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Start Over Author "Joke Verelst" Topic 030104 developmental biology
3 results on '"Joke Verelst"'

1. A Novel Tau Antibody Detecting the First Amino-Terminal Insert Reveals Conformational Differences Among Tau Isoforms

Author

Joris Winderickx, Joke Verelst, Nick Geukens, Mohamed Laghmouchi, Elien De Smidt, Erik Stoops, Debby Thomas, Eugeen Vanmechelen, Joelle Rosseels, Maria Bjerke, Luc Buée, Dorien Vliegen, Sofie Carmans, Sofie Molenberghs, Vanessa Franssens, Sabiha Eddarkaoui, Sebastiaan Engelborghs, Cindy Francois, Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), Lille Neurosciences & Cognition - U 1172 (LilNCog), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille), ADx NeuroSciences NV [Ghent, Belgium], Institute Born-Bunge [Antwerp, Belgium], University of Antwerp (UA), Universitair Ziekenhuis Brussel = University Hospital of Brussels (UZ Brussel), Vrije Universiteit Brussel (VUB), Bio-Incubator [Heverlee, Belgium] (reMYND NV), BUEE, Luc, Lille Neurosciences & Cognition - U 1172 (LilNCog (ex-JPARC)), Universitair Ziekenhus Brussel (UZ Brussel), Clinical Biology, Clinical sciences, Neuroprotection & Neuromodulation, Neurology, and Pathological Anatomy

Subjects
0301 basic medicine, Gene isoform, medicine.drug_class, Transgene, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Saccharomyces cerevisiae, yeast, Monoclonal antibody, Biochemistry, Genetics and Molecular Biology (miscellaneous), Biochemistry, Tau isoforms, Epitope, Insert (molecular biology), 03 medical and health sciences, 0302 clinical medicine, medicine, Molecular Biosciences, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Molecular Biology, [SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], lcsh:QH301-705.5, Biology, Original Research, Medicine(all), biology, Chemistry, [SDV.NEU.NB] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, biology.organism_classification, Molecular biology, 3. Good health, 030104 developmental biology, lcsh:Biology (General), 030220 oncology & carcinogenesis, RNA splicing, biology.protein, monoclonal antibodies, Antibody, Tau, conformational differences
Abstract

As human Tau undergoes pathologically relevant post-translational modifications when expressed in yeast, the use of humanized yeast models for the generation of novel Tau monoclonal antibodies has previously been proven to be successful. In this study, human Tau2N4R-ΔK280 purified from yeast was used for the immunization of mice and subsequent selection of high affinity Tau-specific monoclonal antibodies. The characterization of four novel antibodies in different Tau model systems yielded a phosphorylation-dependent antibody (15A10), an antibody directed to the first microtubule-binding repeat domain (16B12), a carboxy-terminal antibody (20G10) and an antibody targeting an epitope on the hinge of the first and second amino-terminal insert (18F12). The latter was found to be conformation-dependent, suggesting structural differences between the Tau splicing isoforms and allowing insight in the roles played by the amino-terminal inserts. As this monoclonal antibody also has the capacity to detect tangle-like structures in different transgenic Tau mice and neurofibrillary tangles in brain sections of patients diagnosed with Alzheimer's disease, we also tested the diagnostic potential of 18F12 in a pilot study and found this monoclonal antibody to have the ability to discriminate Alzheimer's disease patients from control individuals based on increased Tau levels in the cerebrospinal fluid. ispartof: Frontiers In Molecular Biosciences vol:7 ispartof: location:Switzerland status: Published online

Published
2020

2. The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?

Author

Isabelle Landrieu, Yann Fichou, Joke Verelst, Eugeen Vanmechelen, Youssra K. Al-Hilaly, Luc Buée, Nick Geukens, François Devred, Audrey Perrotin, Miguel Medina, Louise C. Serpell, Caroline Smet-Nocca, Philipp O. Tsvetkov, Bernard Hanseeuw, Joris Winderickx, Department of Chemistry and Biochemistry [Los Angeles], University of California [Los Angeles] (UCLA), University of California (UC)-University of California (UC), University of Sussex, Institut de neurophysiopathologie (INP), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Oncologie biologique et Oncopharmacologie (CRO2), Aix Marseille Université (AMU)- Hôpital de la Timone [CHU - APHM] (TIMONE)-Institut National de la Santé et de la Recherche Médicale (INSERM), Catholic University of Leuven - Katholieke Universiteit Leuven (KU Leuven), ADx Neurosciences NV, Neuropsychologie cognitive et neuroanatomie fonctionnelles de la mémoire humaine, Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM), Cliniques Universitaires Saint-Luc [Bruxelles], Centro de Investigacion Biomédica en Red sobre Enfermedades Neurodegenerativas (CIBERNED), Instituto de Salud Carlos III [Madrid] (ISC), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U837 (JPArc), Université Lille Nord de France (COMUE)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, University of California-University of California, Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), École pratique des hautes études (EPHE)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Center for Biomedical Research in Neurodegenerative Diseases Network [Madrid, Spain] (CIBERNED ), Queen Sofia Foundation Alzheimer Center [Madrid, Spain] (CIEN Foundation), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer (JPArc - U837 Inserm), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université Lille 2 - Faculté de Médecine, UCL - SSS/IONS/NEUR - Clinical Neuroscience, UCL - (SLuc) Service de neurologie, Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)- Hôpital de la Timone [CHU - APHM] (TIMONE)-Aix Marseille Université (AMU), Normandie Université (NU)-Normandie Université (NU)-École pratique des hautes études (EPHE), Centre de Recherche Jean-Pierre AUBERT Neurosciences et Cancer - U1172 Inserm - U837 (JPArc), and Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Lille Nord de France (COMUE)-Université de Lille

Subjects
0301 basic medicine, Computer science, [SDV.NEU.NB]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Neurobiology, Review, lcsh:RC346-429, Translational Research, Biomedical, 0302 clinical medicine, PHOSPHORYLATED TAU, Alzheimer's disease diagnosis, CORE, Alzheimer’s disease, tau structure, tau aggregation, biology, PAIRED HELICAL FILAMENTS, Brain, Alzheimer's disease, 3. Good health, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, Tauopathies, Tau phosphorylation, Life Sciences & Biomedicine, PROTEIN-TAU, Amyloid, NEUROFIBRILLARY PATHOLOGY, Tau protein, tau Proteins, [SDV.CAN]Life Sciences [q-bio]/Cancer, Pathology and Forensic Medicine, 03 medical and health sciences, Cellular and Molecular Neuroscience, Protein Aggregates, CEREBROSPINAL-FLUID, Tau aggregation, mental disorders, Alzheimer’s disease diagnosis, Animals, Humans, lcsh:Neurology. Diseases of the nervous system, Science & Technology, Neurosciences, IN-VITRO, AGGREGATION, Tau structure, EMISSION-TOMOGRAPHY TRACER, 030104 developmental biology, biology.protein, Paired helical filaments, ALZHEIMERS-DISEASE BRAIN, Neurology (clinical), Neurosciences & Neurology, Neuroscience, 030217 neurology & neurosurgery
Abstract

Insights into tau molecular structures have advanced significantly in recent years. This field has been the subject of recent breakthroughs, including the first cryo-electron microscopy structures of tau filaments from Alzheimer's and Pick's disease inclusions, as well as the structure of the repeat regions of tau bound to microtubules. Tau structure covers various species as the tau protein itself takes many forms. We will here address a range of studies that help to define the many facets of tau protein structures and how they translate into pathogenic forms. New results shed light on previous data that need now to be revisited in order to up-date our knowledge of tau molecular structure. Finally, we explore how these data can contribute the important medical aspects of this research - diagnosis and therapeutics. ispartof: ACTA NEUROPATHOLOGICA COMMUNICATIONS vol:7 issue:1 ispartof: location:England status: published

Published
2019

3. Recent Insights on Alzheimer’s Disease Originating from Yeast Models

Author

Daniel P. Mulvihill, Melody Cools, Jimmy Beckers, Joke Verelst, David Seynnaeve, Joris Winderickx, Gernot Fruhmann, Mara Del Vecchio, and Vanessa Franssens

Subjects
0301 basic medicine, GAMMA-SECRETASE, Chemistry, Multidisciplinary, Review, yeast, MICROTUBULE-ASSOCIATED PROTEINS, lcsh:Chemistry, Kluyveromyces, 0302 clinical medicine, Ubiquitin, OXIDATIVE STRESS, lcsh:QH301-705.5, Spectroscopy, Kluyveromyces lactis, TAU-PROTEIN, biology, PAIRED HELICAL FILAMENTS, aggregation, General Medicine, Alzheimer's disease, Computer Science Applications, AMYLOID PRECURSOR PROTEIN, Chemistry, Physical Sciences, amyloid β, Life Sciences & Biomedicine, Alzheimer’s disease, Biochemistry & Molecular Biology, Saccharomyces cerevisiae, tau Proteins, Computational biology, Models, Biological, Catalysis, oligomerization, prion, Inorganic Chemistry, 03 medical and health sciences, Alzheimer Disease, ubiquitin, Schizosaccharomyces, Animals, Humans, Protein oligomerization, Physical and Theoretical Chemistry, Molecular Biology, Science & Technology, Amyloid beta-Peptides, Candida glabrata, Organic Chemistry, IN-VITRO, FRONTOTEMPORAL DEMENTIA, biology.organism_classification, Yeast, amyloid beta, 030104 developmental biology, Proteostasis, lcsh:Biology (General), lcsh:QD1-999, Schizosaccharomyces pombe, biology.protein, PROLYL ISOMERASE PIN1, Tau, BRAIN A-BETA, 030217 neurology & neurosurgery
Abstract

In this review article, yeast model-based research advances regarding the role of Amyloid-β (Aβ), Tau and frameshift Ubiquitin UBB+1 in Alzheimer’s disease (AD) are discussed. Despite having limitations with regard to intercellular and cognitive AD aspects, these models have clearly shown their added value as complementary models for the study of the molecular aspects of these proteins, including their interplay with AD-related cellular processes such as mitochondrial dysfunction and altered proteostasis. Moreover, these yeast models have also shown their importance in translational research, e.g., in compound screenings and for AD diagnostics development. In addition to well-established Saccharomyces cerevisiae models, new upcoming Schizosaccharomyces pombe, Candida glabrata and Kluyveromyces lactis yeast models for Aβ and Tau are briefly described. Finally, traditional and more innovative research methodologies, e.g., for studying protein oligomerization/aggregation, are highlighted. ispartof: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES vol:19 issue:7 ispartof: location:Switzerland status: published

Published
2018

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