Correction to: Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT‑P301L mutation.

Autor: Daude N; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Kim C; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA., Kang SG; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Eskandari-Sedighi G; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Haldiman T; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA., Yang J; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Fleck SC; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Gomez-Cardona E; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Han ZZ; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Borrego-Ecija S; Neurological Tissue Bank of the Biobanc, Hospital Clinic, IDIBAPS, Barcelona, Spain., Wohlgemuth S; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Julien O; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Wille H; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Molina-Porcel L; Neurology Department, Hospital Clinic, IDIBAPS, Barcelona, Spain., Gelpi E; Neurological Tissue Bank of the Biobanc, Hospital Clinic, IDIBAPS, Barcelona, Spain.; Division of Neuropathology and Neurochemistry, Department of Neurology, Medical University of Vienna, Vienna, Austria., Safar JG; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA. jiri.safar@case.edu.; Department of Neurology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA. jiri.safar@case.edu., Westaway D; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada. david.westaway@ualberta.ca.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada. david.westaway@ualberta.ca.

Publikováno v: Acta neuropathologica [Acta Neuropathol] 2021 Mar; Vol. 141 (3), pp. 467-468.

Diverse, evolving conformer populations drive distinct phenotypes in frontotemporal lobar degeneration caused by the same MAPT-P301L mutation.

Autor: Daude N; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Kim C; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA., Kang SG; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Eskandari-Sedighi G; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Haldiman T; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA., Yang J; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Fleck SC; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Gomez-Cardona E; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Han ZZ; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Borrego-Ecija S; Neurological Tissue Bank of the Biobanc, Hospital Clinic, IDIBAPS, Barcelona, Spain., Wohlgemuth S; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada., Julien O; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Wille H; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada., Molina-Porcel L; Neurology Department, Hospital Clinic, IDIBAPS, Barcelona, Spain., Gelpi E; Neurological Tissue Bank of the Biobanc, Hospital Clinic, IDIBAPS, Barcelona, Spain.; Division of Neuropathology and Neurochemistry, Department of Neurology, Medical University of Vienna, Vienna, Austria., Safar JG; Department of Pathology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA. jiri.safar@case.edu.; Department of Neurology, Case Western Reserve University, Institute of Pathology Building, Rm 406, 2085 Adelbert Road, Cleveland, OH, 44106-4907, USA. jiri.safar@case.edu., Westaway D; Centre for Prions and Protein Folding Diseases, University of Alberta, 204 Brain and Aging Research Building, Edmonton, T6G 2M8, Canada. david.westaway@ualberta.ca.; Department of Biochemistry, University of Alberta, Edmonton, AB, Canada. david.westaway@ualberta.ca.

Publikováno v: Acta neuropathologica [Acta Neuropathol] 2020 Jun; Vol. 139 (6), pp. 1045-1070. Date of Electronic Publication: 2020 Mar 26.

α-Synuclein strains target distinct brain regions and cell types.

Autor: Lau A; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., So RWL; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Lau HHC; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada., Sang JC; Department of Chemistry, University of Cambridge, Cambridge, UK., Ruiz-Riquelme A; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; German Center for Neurodegenerative Diseases (DZNE), Tübingen, Germany., Fleck SC; Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.; Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada., Stuart E; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada., Menon S; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada., Visanji NP; Morton and Gloria Shulman Movement Disorders Centre, Toronto Western Hospital, Toronto, Ontario, Canada.; Edmond J. Safra Program in Parkinson's Disease, Toronto Western Hospital, Toronto, Ontario, Canada., Meisl G; Department of Chemistry, University of Cambridge, Cambridge, UK., Faidi R; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada., Marano MM; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Medicine, University of Toronto, Toronto, Ontario, Canada., Schmitt-Ulms C; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada., Wang Z; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada., Fraser PE; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada., Tandon A; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada.; Department of Medicine, University of Toronto, Toronto, Ontario, Canada., Hyman BT; Department of Neurology, Massachusetts General Hospital, Charlestown, MA, USA.; Department of Radiology, Massachusetts General Hospital, Charlestown, MA, USA.; Neuroscience Program, Harvard Medical School, Boston, MA, USA., Wille H; Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada.; Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada., Ingelsson M; Department of Public Health and Caring Sciences/Geriatrics, Uppsala University, Uppsala, Sweden., Klenerman D; Department of Chemistry, University of Cambridge, Cambridge, UK.; UK Dementia Research Institute, University of Cambridge, Cambridge, UK., Watts JC; Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada. joel.watts@utoronto.ca.; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. joel.watts@utoronto.ca.

Publikováno v: Nature neuroscience [Nat Neurosci] 2020 Jan; Vol. 23 (1), pp. 21-31. Date of Electronic Publication: 2019 Dec 02.

A validated LC-MS/MS method for the determination of homocysteic acid in biological samples.

Autor: Gurke R; pharmazentrum frankfurt/ZAFES, Institute of Clinical Pharmacology, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany. Electronic address: gurke@med.uni-frankfurt.de., Schmidt D; Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Branch for Translational Medicine and Pharmacology TMP, Theodor-Stern-Kai 7, 60596, Frankfurt am Main, Germany., Thomas D; pharmazentrum frankfurt/ZAFES, Institute of Clinical Pharmacology, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany., Fleck SC; Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Branch for Translational Medicine and Pharmacology TMP, Theodor-Stern-Kai 7, 60596, Frankfurt am Main, Germany., Geisslinger G; pharmazentrum frankfurt/ZAFES, Institute of Clinical Pharmacology, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany; Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Branch for Translational Medicine and Pharmacology TMP, Theodor-Stern-Kai 7, 60596, Frankfurt am Main, Germany., Ferreirós N; pharmazentrum frankfurt/ZAFES, Institute of Clinical Pharmacology, Goethe University, Theodor-Stern-Kai 7, 60590, Frankfurt am Main, Germany.

Publikováno v: Journal of pharmaceutical and biomedical analysis [J Pharm Biomed Anal] 2019 Sep 10; Vol. 174, pp. 578-587. Date of Electronic Publication: 2019 Jun 21.

Comparative estrogenicity of endogenous, environmental and dietary estrogens in pregnant women II: Total estrogenicity calculations accounting for competitive protein and receptor binding and potency.

Autor: Pande P; Health Effects and Exposure Science, Pacific Northwest National Laboratory, Richland, WA, 99352, USA. Electronic address: paritosh.pande@pnnl.gov., Fleck SC; Division of Biochemical Toxicology, National Center for Toxicological Research, U.S. Food and Drug Administration, Jefferson, AR, 72079, USA. Electronic address: stefanie.fleck@ime.fraunhofer.de., Twaddle NC; Division of Biochemical Toxicology, National Center for Toxicological Research, U.S. Food and Drug Administration, Jefferson, AR, 72079, USA. Electronic address: nathan.twaddle@fda.hhs.gov., Churchwell MI; Division of Biochemical Toxicology, National Center for Toxicological Research, U.S. Food and Drug Administration, Jefferson, AR, 72079, USA. Electronic address: mona.churchwell@fda.hhs.gov., Doerge DR; Division of Biochemical Toxicology, National Center for Toxicological Research, U.S. Food and Drug Administration, Jefferson, AR, 72079, USA. Electronic address: daniel.doerge@fda.hhs.gov., Teeguarden JG; Health Effects and Exposure Science, Pacific Northwest National Laboratory, Richland, WA, 99352, USA; Department of Environmental and Molecular Toxicology, Oregon State University, Corvallis, OR, 93771, USA. Electronic address: justin.teeguarden@pnl.gov.

Publikováno v: Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association [Food Chem Toxicol] 2019 Mar; Vol. 125, pp. 341-353. Date of Electronic Publication: 2018 Dec 13.