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Neuroscience

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57
Citations
11485
World Ranking
4345
National Ranking
372

Biology and Biochemistry

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57
Citations
11518
World Ranking
13849
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Overview

Michael R. Kreutz is affiliated with the Leibniz Institute for Neurobiology in Germany. Their research primarily focuses on biochemistry, genetics, and molecular biology, with a significant interest in neuroscience. A substantial portion of their work intersects with molecular biology, cell biology, and cellular and molecular neuroscience, reflecting a broad engagement with the cellular mechanisms underlying neural function and pathology.

Their scholarly contributions emphasize topics such as neuroscience and neuropharmacology research, cellular transport and secretion, autophagy in disease and therapy, and Alzheimer's disease research and treatments. Additional research themes include RNA regulation and disease, endoplasmic reticulum stress and disease, and mitochondrial function and pathology.

Michael R. Kreutz has published extensively in several scientific venues, including bioRxiv (Cold Spring Harbor Laboratory), Cell Reports, Cellular and Molecular Life Sciences, The EMBO Journal, and Neuron. These platforms reflect a focus on high-impact journals in neurobiology and molecular life sciences.

Among the recent papers associated with their research are:

  • Autophagy and the endolysosomal system in presynaptic function, 2020, Cellular and Molecular Life Sciences
  • Autism-associated SHANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses, 2021, eLife
  • The needs of a synapse-How local organelles serve synaptic proteostasis, 2022, The EMBO Journal
  • Synaptic control of DNA methylation involves activity-dependent degradation of DNMT3A1 in the nucleus, 2020, Neuropsychopharmacology
  • Jacob-induced transcriptional inactivation of CREB promotes Aβ-induced synapse loss in Alzheimer's disease, 2023, The EMBO Journal

Frequent collaborators in their work include Anna Karpova, Katarzyna M. Grochowska, Maria Andres-Alonso, PingAn Yuanxiang, and Eckart D. Gundelfinger. This list suggests collaborative projects spanning various aspects of molecular neuroscience and cellular processes relevant to synaptic function and neurodegenerative diseases.

Best Publications

  • SynGO : An Evidence-Based, Expert-Curated Knowledge Base for the Synapse

    Frank Koopmans;Pim van Nierop;Maria Andres-Alonso;Andrea Byrnes

  • Autistic-like behaviours and hyperactivity in mice lacking ProSAP1/Shank2

    Michael J. Schmeisser;Elodie Ey;Stephanie Wegener;Juergen Bockmann

  • ProSAP/Shank proteins - a family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease.

    Tobias M. Boeckers;Jürgen Bockmann;Michael R. Kreutz;Eckart D. Gundelfinger

  • Proline-rich synapse-associated protein-1/cortactin binding protein 1 (ProSAP1/CortBP1) is a PDZ-domain protein highly enriched in the postsynaptic density.

    Tobias M. Boeckers;Michael R. Kreutz;Carsten Winter;Werner Zuschratter

  • Brevican-deficient mice display impaired hippocampal CA1 long-term potentiation but show no obvious deficits in learning and memory

    Cord Brakebusch;Constanze I. Seidenbecher;Fredrik Asztely;Uwe Rauch

  • Early neuronal dysfunction by amyloid β oligomers depends on activation of NR2B-containing NMDA receptors

    Raik Rönicke;Marina Mikhaylova;Sabine Rönicke;Jessica Meinhardt

  • Proline-rich synapse-associated proteins ProSAP1 and ProSAP2 interact with synaptic proteins of the SAPAP/GKAP family.

    Tobias M. Boeckers;Carsten Winter;Karl-Heinz Smalla;Michael R. Kreutz

  • Concerted action of zinc and ProSAP/Shank in synaptogenesis and synapse maturation

    Andreas M Grabrucker;Andreas M Grabrucker;Mary J Knight;Christian Proepper;Juergen Bockmann

  • Encoding and transducing the synaptic or extrasynaptic origin of NMDA receptor signals to the nucleus.

    Anna Karpova;Marina Mikhaylova;Marina Mikhaylova;Sujoy Bera;Julia Bär

  • Differential expression and dendritic transcript localization of Shank family members: identification of a dendritic targeting element in the 3′ untranslated region of Shank1 mRNA

    Tobias M. Böckers;Tobias M. Böckers;Mailin Segger-Junius;Peter Iglauer;Jürgen Bockmann;Jürgen Bockmann

  • Caldendrin–Jacob: A Protein Liaison That Couples NMDA Receptor Signalling to the Nucleus

    Daniela C Dieterich;Anna Karpova;Marina Mikhaylova;Irina Zdobnova

  • Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin.

    Tobias M. Böckers;Marie Germaine Mameza;Michael R. Kreutz;Jürgen Bockmann

  • The roles of protein expression in synaptic plasticity and memory consolidation

    Tali Rosenberg;Shunit Gal-Ben-Ari;Daniela C. Dieterich;Michael R. Kreutz

  • Zinc deficiency dysregulates the synaptic ProSAP/Shank scaffold and might contribute to autism spectrum disorders

    Stefanie Grabrucker;Linda Jannetti;Matti Eckert;Simone Gaub

  • Abelson interacting protein 1 (Abi-1) is essential for dendrite morphogenesis and synapse formation

    Christian Proepper;Svenja Johannsen;Stefan Liebau;Janine Dahl

  • Dynein light chain regulates axonal trafficking and synaptic levels of Bassoon

    Anna Fejtova;Daria Davydova;Ferdinand Bischof;Vesna Lazarevic

  • Apoptotic versus necrotic characteristics of retinal ganglion cell death after partial optic nerve injury.

    Annett Bien;Constanze I. Seidenbecher;Tobias M. Böckers;Bernhard A. Sabel

  • ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53.

    J. Bockmann;M. R. Kreutz;E. D. Gundelfinger;T. M. Böckers

  • C-terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3.

    Tobias M. Boeckers;Thomas Liedtke;Christina Spilker;Thomas Dresbach

  • Brevican-containing perineuronal nets of extracellular matrix in dissociated hippocampal primary cultures.

    Nora John;Hans Krügel;Renato Frischknecht;Karl-Heinz Smalla

  • Thyrotropin Expression in Hypophyseal Pars Tuberalis-Specific Cells is 3,5,3′-Triiodothyronine, Thyrotropin-Releasing Hormone, and Pit-1 Independent

    J. Bockmann;T. M. Böckers;C. Winter;W. Wittkowski

Frequent Co-Authors

Eckart D. Gundelfinger
Eckart D. Gundelfinger Leibniz Institute for Neurobiology
Constanze I. Seidenbecher
Constanze I. Seidenbecher Leibniz Institute for Neurobiology
Tobias M. Boeckers
Tobias M. Boeckers University of Ulm
Werner Zuschratter
Werner Zuschratter Leibniz Institute for Neurobiology
Craig C. Garner
Craig C. Garner Charité - University Medicine Berlin
Petra Wahle
Petra Wahle Ruhr University Bochum
Hans-Gert Bernstein
Hans-Gert Bernstein Otto-von-Guericke University Magdeburg
Hans-Christian Pape
Hans-Christian Pape University of Münster
Bernhard A. Sabel
Bernhard A. Sabel Otto-von-Guericke University Magdeburg
Bernhard Bogerts
Bernhard Bogerts Otto-von-Guericke University Magdeburg

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