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Chemistry

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Overview

Harald Steiner is affiliated with Ludwig-Maximilians-Universität München in Germany, where their research primarily spans biochemistry, genetics, molecular biology, and medicine. Their work integrates a diverse range of subfields including molecular biology, physiology, law, neurology, and computational theory and mathematics.

The scientist's research covers several main topics, reflecting a multidisciplinary approach. These include Alzheimer's disease research and treatments, protein structure and dynamics, law and political science, lipid membrane structure and behavior, computational drug discovery methods, neuroinflammation and neurodegeneration mechanisms, and machine learning in bioinformatics.

Steiner has published extensively, contributing significantly to the scientific literature in high-impact and specialized venues. Frequent publication outlets include:

  • Die Personalvertretung
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Zenodo (CERN European Organization for Nuclear Research)
  • eLife
  • Current Opinion in Neurobiology

Recent papers authored or co-authored by Steiner demonstrate a focus on neurodegenerative diseases and enzymatic processes associated with Alzheimer's disease. Notable publications include:

  • "Microbiota-derived short chain fatty acids modulate microglia and promote Aβ plaque deposition" (2021, eLife)
  • "Secretases in Alzheimer's disease: Novel insights into proteolysis of APP and TREM2" (2021, Current Opinion in Neurobiology)
  • "Membrane lipid remodeling modulates γ-secretase processivity" (2023, Journal of Biological Chemistry)
  • "γ-Secretase cleavage of the Alzheimer risk factor TREM 2 is determined by its intrinsic structural dynamics" (2020, The EMBO Journal)
  • "Pathogenic Aβ generation in familial Alzheimer's disease: novel mechanistic insights and therapeutic implications" (2020, Current Opinion in Neurobiology)

Collaborative efforts are evident in Steiner's frequent co-authorship network, including researchers such as Frits Kamp, Lukas P. Feilen, Johannes Trambauer, Shuyu Chen, and Martin Zacharias. These collaborations contribute to advancing knowledge within the fields of neurobiology and molecular mechanisms underlying neurodegenerative conditions.

Best Publications

  • Reconstitution of gamma-secretase activity.

    Dieter Edbauer;Edith Winkler;Joerg T. Regula;Brigitte Pesold

  • Presenilin-dependent γ-secretase processing of β-amyloid precursor protein at a site corresponding to the S3 cleavage of Notch

    Magdalena Sastre;Harald Steiner;Klaus Fuchs;Anja Capell

  • A γ-secretase inhibitor blocks Notch signaling in vivo and causes a severe neurogenic phenotype in zebrafish

    Andrea Geling;Harald Steiner;Michael Willem;Laure Bally‐Cuif

  • PEN-2 Is an Integral Component of the γ-Secretase Complex Required for Coordinated Expression of Presenilin and Nicastrin

    Harald Steiner;Edith Winkler;Dieter Edbauer;Stefan Prokop

  • Intracellular Generation and Accumulation of Amyloid β-Peptide Terminating at Amino Acid 42 *

    Christine Wild-Bode;Tsuneo Yamazaki;Anja Capell;Uwe Leimer

  • A loss of function mutation of presenilin-2 interferes with amyloid beta-peptide production and notch signaling.

    Harald Steiner;Karen Duff;Anja Capell;Helmut Romig

  • Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide.

    Sven Lammich;Masayasu Okochi;Masatoshi Takeda;Christoph Kaether

  • Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases

    Harald Steiner;Marcus Kostka;Helmut Romig;Gabriele Basset

  • Maturation and Pro-peptide Cleavage of β-Secretase

    Anja Capell;Harald Steiner;Michael Willem;Hartmut Kaiser

  • Presenilin and nicastrin regulate each other and determine amyloid β-peptide production via complex formation

    Dieter Edbauer;Edith Winkler;Christian Haass;Harald Steiner

  • Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1

    Masayasu Okochi;Harald Steiner;Akio Fukumori;Hisashi Tanii

  • Regulated intramembrane proteolysis – lessons from amyloid precursor protein processing

    Stefan F. Lichtenthaler;Christian Haass;Harald Steiner

  • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production

    Tobias Moehlmann;Edith Winkler;Xuefeng Xia;Dieter Edbauer

  • An Alzheimer‐associated TREM2 variant occurs at the ADAM cleavage site and affects shedding and phagocytic function

    Kai Schlepckow;Gernot Kleinberger;Akio Fukumori;Regina Feederle

  • Microbiota-derived short chain fatty acids modulate microglia and promote Aβ plaque deposition

    Alessio Vittorio Colombo;Rebecca Katie Sadler;Gemma Llovera;Vikramjeet Singh

  • Intramembrane Proteolysis by γ-Secretase

    Harald Steiner;Regina Fluhrer;Christian Haass

  • Expression of Alzheimer’s Disease-associated Presenilin-1 Is Controlled by Proteolytic Degradation and Complex Formation

    Harald Steiner;Anja Capell;Brigitte Pesold;Martin Citron

  • Insulin-degrading Enzyme Rapidly Removes the β-Amyloid Precursor Protein Intracellular Domain (AICD)

    Dieter Edbauer;Michael Willem;Sven Lammich;Harald Steiner

  • The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane.

    J. Wieland;A. M. Nitsche;J. Strayle;H. Steiner

  • Identification of distinct γ-secretase complexes with different APH-1 variants

    Keiro Shirotani;Dieter Edbauer;Stefan Prokop;Christian Haass

  • Alzheimer disease γ-secretase: a complex story of GxGD-type presenilin proteases

    Christian Haass;Harald Steiner

  • Presenilin-1 affects trafficking and processing of βAPP and is targeted in a complex with nicastrin to the plasma membrane

    Christoph Kaether;Sven Lammich;Dieter Edbauer;Michaela Ertl

Frequent Co-Authors

Christian Haass
Christian Haass Ludwig-Maximilians-Universität München
Anja Capell
Anja Capell Ludwig-Maximilians-Universität München
Dieter Edbauer
Dieter Edbauer German Center for Neurodegenerative Diseases
Matthias Brendel
Matthias Brendel Ludwig-Maximilians-Universität München
Stefan F. Lichtenthaler
Stefan F. Lichtenthaler German Center for Neurodegenerative Diseases
Peter Bartenstein
Peter Bartenstein Ludwig-Maximilians-Universität München
Ralf Baumeister
Ralf Baumeister University of Freiburg
Dieter Langosch
Dieter Langosch Technical University of Munich
Paul Cumming
Paul Cumming Queensland University of Technology
Masatoshi Takeda
Masatoshi Takeda Izumi University

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