ArticleJournal of the American Society for Mass Spectrometry2018
Probing Conformational Dynamics of Tau Protein by Hydrogen/Deuterium Exchange Mass Spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Capturing Early Aggregation Transitions of Disordered Tau by Covalent Footprinting Mass Spectrometry.Analytical chemistry · 2026Article
- Unraveling the Structure and Dynamics of Ac-PHF6-NHACS chemical neuroscience · 2024Article
- Fundamentals of HDX-MS.Essays in biochemistry · 2023Review
- Complementary Structural Information for Antibody-Antigen Complexes from Hydrogen-Deuterium Exchange and Covalent Labeling Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Epitope Mapping with Diethylpyrocarbonate Covalent Labeling-Mass Spectrometry.Analytical chemistry · 2022Article
- Binding of the human antioxidation protein αRedox biology · 2021Article
- Research advances in hydrogen-deuterium exchange mass spectrometry for protein epitope mapping.Analytical and bioanalytical chemistry · 2021Review
- Neurodegenerative Proteinopathies in the Proteoform Spectrum-Tools and Challenges.International journal of molecular sciences · 2021Review
- The role of wild-type tau in Alzheimer's disease and related tauopathies.Journal of life sciences (Westlake Village, Calif.) · 2020Article
- Epitope and Paratope Mapping of PD-1/Nivolumab by Mass Spectrometry-Based Hydrogen-Deuterium Exchange, Cross-linking, and Molecular Docking.Analytical chemistry · 2020Article
- Advances and considerations in AD tau-targeted immunotherapy.Neurobiology of disease · 2020Review
- Applications of Mass Spectrometry in the Onset of Amyloid Fibril Formation: Focus on the Analysis of Early-Stage Oligomers.Frontiers in chemistry · 2020Review
- Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2019Article
- Tau Inclusions in Alzheimer's, Chronic Traumatic Encephalopathy and Pick's Disease. A Speculation on How Differences in Backbone Polarization Underlie Divergent Pathways of Tau Aggregation.Frontiers in neuroscience · 2019Article
- Conformational Assessment of Adnectin and Adnectin-Drug Conjugate by Hydrogen/Deuterium Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibrillization of the microtubule-associated protein tau has been recognized as one of the signature pathologies of the nervous system in Alzheimer's disease, progressive supranuclear palsy, and other tauopathies. The conformational transition of tau in the fibrillization process, tau monomer to soluble aggregates to fibrils in particular, remains unclear. Here we report on the use of hydrogen/deuterium exchange mass spectrometry (HDX-MS) in combination with other biochemical approaches, including Thioflavin S fluorescence measurements, enzyme-linked immunosorbent assay (ELISA), and Western blotting to understand the heparin-induced tau's fibrillization. HDX-MS studies including anti-tau antibody epitope mapping experiments provided molecular level details of the full-length tau's conformational dynamics and its regional solvent accessibility upon soluble aggregates formation. The results demonstrate that R3 region in the full-length tau's microtubule binding repeat region (MTBR) is stabilized in the aggregation process, leaving both N and C terminal regions to be solvent exposed in the soluble aggregates and fibrils. The findings also illustrate the practical utility of orthogonal analytical methodologies for the characterization of protein higher order structure. Graphical Abstract ᅟ.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.