Markus Zweckstetter

Research interests

Publications

• Alpha-synuclein research: defining strategic moves in the battle against Parkinson’s disease

  npj Parkinson s Disease · 2021 · https://doi.org/10.1038/s41531-021-00203-9

• Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates

  Nature Communications · 2020 · 10.1038/s41467-020-19843-1

• Lysine/RNA-interactions drive and regulate biomolecular condensation

  Nature Communications · 2019 · 10.1038/s41467-019-10792-y

• RNA polymerase II clustering through carboxy-terminal domain phase separation

  Nature Structural & Molecular Biology · 2018 · 10.1038/s41594-018-0112-y

• Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

  Nature Communications · 2017 · https://doi.org/10.1038/s41467-017-00480-0

• Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

  Proceedings of the National Academy of Sciences · 2015 · 10.1073/pnas.1504081112

• Structural Ensembles of Intrinsically Disordered Proteins Depend Strongly on Force Field: A Comparison to Experiment

  Journal of Chemical Theory and Computation · 2015 · https://doi.org/10.1021/acs.jctc.5b00736

• Structure of the Mitochondrial Translocator Protein in Complex with a Diagnostic Ligand

  Science · 2014 · 10.1126/science.1248725

• Hsp90-Tau Complex Reveals Molecular Basis for Specificity in Chaperone Action

  Cell · 2014 · 10.1016/j.cell.2014.01.037

• Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy

  Chemical Reviews · 2014 · 10.1021/cr400688u

• Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson’s disease

  Acta Neuropathologica · 2013 · 10.1007/s00401-013-1114-9

• NMR Characterization of Long-Range Order in Intrinsically Disordered Proteins

  Journal of the American Chemical Society · 2010 · 10.1021/ja101645g

• Phosphorylation at S87 Is Enhanced in Synucleinopathies, Inhibits α-Synuclein Oligomerization, and Influences Synuclein-Membrane Interactions

  Journal of Neuroscience · 2010 · 10.1523/jneurosci.5922-09.2010

• VDAC, a multi-functional mitochondrial protein regulating cell life and death

  Molecular Aspects of Medicine · 2010 · https://doi.org/10.1016/j.mam.2010.03.002

• Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

  PLoS Biology · 2009 · https://doi.org/10.1371/journal.pbio.1000034

• Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models

  The EMBO Journal · 2009 · 10.1038/emboj.2009.257

• Structure of the human voltage-dependent anion channel

  Proceedings of the National Academy of Sciences · 2008 · 10.1073/pnas.0808115105

• Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein

  Journal of Biological Chemistry · 2008 · 10.1074/jbc.m800747200

• NMR: prediction of molecular alignment from structure using the PALES software

  Nature Protocols · 2008 · 10.1038/nprot.2008.36

• Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement

  Journal of the American Chemical Society · 2006 · 10.1021/ja0618649

• Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

  Proceedings of the National Academy of Sciences · 2005 · 10.1073/pnas.0407881102

• Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

  Journal of Biological Chemistry · 2005 · 10.1074/jbc.m501565200

• Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein

  Proceedings of the National Academy of Sciences · 2005 · https://doi.org/10.1073/pnas.0407146102

• Mars - robust automatic backbone assignment of proteins

  Journal of Biomolecular NMR · 2004 · 10.1023/b:jnmr.0000042954.99056.ad

• NMR of α‐synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation

  The EMBO Journal · 2004 · 10.1038/sj.emboj.7600211

• Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMR

  Journal of the American Chemical Society · 2000 · https://doi.org/10.1021/ja0000908

Current projects

No projects listed.