitatory transmitter certain synaptic pathways [Evans, R.J., Derkach, V. & Surprenant, A. (1992) Nature (London) 357, 503-505; Edwards, F.A., Gigg, A.J. Colquhoun, D. 359, 144-147]. Here, we report cloning characterization of complementary DNA from rat brain, encoding an additional member (P2X4) emerging multigenic...

10.1073/pnas.93.8.3684 article EN Proceedings of the National Academy of Sciences 1996-04-16

Joro spider toxin (JSTX) is one of the most potent antagonists glutamatergic AMPA/KA (alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate) receptor channels in invertebrates and vertebrates. A differential blocking effect on certain types synapses--e.g., parallel climbing fiber synaptic inputs to rat cerebellar Purkinje neurons--has been shown by using a synthetic analog toxin. By investigating molecular basis JSTX action recombinant receptors GluR1-GluR4 GluR6 expressed Xenopus...

10.1073/pnas.90.14.6528 article EN Proceedings of the National Academy of Sciences 1993-07-15

The cloning of cDNAs that encode functional glutamate receptors makes it possible to produce antibodies can be used as high-affinity probes for the localization and characterization these in mammalian brain. We have made different regions first cloned member this family, GluR1, using bacterially overproduced antigen. On Western blots, antisera detect glycoprotein(s) 105 kDa present crude membranes hippocampus cerebellum. 105-kDa band is associated with postsynaptic densities, observed...

10.1523/jneurosci.11-09-02713.1991 article EN cc-by-nc-sa Journal of Neuroscience 1991-09-01

Autoantibodies of the IgG class against N-methyl-d-aspartate-receptor subunit NR1 (NMDAR1) were first described in anti-NMDAR encephalitis and seen as disease indicators. Recent work on together over 5000 individuals challenged this exclusive view by showing age-dependently up to >20% NMDAR1-autoantibody seroprevalence with comparable immunoglobulin titer distribution across health disease. The key question therefore is understand properties these autoantibodies, also healthy carriers, order...

10.1038/mp.2016.125 article EN cc-by-nc-nd Molecular Psychiatry 2016-08-09

Hydrophobic amino acids, rather than glutamate, activate the Arabidopsis glutamate receptor homolog AtGLR1.4.

10.1126/scisignal.2003762 article EN Science Signaling 2013-06-11

Autoantibodies of the IgG class against N-methyl-D-aspartate-receptor subunit-NR1 (NMDAR1-AB) were considered pathognomonic for anti-NMDAR encephalitis. This view has been challenged by age-dependent seroprevalence (up to >20%) functional NMDAR1-AB all immunoglobulin classes found in >5000 individuals, healthy or affected different diseases. These findings question a merely encephalitogenic role NMDAR1-AB. Here, we show that belong normal autoimmune repertoire dogs, cats, rats, mice,...

10.1038/s41380-017-0011-3 article EN cc-by-nc-sa Molecular Psychiatry 2018-02-09

Abstract N -methyl- D -aspartate receptors (NMDARs) play a central role in synaptic plasticity, learning and memory, are implicated various neuronal disorders. We synthesized diffusible photochromic glutamate analogue, azobenzene-triazole-glutamate ( ATG ), which is specific for NMDARs functions as photoswitchable agonist. inactive its dark-adapted trans -isoform, but can be converted into active cis -isoform using one-photon (near UV) or two-photon (740 nm) excitation. Irradiation with...

10.1038/ncomms9076 article EN cc-by Nature Communications 2015-08-27

All ionotropic glutamate receptor (iGluR) subunits analyzed so far are heavily <i>N</i>-glycosylated at multiple sites on their amino-terminal extracellular domains. Although the exact functional significance of this glycosylation remains to be determined, it has been suggested that <i>N</i>-glycosylation may a precondition for formation ion channels. In particular, argued is required ligand binding sites. We heterologously expressed recombinant receptors (GluRs) all three pharmacological...

10.1124/mol.52.5.861 article EN Molecular Pharmacology 1997-11-01

The family of AMPA receptors is encoded by four genes that are differentially spliced to result in the flip or flop versions subunits GluR1 GluR4. GluR2 further modified at so-called Q/R site posttranscriptional RNA editing. Delivery plasma membrane and synaptic trafficking controlled transmembrane receptor regulatory proteins (TARPs). Additionally, TARPs influence essential electrophysiological properties channels such as desensitization agonist efficacies. Here, we compare all known...

10.1523/jneurosci.4185-06.2007 article EN cc-by-nc-sa Journal of Neuroscience 2007-04-04
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