His scientific interests lie mostly in Biochemistry, Biophysics, Alpha-synuclein, Protein structure and Cell biology. His Biophysics research integrates issues from Plasma protein binding, Tau protein, Microtubule assembly, Nuclear magnetic resonance spectroscopy and Microtubule. His Alpha-synuclein research is multidisciplinary, incorporating perspectives in Neurodegeneration, Stereochemistry and In vivo.
His research integrates issues of Protein secondary structure, Crystallography, Protein folding, Peptide sequence and Binding site in his study of Protein structure. The Phosphorylation research he does as part of his general Cell biology study is frequently linked to other disciplines of science, such as Neurotoxicity, therefore creating a link between diverse domains of science. His Phosphorylation research incorporates themes from Chromatin, RNA polymerase and Yeast.
Markus Zweckstetter mostly deals with Biophysics, Biochemistry, Nuclear magnetic resonance spectroscopy, Protein structure and Crystallography. His Biophysics study integrates concerns from other disciplines, such as Plasma protein binding, Tau protein, Microtubule and Phosphorylation. Markus Zweckstetter combines subjects such as Alpha-synuclein and Cell biology with his study of Biochemistry.
The various areas that Markus Zweckstetter examines in his Alpha-synuclein study include Mutation, Mutant, In vivo and Amyloid. His Protein structure study combines topics from a wide range of disciplines, such as Membrane protein and Protein folding. His Protein aggregation research is multidisciplinary, relying on both P3 peptide, α synuclein, Synucleinopathies, Neurodegeneration and Alzheimer's disease.
His primary areas of study are Biophysics, Tau protein, Phosphorylation, Protein aggregation and Intrinsically disordered proteins. His study in Biophysics is interdisciplinary in nature, drawing from both Nuclear magnetic resonance spectroscopy, In vitro, Microtubule and Membrane protein. His work carried out in the field of Nuclear magnetic resonance spectroscopy brings together such families of science as Protein structure, Cyclophilin A and Isomerase.
The Tau protein study combines topics in areas such as Tau pathology, Chaperone, Tubulin and Pharmacology, Drug. His biological study spans a wide range of topics, including Downregulation and upregulation and Alpha-synuclein, Synucleinopathies. His research investigates the connection between Protein aggregation and topics such as α synuclein that intersect with issues in Lewy body, Internalization, Dementia and Liquid liquid.
Markus Zweckstetter focuses on Biophysics, Tau protein, Phosphorylation, In vitro and Cell biology. His Biophysics study incorporates themes from Nuclear magnetic resonance spectroscopy, Microtubule, Dimer and Function. His work deals with themes such as Protein structure, Protein aggregation and Atrophy, which intersect with Nuclear magnetic resonance spectroscopy.
His Tau protein research includes themes of Atpase activity, Neurodegeneration, Chaperone, Intrinsically disordered proteins and Cellular homeostasis. His Phosphorylation research incorporates elements of Alpha-synuclein, Synucleinopathies, Yeast, Chromatin and RNA polymerase. Markus Zweckstetter interconnects RNA, Transcription and Gene in the investigation of issues within Cell biology.
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Release of long-range tertiary interactions potentiates aggregation of natively unstructured α-synuclein
Carlos W. Bertoncini;Young-Sang Jung;Claudio O. Fernandez;Wolfgang Hoyer.
Proceedings of the National Academy of Sciences of the United States of America (2005)
VDAC, a multi-functional mitochondrial protein regulating cell life and death.
Varda Shoshan-Barmatz;Vito De Pinto;Markus Zweckstetter;Ziv Raviv.
Molecular Aspects of Medicine (2010)
Structure of the human voltage-dependent anion channel
Monika Bayrhuber;Thomas Meins;Michael Habeck;Stefan Becker.
Proceedings of the National Academy of Sciences of the United States of America (2008)
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Marco D Mukrasch;Stefan Bibow;Jegannath Korukottu;Sadasivam Jeganathan.
PLOS Biology (2009)
Pre‐fibrillar α‐synuclein variants with impaired β‐structure increase neurotoxicity in Parkinson's disease models
Damla Pinar Karpinar;Madhu Babu Gajula Balija;Sebastian Kügler;Felipe Opazo.
The EMBO Journal (2009)
Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease
Rodolfo M. Rasia;Carlos W. Bertoncini;Derek Marsh;Wolfgang Hoyer.
Proceedings of the National Academy of Sciences of the United States of America (2005)
NMR: prediction of molecular alignment from structure using the PALES software.
Markus Zweckstetter.
Nature Protocols (2008)
Mars -- robust automatic backbone assignment of proteins.
Young-Sang Jung;Markus Zweckstetter.
Journal of Biomolecular NMR (2004)
Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein
Katerina E. Paleologou;Adrian W. Schmid;Carla C. Rospigliosi;Hai Young Kim.
Journal of Biological Chemistry (2008)
Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement.
Andrés Binolfi;Rodolfo M. Rasia;Carlos W. Bertoncini;Marcelo Ceolin.
Journal of the American Chemical Society (2006)
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