NMR Studies of Tau Protein in Tauopathies
Tauopathies, including Alzheimer’s disease (AD), are the most troublesome of all age-related chronic conditions, as there are no well-established disease-modifying therapies for their prevention and treatment. Spatio-temporal distribution of tau protein pathology correlates with cognitive decline an...
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Frontiers Media S.A.
2021
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oai:doaj.org-article:217c956f629f478a813ac5043d5e89552021-11-11T10:25:34ZNMR Studies of Tau Protein in Tauopathies2296-889X10.3389/fmolb.2021.761227https://doaj.org/article/217c956f629f478a813ac5043d5e89552021-11-01T00:00:00Zhttps://www.frontiersin.org/articles/10.3389/fmolb.2021.761227/fullhttps://doaj.org/toc/2296-889XTauopathies, including Alzheimer’s disease (AD), are the most troublesome of all age-related chronic conditions, as there are no well-established disease-modifying therapies for their prevention and treatment. Spatio-temporal distribution of tau protein pathology correlates with cognitive decline and severity of the disease, therefore, tau protein has become an appealing target for therapy. Current knowledge of the pathological effects and significance of specific species in the tau aggregation pathway is incomplete although more and more structural and mechanistic insights are being gained using biophysical techniques. Here, we review the application of NMR to structural studies of various tau forms that appear in its aggregation process, focusing on results obtained from solid-state NMR. Furthermore, we discuss implications from these studies and their prospective contribution to the development of new tauopathy therapies.Kristine KitokaRostislav SkrabanaRostislav SkrabanaNorbert GasparikNorbert GasparikJozef HritzJozef HritzKristaps JaudzemsKristaps JaudzemsFrontiers Media S.A.articletaunuclear magnetic resonanceprotein structureAlzheimer’s diseasefilamentsBiology (General)QH301-705.5ENFrontiers in Molecular Biosciences, Vol 8 (2021) |
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tau nuclear magnetic resonance protein structure Alzheimer’s disease filaments Biology (General) QH301-705.5 |
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tau nuclear magnetic resonance protein structure Alzheimer’s disease filaments Biology (General) QH301-705.5 Kristine Kitoka Rostislav Skrabana Rostislav Skrabana Norbert Gasparik Norbert Gasparik Jozef Hritz Jozef Hritz Kristaps Jaudzems Kristaps Jaudzems NMR Studies of Tau Protein in Tauopathies |
description |
Tauopathies, including Alzheimer’s disease (AD), are the most troublesome of all age-related chronic conditions, as there are no well-established disease-modifying therapies for their prevention and treatment. Spatio-temporal distribution of tau protein pathology correlates with cognitive decline and severity of the disease, therefore, tau protein has become an appealing target for therapy. Current knowledge of the pathological effects and significance of specific species in the tau aggregation pathway is incomplete although more and more structural and mechanistic insights are being gained using biophysical techniques. Here, we review the application of NMR to structural studies of various tau forms that appear in its aggregation process, focusing on results obtained from solid-state NMR. Furthermore, we discuss implications from these studies and their prospective contribution to the development of new tauopathy therapies. |
format |
article |
author |
Kristine Kitoka Rostislav Skrabana Rostislav Skrabana Norbert Gasparik Norbert Gasparik Jozef Hritz Jozef Hritz Kristaps Jaudzems Kristaps Jaudzems |
author_facet |
Kristine Kitoka Rostislav Skrabana Rostislav Skrabana Norbert Gasparik Norbert Gasparik Jozef Hritz Jozef Hritz Kristaps Jaudzems Kristaps Jaudzems |
author_sort |
Kristine Kitoka |
title |
NMR Studies of Tau Protein in Tauopathies |
title_short |
NMR Studies of Tau Protein in Tauopathies |
title_full |
NMR Studies of Tau Protein in Tauopathies |
title_fullStr |
NMR Studies of Tau Protein in Tauopathies |
title_full_unstemmed |
NMR Studies of Tau Protein in Tauopathies |
title_sort |
nmr studies of tau protein in tauopathies |
publisher |
Frontiers Media S.A. |
publishDate |
2021 |
url |
https://doaj.org/article/217c956f629f478a813ac5043d5e8955 |
work_keys_str_mv |
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_version_ |
1718439108386226176 |