Publications 2020

  • S. Gonda, J. Giesen, A. Sieberath, F. West, R. Buchholz, O. Klatt, T. Ziebarth, A. Räk, S. Kleinhubbert, C. Riedel, M. Hollmann, M.I.K. Hamad, A. Reiner, and P. Wahle (2020).
    GluN2B but not GluN2A for basal dendritic growth of cortical pyramidal neurons.
    Frontiers in Neuroanatomy 14: 571351.
    doi: 10.3389/fnana.2020.571351
  • A. Bliznyuk, M. Hollmann, and Y. Grossman (2020).
    The mechanism of NMDA receptor hyperexcitation in high pressure helium and hyperbaric oxygen.
    Frontiers in Physiology 11: 1057.
    doi: 10.3389/fphys.2020.01057
  • H. Pan, A.A. Steixner-Kumar, A. Seelbach, N. Deutsch, A. Ronnenberg, D. Tapken, N. von Ahsen, M. Mitjans, H. Worthmann, R. Trippe, C. Klein-Schmidt, N. Schopf, K. Rentzsch, M. Begemann, J. Wienands, W. Stöcker, K. Weissenborn, M. Hollmann, K.-A. Nave, F. Lühder, and H. Ehrenreich (2020).
    Multiple inducers and novel roles of autoantibodies against the obligatory NMDAR subunit NR1: a translational study from chronic life stress to brain injury.
    Molecular Psychiatry
    doi: 10.1038/s41380-020-0672-1

Publications 2019

  • J.A. Schreiber, D. Schepmann, B. Frehland, S. Thum, M. Datunashvili, T. Budde, M. Hollmann, N. Strutz-Seebohm, B. Wünsch, and G. Seebohm (2019).
    A common mechanism allows selective targeting of GluN2B subunit-containing N-methyl-D-aspartate receptors.
    Communications Biology 2: 420.
    doi: 10.1038/s42003-019-0645-6
  • A. Holz, F. Mülsch, M.K. Schwarz, M. Hollmann, M.D. Döbrössy, V.A. Coenen, M. Bartos, C. Normann, K. Biber, D. van Calker, T. Serchov (2019).
    Enhanced mGlu5 signaling in excitatory neurons promotes rapid antidepressant effects via AMPA receptor activation.
    Neuron 104(2): 338-352.
    doi: 10.1016/j.neuron.2019.07.011
  • A. Bliznyuk, M. Hollmann, and Y. Grossman (2019).
    High pressure stress response: Involvement of NMDA receptor subtypes and molecular markers.
    Frontiers in Physiology. Environmental, Aviation and Space Physiology 10: 1234.
    doi: 10.3389/fphys.2019.01234
  • H. Ehrenreich, H. Pan, and M. Hollmann (2019).
    Active immunization, autoimmunity and encephalitis: The missing links.
    Letter to Science Translational Medicine.
  • E.P. Barykin, A.I. Garifulina, E.V. Kruykova, E.N. Spirova, A.A. Anashkina, A.A. Adzhubei, I.V. Shelukhina, I.E. Kasheverov, V.A. Mitkevich, S.A. Kozin, M. Hollmann, V.I. Tsetlin, and A.A. Makarov (2019).
    Isomerization of Asp7 in beta-amyloid enhances inhibition of the α7 nicotinic receptor and promotes neurotoxicity.
    Cells 8(8): 771.
    doi: 10.3390/cells8080771
  • J.B.H. Wilke, H. Ehrenreich, and M. Hollmann (2019).
    Autoantibodies against NMDA receptors – Janus-faced molecules?
    Neuroforum 25(2).
    doi: 10.1515/nf-2018-0025
  • L.J. van Gemert, T. Huelsken, M.L. Rusmore-Villaume, and M. Hollmann (2019).
    Sinum haliotoideum (Linnaeus, 1758): historic and modern records from the Red Sea, with a discussion of its convoluted taxonomic history (Gastropoda, Naticidae).
    Basteria 83(1-3): 3-12.

Publications 2018

  • A. Jack, M.I.K. Hamad, S. Gonda, S. Gralla, S. Pahl, M. Hollmann, and P. Wahle (2018).
    Development of cortical pyramidal cell and interneuronal dendrites: a role for kainate receptor subunits and NETO1.
    Molecular Neurobiology 56(7): 4960-4979.
    doi: 10.1007/s12035-018-1414-0
  • J. Borycz, A. Ziegler, J.A. Borycz, G. Uhlenbrock, D. Tapken, L. Caceres, M. Hollmann, B.T. Hovemann, I.A. Meinertzhagen (2018).
    Location and functions of Inebriated in the Drosophila eye.
    Biology Open 7(7): bio034926.
    doi: 10.1242/bio.034926
  • S. Pachernegg, S. Eilebrecht, E. Eilebrecht, H. Schöneborn, S. Neumann, A.G. Benecke, and M. Hollmann (2018).
    The siRNA-mediated knockdown of GluN3A in 46C-derived neural stem cells affects mRNA expression levels of neural genes, including known iGluR interactors.
    PLoS ONE 13(2): e0192242.
    doi: 10.1371/journal.pone.0192242
  • H. Pan, B. Oliveira, G. Saher, E. Dere, D. Tapken, M. Mitjans, J. Seidel, J, Wesolowski, D. Wakhloo, C. Klein-Schmidt, A. Ronnenberg, K. Schwabe, R. Trippe, K. Mätz-Rensing, S. Berghoff, Y. Al-Krinawe, H. Martens, M. Begemann, W. Stöcker, F.-J. Kaup, R. Mischke, S. Boretius, K.-A. Nave, J.K. Krauss, M. Hollmann, F. Lühder, and H. Ehrenreich (2019).
    Uncoupling the widespread occurrence of anti-NMDAR1 autoantibodies from neuropsychiatric disease in a novel autoimmune model.
    Molecular Psychiatry 24: 1489-1501.
    doi: 10.1038/s41380-017-0011-3

Publications 2017

  • F.W.W. Hartrampf, D.M. Barber, K. Gottschling, P. Leippe, M. Hollmann, and D. Trauner (2017).
    Development of a photoswitchable antagonist of NMDA receptors.
    Tetrahedron 73(33): 4905-4912.
    doi: 10.1016/j.tet.2017.06.056
  • I. Shelukhina, E. Spirova, D. Kudryavtsev, L. Ojomoko, M. Werner, C. Methfessel, M. Hollmann, and V. Tsetlin (2017).
    Calcium imaging with genetically encoded sensor Case12: Facile analysis of α7/α9 nAChR mutants.
    PLoS ONE 12(8): e0181936.
    doi: 10.1371/journal.pone.0181936
  • D. Tapken, T.B. Steffensen, R. Leth, L.B. Kristensen, A. Gerbola, M. Gajhede, F.S. Jørgensen, L. Olsen, and J.S. Kastrup (2017).
    The low binding affinity of D-serine at the ionotropic glutamate receptor GluD2 can be attributed to the hinge region.
    Scientific Reports 7: 46145.
    doi: 10.1038/srep46145
  • D.M. Barber, S.-A. Liu, K. Gottschling, M. Sumser, M. Hollmann, and D. Trauner (2017).
    Optical control of AMPA receptors using a photoswitchable quinoxaline-2,3-dione antagonist.
    Chemical Science 8: 611-615.
    doi: 10.1039/C6SC01621A

Publications 2016

  • E. Castillo-Gómez, B. Oliveira, D. Tapken, S. Bertrand, C. Klein-Schmidt, H. Pan, P. Zafeiriou, J. Steiner, B. Jurek, R. Trippe, H. Prüss, W.-H. Zimmermann, D. Bertrand, H. Ehrenreich, and M. Hollmann (2017).
    All naturally occurring autoantibodies against the NMDA receptor subunit NR1 have pathogenic potential irrespective of epitope and immunoglobulin class.
    Molecular Psychiatry 22: 1776-1784.
    doi: 10.1038/mp.2016.125
    Abstract      Press Release
  • A. Bliznyuk, G. Gradwohl, M. Hollmann, and Y. Grossman (2016).
    The enigma of the dichotomic pressure response of GluN1-4a/b splice variants of NMDA receptor: experimental and statistical analyses.
    Frontiers in Molecular Neuroscience 9: 40.
    doi: 10.3389/fnmol.2016.00040

Publications 2015

  • V. Matschke, C. Theiss, M. Hollmann, E. Schulze-Bahr, F. Lang, G. Seebohm, and N. Strutz-Seebohm (2015).
    NDRG2 phosphorylation provides negative feedback for SGK1-dependent regulation of a kainate receptor in astrocytes.
    Frontiers in Cellular Neuroscience 9: 387.
    doi: 10.3389/fncel.2015.00387
  • L. Laprell, E. Repak, V. Franckevicius, F. Hartrampf, J. Terhag, M. Hollmann, M. Sumser, N. Rebola, D.A. DiGregorio, and D. Trauner (2015).
    Optical control of NMDA receptors with a diffusible photoswitch.
    Nature Communications 6: 8076.
    doi: 10.1038/ncomms9076
  • A. Bliznyuk, B. Aviner, H. Golan, M. Hollmann, and Y. Grossman (2015).
    The N-methyl-D-aspartate receptor's neglected subunit – GluN1 matters under normal and hyperbaric conditions.
    European Journal of Neuroscience 42(8): 2577-2584.
    doi: 10.1111/ejn.130229
  • S. Pachernegg, Y. Münster, E. Muth-Köhne, G. Fuhrmann, and M. Hollmann (2015).
    GluA2 is rapidly edited at the Q/R site during neural differentiation in vitro.
    Frontiers in Cellular Neuroscience 9: 69.
    doi: 10.3389/fncel.2015.00069

Publications 2014

  • G. Seebohm, E. Wrobel, M. Pusch, M. Dicks, J. Terhag, V. Matschke, I. Rothenberg, O.N. Ursu, F. Hertel, L. Pott, F. Lang, E. Schulze-Bahr, M. Hollmann, R. Stoll, and N. Strutz-Seebohm (2014).
    Structural basis of PI(4,5)P2-dependent regulation of GluA1 by phosphatidylinositol-5-phosphate 4-kinase, type II, alpha (PIP5K2A).
    Pflügers Archiv – European Journal of Physiology.
    doi: 10.1007/s00424-013-1424-8
  • S. Pahl, D. Tapken, S.C. Haering, and M. Hollmann (2014).
    Trafficking of kainate receptors.
    Membranes 4(3): 565-595.
    doi: 10.3390/membranes4030565
  • S.C. Haering, D. Tapken, S. Pahl, and M. Hollmann (2014).
    Auxiliary subunits: Shepherding AMPA receptors to the plasma membrane.
    Membranes 4(3): 469-490.
    doi: 10.3390/membranes4030469
  • M.I.K. Hamad, A. Jack, O. Klatt, M. Lorkowski, T. Strasdeit, S. Kott, C. Sager, M. Hollmann, and P. Wahle (2014).
    Type I TARPs promote dendritic growth of early postnatal neocortical pyramidal cells in organotypic cultures.
    Development 141: 1737-1748.
    doi: 10.1242/dev.099697
  • J. Trippe, K. Steinke, A. Orth, P.M. Faustmann, M. Hollmann, and C.G. Haase (2014).
    Autoantibodies to glutamate receptor antigens in multiple sclerosis and Rasmussen's encephalitis.
    Neuroimmunomodulation 21: 189-194.
    doi: 10.1159/0003565197

Publications 2013

  • S. Pachernegg, I. Joshi, E. Muth-Köhne, S. Pahl, Y. Münster, J. Terhag, M. Karus, M. Werner, Z.-L. Ma-Högemeier, C. Körber, T. Grunwald, A. Faissner, S. Wiese, and M. Hollmann (2013).
    Undifferentiated embryonic stem cells express ionotropic glutamate receptor mRNAs.
    Frontiers in Cellular Neuroscience 7: 241.
    doi: 10.3389/fncel.2013.00241
  • D. Tapken, U. Anschütz, L.-H. Liu, T. Huelsken, G. Seebohm, D. Becker, and M. Hollmann (2013).
    A plant homolog of animal glutamate receptors is an ion channel gated by multiple hydrophobic amino acids.
    Science Signaling 6(279): ra47.
    doi: 10.1126/scisignal.2003762
    Abstract      Press Release
      Access the recommendation on F1000Prime

  • A. Orth, D. Tapken, and M. Hollmann (2013).
    The delta subfamily of glutamate receptors: characterization of receptor chimeras and mutants.
    European Journal of Neuroscience 37(10): 1620-1630.
    doi: 10.1111/ejn.12193

Publications 2012

  • T. Huelsken, D. Tapken, T. Dahlmann, H. Wägele, C. Riginos, and M. Hollmann (2012).
    Systematics and phylogenetic species delimitation within Polinices s.l. (Caenogastropoda: Naticidae) based on molecular data and shell morphology.
    Organisms Diversity and Evolution 12(4): 349-375.
    doi: 10.1007/s13127-012-0111-5
  • A. Mor, Y.Y. Kuttner, S. Levy, M. Mor, M. Hollmann, and Y. Grossman (2012).
    Pressure-selective modulation of NMDA receptor subtypes may reflect 3D
    structural differences.
    Frontiers in Cellular Neuroscience 6: 37.
    doi: 10.3389/fncel.2012.00037
  • C. Herold, I. Joshi, O. Chehadi, M. Hollmann, and O. Güntürkün (2012).
    Plasticity in D1-like receptor expression is associated with different components of cognitive processes.
    PLoS One 7(5): e36484.
    doi: 10.1371/journal.pone.0036484
  • S. Pachernegg, N. Strutz-Seebohm, and M. Hollmann (2012).
    GluN3 subunit-containing NMDA receptors: not just one-trick ponies.
    Trends in Neurosciences 35(4): 240-249.
    doi: 10.1016/j.tins.2011.11.010
  • G. Seebohm, S. Neumann, C. Theiss, T. Novkovic, E.V. Hill, J.M. Tavaré, F. Lang, M. Hollmann, D. Manahan-Vaughan, and N. Strutz-Seebohm (2012).
    Identification of a novel signaling pathway and its relevance for GluA1 recycling.
    PLoS One 7(3): e33889.
    doi: 10.1371/journal.pone.0033889

Publications 2011

  • T. Huelsken, H. Wägele, B. Peters, A. Mather, and M. Hollmann (2011).
    Molecular analysis of adults and egg masses reveals two independent lineages within the infaunal gastropod Naticarius onca (Röding, 1798) (Caenogastropoda: Naticidae).
    Molluscan Research 31(3): 141-151.
  • M.I.K. Hamad, Z.-L. Ma-Högemeier, C. Riedel, C. Conrads, T. Veitinger, T. Habijan, J.-N. Schulz, M. Krause, M.J. Wirth, M. Hollmann, and P. Wahle (2011).
    Cell class-specific regulation of neocortical dendrite and spine growth by AMPA receptor splice and editing variants.
    Development 138(19): 4301-4313.
    doi: 10.1242/dev.071076
    Abstract      Press release
  • T. Huelsken, S. Schreiber, and M. Hollmann (2011).
    COI amplification success from mucus-rich marine gastropods (Gastropoda: Naticidae) depends on DNA extraction method and preserving agent.
    Mitteilungen der Deutschen Malakozoologischen Gesellschaft 85: 17-26.

Publications 2010

  • J. Terhag, K. Gottschling, and M. Hollmann (2010).
    The transmembrane domain C of AMPA receptors is critically involved in receptor function and modulation.
    Frontiers in Molecular Neuroscience 3: 117.
    doi: 10.3389/fnmol.2010.00117
  • E. Muth-Köhne, S. Pachernegg, M. Karus, A. Faissner, and M. Hollmann (2010).
    Expression of NMDA receptors and Ca2+-impermeable AMPA receptors requires neuronal differentiation and allows discrimination between two different types of neural stem cells.
    Cellular Physiology and Biochemistry 26(6): 935-946.
    doi: 10.1159/000324002
  • N.A. Čavara, A. Orth, G. Seebohm, G. Hicking, and M. Hollmann (2010).
    Residues at the tip of the pore loop of NR3-containing NMDA receptors determine Ca2+ permeability and Mg2+ block.
    BMC Neuroscience 11: 133.
    doi: 10.1186/1471-2202-11-133
  • S.M. Schmid and M. Hollmann (2010).
    Bridging the synaptic cleft: Lessons from orphan glutamate receptors.
    Science Signaling 3(136): pe28.
    doi: 10.1126/scisignal.3136pe28
  • Z.-L. Ma-Högemeier, C. Körber, M. Werner, D. Racine, E. Muth-Köhne, D. Tapken, and M. Hollmann (2010).
    Oligomerization in the endoplasmic reticulum and intracellular trafficking of kainate receptors are subunit- but not editing-dependent.
    Journal of Neurochemistry 113(6): 1403-1415.
    doi: 10.1111/j.1471-4159.2009.06559.x
  • J. Terhag, N.A. Čavara, and M. Hollmann (2010).
    Cave canalem: How endogenous ion channels may interfere with heterologous expression in Xenopus oocytes.
    Methods 51(1): 66-74 (“Xenopus Oocytes as an Experimental System”).
    doi: 10.1016/j.ymeth.2010.01.034
  • C. Sager, D. Tapken, and M. Hollmann (2010).
    The C-terminal domains of TARPs: Unexpectedly versatile domains.
    Channels 4(3): 155-158.
    doi: 10.4161/chan.4.3.11349
  • E. Muth-Köhne, J. Terhag, S. Pahl, M. Werner, I. Joshi, and M. Hollmann (2010).
    Functional excitatory GABAA receptors precede ionotropic glutamate receptors in radial glia-like neural stem cells.
    Molecular and Cellular Neuroscience 43(2): 209-221.
    doi: 10.1016/j.mcn.2009.11.002

Publications 2009

  • C. Sager, J. Terhag, S. Kott, and M. Hollmann (2009).
    C-terminal domains of transmembrane α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptor regulatory proteins not only facilitate trafficking but are major modulators of AMPA receptor function.
    Journal of Biological Chemistry 284(47): 32413-32424.
    doi: 10.1074/jbc.M109.039891
  • C. Schmidt and M. Hollmann (2009).
    Molecular and functional characterization of Xenopus laevis N-methyl-D-aspartate receptors.
    Molecular and Cellular Neuroscience 42(2): 116-127.
    doi: 10.1016/j.mcn.2009.06.004
  • C. Schmidt, C. Klein, and M. Hollmann (2009).
    Xenopus laevis oocytes endogenously express all subunits of the ionotropic glutamate receptor family.
    Journal of Molecular Biology 390(2): 182-195.
    doi: 10.1016/j.jmb.2009.05.008
  • S.M. Schmid, S. Kott, C. Sager, T. Huelsken, and M. Hollmann (2009).
    The glutamate receptor subunit delta2 is capable of gating its intrinsic ion channel as revealed by ligand binding domain transplantation.
    Proceedings of the National Academy of Sciences (USA) 106(25): 10320-10325.
    doi: 10.1073/pnas.0900329106
    Abstract      Press release
  • N.A. Čavara, A. Orth, and M. Hollmann (2009).
    Effects of NR1 splicing on NR1/NR3B-type excitatory glycine receptors.
    BMC Neuroscience 10: 32.
    Was "Featured article" on BMC Neuroscience journal homepage.
    doi: 10.1186/1471-2202-10-32
  • C. Villmann, J. Oertel, Z.-L. Ma-Högemeier, M. Hollmann, R. Sprengel, K. Becker, H.-G. Breitinger, and C.-M. Becker (2009).
    Functional complementation of Glra1spd-ot, a glycine receptor subunit mutant, by independently expressed C-terminal domains.
    Journal of Neuroscience 29(8): 2440-2452.
    doi: 10.1523/jneurosci.4400-08.2009
  • S. Kott, C. Sager, D. Tapken, M. Werner, and M. Hollmann (2009).
    Comparative analysis of the pharmacology of GluR1 in complex with TARPs γ2, γ3, γ4, and γ8.
    Neuroscience 158(1): 78-88 (Special issue “Protein Trafficking, Targeting, and Interaction at the Glutamate Synapse”).
    doi: 10.1016/j.neuroscience.2007.12.047
  • C. Sager, D. Tapken, S. Kott, and M. Hollmann (2009).
    Functional modulation of AMPA receptors by transmembrane AMPA receptor regulatory proteins.
    Neuroscience 158(1): 45-54 (Special issue “Protein Trafficking, Targeting, and Interaction at the Glutamate Synapse”).
    doi: 10.1016/j.neuroscience.2007.12.046

Publications 2008

  • A. Mor, S. Levy, M. Hollmann, and Y. Grossman (2008).
    Differential effect of high pressure on NMDA receptor currents in Xenopus laevis oocytes.
    Diving and Hyperbaric Medicine 38(4): 134-136.
  • C. Villmann, J. Hoffmann, M. Werner, S. Kott, N. Strutz-Seebohm, T. Nilsson, and M. Hollmann (2008).
    Different structural requirements for funtional ion pore transplantation suggest different gating mechanisms of NMDA and kainate receptors.
    Journal of Neurochemistry 107(2): 453-465.
    doi: 10.1111/j.1471-4159.2008.05623.x
  • D. Tapken and M. Hollmann (2008).
    Arabidopsis thaliana glutamate receptor ion channel function demonstrated by ion pore transplantation.
    Journal of Molecular Biology 383(1): 36-48.
    doi: 10.1016/j.jmb.2008.06.076
  • L. Zhang, J. Schessl, M. Werner, C. Bonnemann, G. Xiong, J. Mojsilovic-Petrovic, W. Zhou, A. Cohen, P. Seeburg, H. Misawa, A. Jayaram, K. Personius, M. Hollmann, R. Sprengel, and R. Kalb (2008).
    Role of GluR1 in activity-dependent motor system development.
    Journal of Neuroscience 28(40): 9953-9968.
    doi: 10.1523/jneurosci.0880-08.2008
  • N.A. Čavara and M. Hollmann (2008).
    Shuffling the deck anew: How NR3 tweaks NMDA receptor function.
    Molecular Neurobiology 38(1): 16-26.
    doi: 10.1007/s12035-008-8029-9
  • S.M. Schmid und M. Hollmann (2008).
    Molekulare Scharniere bei Glutamatrezeptoren: Schalter für den Ionenkanal und therapeutische Targets.
    Deutsche Zeitschrift für Klinische Forschung, 2008(7/8): 57-61.
  • S.M. Schmid and M. Hollmann (2008).
    To gate or not to gate: Are the delta subunits in the glutamate receptor family functional ion channels?
    Molecular Neurobiology 37(2-3): 126-141.
    doi: 10.1007/s12035-008-8025-0
  • T. Huelsken, C. Marek, S. Schreiber, I. Schmidt, and M. Hollmann (2008).
    The Naticidae (Mollusca: Gastropoda) of Giglio Island (Tuscany, Italy): Shell characters, live animals, and a molecular analysis of egg masses.
    Zootaxa 1770: 1-40.
    Free full-text article (open access)
  • C. Schmidt and M. Hollmann (2008).
    Apparent homomeric NR1 currents observed in Xenopus oocytes are caused by an endogenous NR2 subunit.
    Journal of Molecular Biology 376(3): 658-670.
    doi: 10.1016/j.jmb.2007.11.105

publications 2007

  • S.M. Schmid and M. Hollmann (2007).
    What does it take to gate AMPA receptors?
    Channels 1(6): 404-407.
    doi: 10.4161/chan.1.6.5813
  • R.W. Teichert, E.C. Jimenez, V. Twede, M. Watkins, M. Hollmann, G. Bulaj, and B. Olivera (2007).
    Novel conantokins from Conus parius venom are specific antagonists of NMDA receptors.
    Journal of Biological Chemistry 282(51): 36905-36913.
    doi: 10.1074/jbc.M706611200
  • S.M. Schmid, C. Körber, S. Herrmann, M. Werner, and M. Hollmann (2007).
    A domain linking the AMPA receptor agonist binding site to the ion pore controls gating and causes lurcher properties when mutated.
    Journal of Neuroscience 27(45): 12230-12241.
    doi: 10.1523/jneurosci.3175-07.2007
    Abstract      Press release
  • C. Körber, M. Werner, S. Kott, Z.-L. Ma, and M. Hollmann (2007).
    The transmembrane AMPA receptor regulatory protein γ4 is a more effective modulator of AMPA receptor function than stargazin (γ2).
    Journal of Neuroscience 27(31): 8442-8447.
    doi: 10.1523/jneurosci.0424-07.2007
  • C. Körber, M. Werner, J. Hoffmann, C. Sager, M. Tietze, S.M. Schmid, S. Kott, and M. Hollmann (2007).
    Stargazin interaction with α-amino-3-hydroxy-5-methyl-4-isoxazole propionate (AMPA) receptors is critically dependent on the amino acid at the narrow constriction of the ion channel.
    Journal of Biological Chemistry 282(26): 18758-18766.
    doi: 10.1074/jbc.M611182200
  • S. Kott, M. Werner, C. Körber, and M. Hollmann (2007).
    Electrophysiological properties of AMPA receptors are differentially modulated depending on the associated member of the TARP family.
    Journal of Neuroscience 27(14): 3780-3789.
    doi: 10.1523/jneurosci.4185-06.2007
    Abstract      Press release (in German)
  • Z.-L. Ma, M. Werner, C. Körber, I. Joshi, M. Hamad, P. Wahle, and M. Hollmann (2007).
    Quantitative analysis of co-transfection efficiencies in studies of ionotropic glutamate receptor complexes.
    Journal of Neuroscience Research 85(1): 99-115.
    doi: 10.1002/jnr.21096

publications 2006

  • N. Strutz-Seebohm, G. Korniychuck, R. Baltaev, O.N. Ureche, A.F. Mack, Z.-L. Ma, M. Hollmann, R. Schwarz, F. Lang, and G. Seebohm (2006).
    Functional significance of the kainate receptor GluR6(M836I) mutation that is linked to autism.
    Cellular Physiology and Biochemistry 18: 287-294.
    doi: 10.1159/000097675
  • J. Hoffmann, C. Villmann, M. Werner, and M. Hollmann (2006).
    Investigation via ion pore transplantation of the putative relationship between glutamate receptors and K+ channels.
    Molecular and Cellular Neuroscience 33(4): 358-370.
    doi: 10.1016/j.mcn.2006.08.004
  • J. Hoffmann, A. Gorodetskaia, and M. Hollmann (2006).
    Ion pore properties of ionotropic glutamate receptors are modulated by a transplanted potassium channel selectivity filter.
    Molecular and Cellular Neuroscience 33(3): 335-343.
    doi: 10.1016/j.mcn.2006.08.006
  • G.-B. Jeong, M. Werner, V. Gazula, T. Itoh, M. Roberts, S. David, B. Pfister, A. Cohen, R.L. Neve, M. Hollmann, and R. Kalb (2006).
    Bi-directional control of motor neuron dendrite remodeling by the calcium permeability of AMPA receptors.
    Molecular and Cellular Neuroscience 32(3): 299-314.
    doi: 10.1016/j.mcn.2006.04.008
  • T. Huelsken, M. Clemmensen, and M. Hollmann (2006).
    Neverita delessertiana (Récluz in Chenu, 1843): a naticid species (Gastropoda: Caenogastropoda) distinct from Neverita duplicata (Say, 1822) based on molecular data, morphological characters, and geographical distribution.
    Zootaxa 1257: 1-25.
    Free full-text article (open access)
  • D. Tapken and M. Hollmann (2006).
    Homologs of mammalian glutamate receptors in invertebrates and plants.
    In: Biological and biophysical aspects of ligand-gated ion channel receptor superfamilies, H. Arias, ed. Research Signpost, Trivandrum, pp. 321-382.
  • C. Schmidt, M. Werner, and M. Hollmann (2006).
    Revisiting the postulated “unitary glutamate receptor”: Electrophysiological and pharmacological analysis in two heterologous expression systems fails to detect any evidence for its existence.
    Molecular Pharmacology 69(1): 119-129.
    doi: 10.1124/mol.105.016840

publications 2001 to 2005

  • N. Strutz-Seebohm, G. Seebohm, E. Shumilina, A.F. Mack, H.-J. Wagner, A. Lampert, F. Grahammer, G. Henke, L. Just, T. Skutella, M. Hollmann, and F. Lang (2005).
    Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase isoforms in the regulation of GluR6 expression.
    Journal of Physiology 565(Pt 2): 391-401.
    doi: 10.1113/jphysiol.2004.079624
  • N. Strutz-Seebohm, G. Seebohm, A.F. Mack, H.-J. Wagner, L. Just, T. Skutella, U.E. Lang, G. Henke, M. Striegel, M. Hollmann, N. Rouach, R.A. Nicoll, J.A. McCormick, J. Wang, D. Pearce, and F. Lang (2005).
    Regulation of GluR1 abundance in murine hippocampal neurones by serum- and glucocorticoid-inducible kinase 3.
    Journal of Physiology 565(Pt 2): 381-390.
    doi: 10.1113/jphysiol.2004.079582
  • I. Paarmann, D. Frermann, B.U. Keller, C. Villmann, H.G. Breitinger, and M. Hollmann (2005).
    Kinetics and subunit composition of NMDA receptors in respiratory-related neurons.
    Journal of Neurochemistry 93(4): 812-824.
    doi: 10.1111/j.1471-4159.2005.03027.x
  • N. Strutz-Seebohm, M. Werner, D.M. Madsen, G. Seebohm, Y. Zheng, C.S. Walker, A.V. Maricq, and M. Hollmann (2003).
    Functional analysis of Caenorhabditis elegans glutamate receptor subunits by domain transplantation.
    Journal of Biological Chemistry 278(45): 44691-44701.
    doi: 10.1074/jbc.M305497200
  • A. Thalhammer, I. Everts, and M. Hollmann (2002).
    Inhibition by lectins of glutamate receptor desensitization is determined by the lectin's sugar specificity at kainate but not AMPA receptors.
    Molecular and Cellular Neuroscience 21(4): 521-533.
    doi: 10.1006/mcne.2002.1137
  • N. Strutz, C. Villmann, H.-G. Breitinger, M. Werner, R.J. Wenthold, P. Kizelsztein, V.I. Teichberg, and M. Hollmann (2002).
    Kainate binding proteins are rendered functional ion channels upon transplantation of two short pore-flanking domains from a kainate receptor.
    Journal of Biological Chemistry 277(50): 48035-48042.
    doi: 10.1074/jbc.M209647200
  • F.M. Inglis, R. Crockett, S. Korada, W.C. Abraham, M. Hollmann, and R.G. Kalb (2002).
    The AMPA receptor subunit GluR1 regulates dendritic architecture of motor neurons.
    Journal of Neuroscience 22(18): 8042-8051.
  • B. Lacombe, D. Becker, R. Hedrich, R. DeSalle, M. Hollmann, J.M. Kwak, J.I. Schröder, N. Le Novère, H.G. Nam, E.P. Spalding, M. Tester, F.J. Turano, J. Chiu, and G. Coruzzi (2001).
    The identity of plant glutamate receptors.
    Science 292(5521): 1486-1487.
    doi: 10.1126/science.292.5521.1486b
  • N. Strutz, C. Villmann, A. Thalhammer, P. Kizelsztein, M. Eisenstein, V.I. Teichberg, and M. Hollmann (2001).
    Identification of domains and amino acids involved in GluR7 ion channel function.
    Journal of Neuroscience 21(2): 401-411.

publications 1996 to 2000

  • P. Kizelsztein, M. Eisenstein, N. Strutz, M. Hollmann, and V.I. Teichberg (2000).
    Mutant cycle analysis of the active and desensitized states of an AMPA receptor induced by willardiines.
    Biochemistry 39(42): 12819-12827.
    doi: 10.1021/bi000962i
  • I. Paarmann, D. Frermann, B.U. Keller, and M. Hollmann (2000).
    Expression of 15 glutamate receptor subunits and various splice variants in tissue slices and single neurons of brainstem nuclei, and potential functional implications.
    Journal of Neurochemistry 74(4): 1335-1345.
    doi: 10.1046/j.1471-4159.2000.0741335.x
  • H.S. White, R.T. McCabe, H. Armstrong, S. Donevan, L.J. Cruz, F.C. Abogadie, J. Torres, J.E. Rivier, I. Paarmann, M. Hollmann, and B.M. Olivera (2000).
    In vitro and in vivo characterization of Conantokin-R, a selective NMDA receptor antagonist isolated from the venom of the fish-hunting snail Conus radiatus.
    Journal of Pharmacology and Experimental Therapeutics 292(1): 425-432.
  • A. Thalhammer, T. Morth, N. Strutz, and M. Hollmann (1999).
    A desensitization-inhibiting mutation in the glutamate binding site of rat α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is dominant in heteromultimeric complexes.
    Neuroscience Letters 277(3): 161-164.
    doi: 10.1016/S0304-3940(99)00885-X
  • C. Villmann, N. Strutz, T. Morth, and M. Hollmann (1999).
    Investigation by ion channel domain transplantation of rat glutamate receptor subunits, orphan receptors, and a putative NMDA receptor subunit.
    European Journal of Neuroscience 11(5): 1765-1778.
    doi: 10.1046/j.1460-9568.1999.00594.x
  • I. Everts, R. Petroski, P. Kizelsztein, V.I. Teichberg, S.F. Heinemann, and M. Hollmann (1999).
    Lectin-induced inhibition of desensitization of the kainate receptor GluR6 depends on the activation state and can be mediated by a single native or ectopic N-linked carbohydrate side chain.
    Journal of Neuroscience 19(3): 916-927.
  • M. Blaschke, D. Gremmels, I. Everts, E. Weigand, S.F. Heinemann, M. Hollmann, and B.U. Keller (1997).
    Pharmacological differentiation between neuronal and recombinant glutamate receptor channels expressed in Xenopus oocytes.
    Neuropharmacology 36(11-12): 1489-1501.
    doi: 10.1016/S0028-3908(97)00151-2
  • I. Everts, C. Villmann, and M. Hollmann (1997).
    N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation.
    Molecular Pharmacology 52(5): 861-873.
  • C. Villmann, L. Bull, and M. Hollmann (1997).
    Kainate binding proteins possess functional ion channel domains.
    Journal of Neuroscience 17(20): 7634-7643.
  • F. Soto, M. Garcia-Guzman, J.M. Gomez-Hernandez, M. Hollmann, C. Karschin, and W. Stühmer (1996).
    P2X4: An ATP-activated ionotropic receptor cloned from rat brain.
    Proceedings of the National Academy of Sciences (USA) 93(8): 3684-3688.

publications 1991 to 1995

  • M. Hollmann, C. Maron, and S. Heinemann (1994).
    N-Glycosylation site tagging suggests a three transmembrane domain topology for the glutamate receptor GluR1.
    Neuron 13(6): 1331-1343.
    doi: 10.1016/0896-6273(94)90419-7
  • M. Blaschke, B.U. Keller, R. Rivosecchi, M. Hollmann, S. Heinemann, and A. Konnerth (1993).
    A single amino-acid determines the subunit-specific spider toxin block of α-amino-3-hydroxy-5-methylisoxazole-4-propionate/kainate receptor channels.
    Proceedings of the National Academy of Sciences (USA) 90(14): 6528-6532.
  • M. Hollmann, J. Boulter, C. Maron, L. Beasley, J. Sullivan, G. Pecht, and S. Heinemann (1993).
    Zinc potentiates agonist-induced currents at certain splice variants of the NMDA receptor.
    Neuron 10(5): 943-954.
    doi: 10.1016/0896-6273(93)90209-A
  • B.U. Keller, M. Blaschke, R. Rivosecchi, M. Hollmann, S. Heinemann, and A. Konnerth (1993).
    Identification of a subunit-specific antagonist of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate/kainate receptor channels.
    Proceedings of the National Academy of Sciences (USA) 90(2): 605-609.
  • B.U. Keller, M. Hollmann, S. Heinemann, and A. Konnerth (1992).
    Calcium influx through subunits GluR1/GluR3 of kainate/AMPA receptor channels is regulated by cAMP dependent protein kinase.
    EMBO Journal 11(3): 891-896.
  • S.W. Rogers, T.E. Hughes, M. Hollmann, G.P. Gasic, E.S. Deneris, and S. Heinemann (1991).
    The characterization and localization of the glutamate receptor subunit GluR1 in the rat brain.
    Journal of Neuroscience 11(9): 2713-2724.
  • M. Hollmann, M. Hartley, and S. Heinemann (1991).
    Ca2+ permeability of KA-AMPA-gated glutamate receptor channels depends on subunit composition.
    Science 252(5007): 851-853.
    doi: 10.1126/science.1709304

publications 1985 to 1990

  • B. Bettler, J. Boulter, I. Hermans-Borgmeyer, A. O'Shea-Greenfield, E.S. Deneris, C. Moll, U. Borgmeyer, M. Hollmann, and S. Heinemann (1990).
    Cloning of a novel glutamate receptor subunit, GluR5: expression in the nervous system during development.
    Neuron 5(5): 583-595.
    doi: 10.1016/0896-6273(90)90213-Y
  • J. Boulter, M. Hollmann, A. O’Shea-Greenfield, M. Hartley, E. Deneris, C. Maron, and S. Heinemann (1990).
    Molecular cloning and functional expression of glutamate receptor subunit genes.
    Science 249(4972): 1033-1037.
    doi: 10.1126/science.2168579
  • M. Hollmann, A. O’Shea-Greenfield, S.W. Rogers, and S. Heinemann (1989).
    Cloning by functional expression of a member of the glutamate receptor family.
    Nature 342(6250): 643-648.
    doi: 10.1038/342643a0
  • M. Hollmann and W. Seifert (1989).
    Glutamate transport and not glutamate receptor binding is stimulated by gangliosides in a Ca2+-dependent manner in rat brain synaptic plasma membranes.
    Journal of Neurochemistry 53(3): 716-723.
    doi: 10.1111/j.1471-4159.1989.tb11763.x
  • M. Hollmann, J. Harnecker, and W. Seifert (1988).
    Calcium ions induce glutamate transport into rat brain membrane vesicles in the absence of sodium and chloride: evidence for a novel uptake site?
    FEBS Letters 228(1): 74-78.
    doi: 10.1016/0014-5793(88)80588-X
  • M. Hollmann and W. Seifert (1986).
    Gangliosides modulate glutamate receptor binding in rat brain synaptic plasma membranes.
    Neuroscience Letters 65(2): 133-138.
    doi: 10.1016/0304-3940(86)90292-2
  • J.M. Wolff, J. Pfeifle, M. Hollmann, and F.A. Anderer (1985).
    Immunodetection of nitrocellulose-adhesive proteins at the nanogram level after trinitrophenyl modification.
    Analytical Biochemistry 147(2): 396-400.
    doi: 10.1016/0003-2697(85)90288-X
  • M. Hollmann, H.J. Staab, E. Spindler, M. Sproll, F.A. Anderer, and H.P. Fortmeyer (1985).
    Monoclonal antibody-defined circulating human tumor-associated antigen with epitope shared by cytokeratins.
    Biochemical and Biophysical Research Communications 128(1): 34-39.
    doi: 10.1016/0006-291X(85)91640-7

Reviews 1986 to 1999

  • M. Hollmann (1999).
    Structure of ionotropic glutamate receptors.
    In: Handbook of Experimental Pharmacology, Vol. 141, Ionotropic Glutamate Receptors in the CNS, P. Jonas and H. Monyer, eds. Springer Verlag, Berlin, pp. 3-98.
  • M. Hollmann (1997).
    Transmembrantopologie der Glutamatrezeptoren.
    In: Max-Planck-Gesellschaft Jahrbuch 1997 (ed. Generalverwaltung der Max-Planck-Gesellschaft), pp. 229-233. Vandenhoeck & Ruprecht, Göttingen.
  • M. Hollmann (1996).
    The topology of glutamate receptors: Sorting through the domains.
    In: The Ionotropic Glutamate Receptors, D.T. Monaghan and R. Wenthold, eds. Humana Press, Totowa, NJ, USA, pp. 39-79.
  • M. Hollmann and S. Heinemann (1994).
    Cloned glutamate receptors.
    Annual Review of Neuroscience 17: 31-108.
    doi: 10.1146/
  • M. Hollmann, J. Boulter, C. Maron, and S. Heinemann (1994).
    Molecular biology of glutamate receptors: Potentiation of N-methyl-D-aspartate receptor splice variants by zinc.
    Renal Physiology and Biochemistry 17(3-4): 182-183.
    doi: 10.1159/000173813
  • G.P. Gasic and M. Hollmann (1992).
    Molecular neurobiology of glutamate receptors.
    Annual Review of Physiology 54: 507-536.
    doi: 10.1146/
  • S. Heinemann, B. Bettler, J. Boulter, E. Deneris, G. Gasic, M. Hartley, M. Hollmann, T.E. Hughes, and S. Rogers (1992).
    The glutamate receptor structure and function.
    In: Drug Research Related to Neuroactive Amino Acids, Alfred Benzon Symposium 32, A. Schousboe, N.H. Diemer, H. Kofod, eds., pp. 163-184; P.J. Schmidts Bogtrykkeri, Munksgaard, Copenhagen.
  • J. Boulter, B. Bettler, R. Dingledine, R. Duvoisin, J. Egebjerg, G. Gasic, M. Hartley, I. Hermans-Borgmeyer, M. Hollmann, T.E. Hughes, R.I. Hume, C. Moll, S. Rogers, and S. Heinemann (1992).
    Molecular biology of the glutamate receptors.
    In: Excitatory Amino Acids, R.P. Simon, ed., FIDIA Research Symposium Series 9, pp. 9-13, Thieme, New York/Stuttgart.
  • S. Heinemann, B. Bettler, J. Boulter, E. Deneris, G. Gasic, M. Hartley, M. Hollmann, T.E. Hughes, A. O'Shea-Greenfield, and S. Rogers (1991).
    The glutamate receptors: Genes, structure and expression.
    In: Neurotransmitter Regulation and Gene Transcription, E. Costa & T.H. Joh eds., FIDIA Research Foundation Symposium Series 7, pp. 143-165; Thieme, New York/Stuttgart.
  • S. Heinemann, B. Bettler, J. Boulter, E. Deneris, G. Gasic, M. Hartley, M. Hollmann, T.E. Hughes, A. O'Shea-Greenfield, and S. Rogers (1991).
    The glutamate receptors: Genes, structure and expression.
    In: Glutamate, Cell Death and Memory, P. Ascher, D.W. Choi, Y. Christen (eds.) Foundation IPSEN Springer, Berlin, pp. 12-29.
  • S. Heinemann, B. Bettler, J. Boulter, E. Deneris, G. Gasic, M. Hartley, T.E. Hughes, A. O'Shea-Greenfield, S. Rogers, and M. Hollmann (1991).
    The glutamate receptor gene family: evidence that the GluR1, GluR2 and GluR3 subunits form multiple glutamate receptors.
    In: Transmitter Amino Acid Receptors: Structure, Transduction and Models for Drug Development, E.A. Barnard & E. Costa, eds. FIDIA Research Foundation Symposium Series 6, pp. 341-355. Thieme, New York/Stuttgart.
  • S. Heinemann, B. Bettler, J. Boulter, E. Deneris, G. Gasic, M. Hartley, M. Hollmann, T.E. Hughes, A. O'Shea-Greenfield, and S. Rogers (1991).
    The glutamate receptor gene family.
    In: Excitatory Amino Acids, B.S. Meldrum, F. Moroni, R.P. Simon, and J.H. Woods (eds.), FIDIA Research Foundation Symposium Series 5, pp. 109-133; Raven Press, New York.
  • S. Heinemann, J. Boulter, J. Connolly, E. Deneris, R. Duvoisin, M. Hartley, I. Hermans-Borgmeyer, M. Hollmann, A. O’Shea-Greenfield, R. Papke, S. Rogers, and J. Patrick (1991).
    The nicotinic receptor genes.
    In: Clinical Neuropharmacology 14, Supplement 1 (ed. E. Costa). pp. S45-S61, Raven Press, New York.
  • S. Heinemann, J. Boulter, J. Connolly, E. Deneris, R. Duvoisin, M. Hartley, I. Hermans-Borgmeyer, M. Hollmann, A. O’Shea-Greenfield, R. Papke, S. Rogers, and J. Patrick (1991).
    Brain nicotinic receptor genes.
    In: Molecular Approaches to Drug Abuse Research, National Institute on Drug Abuse (NIDA) Research Monographs, Rockville; vol. 111, pp. 3-23.
  • M. Hollmann, S.W. Rogers, A. O’Shea-Greenfield, E.S. Deneris, T.E. Hughes, G. Gasic, and S. Heinemann (1990).
    The glutamate receptor GluR-K1: Structure, function, and expression in the brain.
    Cold Spring Harbor Symposia on Quantitative Biology 55, 41-55.
  • S. Heinemann, J. Boulter, J. Connolly, E. Deneris, R. Duvoisin, M. Hartley, I. Hermans-Borgmeyer, M. Hollmann, A. O’Shea-Greenfield, R. Papke, S. Rogers, and J. Patrick (1989).
    The nicotinic receptor genes.
    In: Hoechst-Roussel Pharmaceuticals Research Seminar, October 1989, Hershey, PA.
  • M. Hollmann and W. Seifert (1987).
    Stimulation of glutamate receptor binding in rat brain synaptic plasma membranes by gangliosides.
    In: New Trends in Ganglioside Research: Neurochemical and Neurodegenerative Aspects, R.K. Ledeen, G. Tettamanti, R. Yu, E. Hogan, and A. Yates, eds., pp. 513-519, Liviana Press, Padova.
  • W. Seifert, A. Wieraszko, H. Terlau, and M. Hollmann (1987).
    Gangliosides and neuronal plasticity in the hippocampus.
    In: Gangliosides and Modulation of Neuronal Functions, H. Rahmann, ed. NATO ASI Series H7: 523-528. Springer, Berlin/Heidelberg.
  • W. Seifert, M. Hollmann, D. Masco, and F. Förster (1987).
    Gangliosides as neuromodulatory and neurotrophic agents for central neurons.
    In: Metabolism and Development of the Nervous System, S. Tucek, ed. Proceedings of the 6th ESN-meeting in Prague, pp.35-40, Wiley & Sons, Chichester.
  • W. Seifert, M. Hollmann, and A. Wieraszko (1986).
    A functional role for ganglioside GM1 in synaptic transmission and synaptic plasticity of the rat hippocampus.
    In: Learning and Memory, H. Matthies, ed. Advances in Biosciences 59: 247-253. Pergamon Press, Oxford.