Cleavage site-directed antibodies reveal the prion protein in humans is shed by ADAM10 at Y226 and associates with misfolded protein deposits in neurodegenerative diseases.

Autor: Song F; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Kovac V; Centre for Immunology and Development, Blood Transfusion Centre of Slovenia (BTCS), Ljubljana, Slovenia., Mohammadi B; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Littau JL; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Scharfenberg F; Institute of Biochemistry, University of Kiel, Kiel, Germany., Matamoros Angles A; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Vanni I; Department of Food Safety and Veterinary Public Health, Istituto Superiore di Sanità, Rome, Italy., Shafiq M; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Orge L; National Institute for Agricultural and Veterinary Research (INIAV), Oeiras, Portugal.; Animal and Veterinary Research Centre (CECAV), University of Trás-os-Montes and Alto Douro (UTAD), Vila Real, Portugal., Galliciotti G; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Djakkani S; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Linsenmeier L; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Černilec M; Centre for Immunology and Development, Blood Transfusion Centre of Slovenia (BTCS), Ljubljana, Slovenia., Hartman K; Centre for Immunology and Development, Blood Transfusion Centre of Slovenia (BTCS), Ljubljana, Slovenia., Jung S; Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Bochum, Germany., Tatzelt J; Department of Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, Bochum, Germany.; Cluster of Excellence RESOLV, Ruhr University Bochum, Bochum, Germany., Neumann JE; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany.; Center for Molecular Neurobiology Hamburg (ZMNH), UKE, Hamburg, Germany., Damme M; Institute of Biochemistry, University of Kiel, Kiel, Germany., Tschirner SK; German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.; Neuroproteomics, School of Medicine and Health, Klinikum rechts der Isar, Technical University Munich, 81675, Munich, Germany., Lichtenthaler SF; German Center for Neurodegenerative Diseases (DZNE), Munich, Germany.; Neuroproteomics, School of Medicine and Health, Klinikum rechts der Isar, Technical University Munich, 81675, Munich, Germany.; Munich Cluster for Systems Neurology (SyNergy), Munich, Germany., Ricklefs FL; Department of Neurosurgery, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Sauvigny T; Department of Neurosurgery, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Schmitz M; Department of Neurology, University Medical Center Göttingen, Göttingen, Germany., Zerr I; Department of Neurology, University Medical Center Göttingen, Göttingen, Germany., Puig B; Department of Neurology, Experimental Research in Stroke and Inflammation (ERSI), UKE, Hamburg, Germany., Tolosa E; Department of Immunology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Ferrer I; Department of Pathology and Experimental Therapeutics, University of Barcelona, IDIBELL, Hospitalet de Llobregat, Spain., Magnus T; Department of Neurology, Experimental Research in Stroke and Inflammation (ERSI), UKE, Hamburg, Germany., Rupnik MS; Center for Physiology and Pharmacology, Medical University of Vienna, Vienna, Austria., Sepulveda-Falla D; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Matschke J; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Šmid LM; LNPR, Institute of Pathophysiology and Prion Laboratory, Institute of Pathology, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia., Bresjanac M; LNPR, Institute of Pathophysiology and Prion Laboratory, Institute of Pathology, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia., Andreoletti O; UMR INRAE ENVT 1225, Interactions Hôtes-Agents Pathogènes, École Nationale Vétérinaire de Toulouse, Toulouse, France., Krasemann S; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Foliaki ST; Laboratory of Persistent Viral Diseases, Division of Intramural Research, Rocky Mountain Laboratories, National Institutes of Health, Hamilton, MT, USA., Nonno R; Department of Food Safety and Veterinary Public Health, Istituto Superiore di Sanità, Rome, Italy., Becker-Pauly C; Institute of Biochemistry, University of Kiel, Kiel, Germany., Monzo C; Institute for Regenerative Medicine and Biotherapies (IRMB), Neural Stem Cell, MSC and Neurodegenerative Diseases, INSERM, Montpellier, France., Crozet C; Institute for Regenerative Medicine and Biotherapies (IRMB), Neural Stem Cell, MSC and Neurodegenerative Diseases, INSERM, Montpellier, France., Haigh CL; Laboratory of Persistent Viral Diseases, Division of Intramural Research, Rocky Mountain Laboratories, National Institutes of Health, Hamilton, MT, USA., Glatzel M; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany., Curin Serbec V; Centre for Immunology and Development, Blood Transfusion Centre of Slovenia (BTCS), Ljubljana, Slovenia. vladka.curin@ztm.si., Altmeppen HC; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany. h.altmeppen@uke.de.

Publikováno v: Acta neuropathologica [Acta Neuropathol] 2024 Jul 09; Vol. 148 (1), pp. 2. Date of Electronic Publication: 2024 Jul 09.

Morphological Transformations of SARS-CoV-2 Nucleocapsid Protein Biocondensates Mediated by Antimicrobial Peptides.

Autor: Campanile M; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 26, 80126, Naples, Italy., Kurtul ED; Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Dec R; Physical Chemistry I - Biophysical Chemistry, Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Strasse 4a, 44227, Dortmund, Germany., Möbitz S; Physical Chemistry I - Biophysical Chemistry, Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Strasse 4a, 44227, Dortmund, Germany., Del Vecchio P; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 26, 80126, Naples, Italy., Petraccone L; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 26, 80126, Naples, Italy., Tatzelt J; Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Oliva R; Department of Chemical Sciences, University of Naples Federico II, Via Cintia, 26, 80126, Naples, Italy., Winter R; Physical Chemistry I - Biophysical Chemistry, Department of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Strasse 4a, 44227, Dortmund, Germany.

Publikováno v: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 May 23; Vol. 30 (29), pp. e202400048. Date of Electronic Publication: 2024 Apr 10.

Key Role of the Solvent in Driving Liquid-Liquid Phase Separation

Autor: Adams, E., Ahlers, J., Bader, V., Pezzotti, S., Winklhofer, K. F., Tatzelt, J., Havenith, M.

Publikováno v: DPG Spring Meeting Condensed Matter Section, 26.-30.03.2023, Dresden, Germany

In recent years the importance of the aqueous solvent in influencing protein structure, function, and dynamics has been recognized. Coupling of water molecules to the protein surface results in an interfacial region in which water molecules within th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______4577::6503f8bf814dabb4364df3f0234be01c
https://www.hzdr.de/publications/Publ-37077-1

NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62.

Autor: Furthmann N; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Bader V; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany.; Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Angersbach L; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Blusch A; Department of Neurology, St Josef Hospital, Ruhr University Bochum, 44791, Bochum, Germany., Goel S; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Sánchez-Vicente A; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Krause LJ; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany.; Cluster of Excellence RESOLV, 44801, Bochum, Germany., Chaban SA; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Grover P; Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Trinkaus VA; Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany., van Well EM; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Jaugstetter M; Analytical Chemistry II, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Tschulik K; Cluster of Excellence RESOLV, 44801, Bochum, Germany.; Analytical Chemistry II, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44801, Bochum, Germany., Damgaard RB; Department of Biotechnology and Biomedicine, Technical University of Denmark, 2800, Kongens Lyngby, Denmark., Saft C; Department of Neurology, St Josef Hospital, Ruhr University Bochum, 44791, Bochum, Germany., Ellrichmann G; Department of Neurology, St Josef Hospital, Ruhr University Bochum, 44791, Bochum, Germany.; Department of Neurology, Klinikum Dortmund, University Witten/Herdecke, 44135, Dortmund, Germany., Gold R; Department of Neurology, St Josef Hospital, Ruhr University Bochum, 44791, Bochum, Germany., Koch A; Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Department of Neuropathology, Charitéplatz 1, 10117, Berlin, Germany., Englert B; Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Department of Neuropathology, Charitéplatz 1, 10117, Berlin, Germany.; Center for Neuropathology and Prion Research, Ludwig-Maximilians University, 81377, Munich, Germany., Westenberger A; Institute of Neurogenetics, University of Lübeck, Lübeck, Germany., Klein C; Institute of Neurogenetics, University of Lübeck, Lübeck, Germany., Jungbluth L; Ernst-Ruska Centre for Microscopy and Spectroscopy with Electrons (ER-C-3/Structural Biology), Forschungszentrum Jülich, Jülich, Germany.; Institute for Biological Information Processing (IBI-6/Cellular Structural Biology), Forschungszentrum Jülich, Jülich, Germany., Sachse C; Ernst-Ruska Centre for Microscopy and Spectroscopy with Electrons (ER-C-3/Structural Biology), Forschungszentrum Jülich, Jülich, Germany.; Institute for Biological Information Processing (IBI-6/Cellular Structural Biology), Forschungszentrum Jülich, Jülich, Germany.; Department of Biology, Heinrich Heine University, Düsseldorf, Germany., Behrends C; Munich Cluster for Systems Neurology, Faculty of Medicine, Ludwig-Maximilians-Universität München, Munich, Germany., Glatzel M; Institute of Neuropathology, University Medical Center Hamburg-Eppendorf, Martinistraße 52, 20251, Hamburg, Germany., Hartl FU; Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152, Martinsried, Germany.; Munich Cluster for Systems Neurology (SyNergy), 81377, Munich, Germany., Nakamura K; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA, USA.; Department of Neurology, University of California, San Francisco, CA, USA., Christine CW; Department of Neurology, University of California, San Francisco, CA, USA.; Weill Institute for Neurosciences, University of California San Francisco, San Francisco, CA, USA., Huang EJ; Department of Neurology, University of California, San Francisco, CA, USA.; Department of Pathology, University of California, San Francisco, CA, USA., Tatzelt J; Department Biochemistry of Neurodegenerative Diseases, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany.; Cluster of Excellence RESOLV, 44801, Bochum, Germany., Winklhofer KF; Department Molecular Cell Biology, Institute of Biochemistry and Pathobiochemistry, Ruhr University Bochum, 44801, Bochum, Germany. konstanze.winklhofer@rub.de.; Cluster of Excellence RESOLV, 44801, Bochum, Germany. konstanze.winklhofer@rub.de.

Publikováno v: Nature communications [Nat Commun] 2023 Dec 19; Vol. 14 (1), pp. 8368. Date of Electronic Publication: 2023 Dec 19.

Remodeling of the fibrillation pathway of ��-synuclein by interaction with antimicrobial peptide LL-III

Autor: Oliva, Rosario, Mukherjee, Sanjib K., Ostermeier, Lena, Pazurek, Lilli A., Kriegler, Simon, Bader, Verian, Prumbaum, Daniel, Raunser, Stefan, Winklhofer, Konstanze F., Tatzelt, J��rg, Winter, Roland

Liquid-liquid phase separation (LLPS) has emerged as a key mechanism for intracellular organization, and many recent studies have provided important insights into the role of LLPS in cell biology. There is also evidence that LLPS is associated with a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::73a36b4c9eccc3717acb140476222c3e