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© 2024 by the authors.There was an error in the original publication [1]. References 34, 41, 52, 53, 56, 61, 64, 65, 68, 69, 71, 72, 74, 75, 76, 77, 81, 85, 86, 110, 112, and 114 were not the ones intended, and were unrelated with the main text. A correction has been made to References 34, 41, 52, 53, 56, 61, 64, 65, 68, 69, 71, 72, 74, 75, 76, 77, 81, 85, 86, 110, 112, and 114, and appear as follows: Chaudhary, A.R.; Berger, F.; Berger, C.L.; Hendricks, A.G. Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams. Traffic 2018, 19, 111–121. Lim, S.; Haque, M.M.; Kim, D.; Kim, D.J.; Kim, Y.K. Cell-based Models To Investigate Tau Aggregation. Comput. Struct. Biotechnol. J. 2014, 12, 7–13. Lee, V.M.; Goedert, M.; Trojanowski, J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 2001, 24, 1121–1159. Rademakers, R.; Cruts, M.; van Broeckhoven, C. The role of tau (MAPT) in frontotemporal dementia and related tauopathies. Hum. Mutat. 2004, 24, 277–295. Cowan, C.M.; Mudher, A. Are tau aggregates toxic or protective in tauopathies? Front. Neurol. 2013, 4, 114. Furcila, D.; Domínguez-Álvaro, M.; DeFelipe, J.; Alonso-Nanclares, L. Subregional Density of Neurons, Neurofibrillary Tangles and Amyloid Plaques in the Hippocampus of Patients With Alzheimer’s Disease. Front. Neuroanat. 2019, 13, 99. He, Z.; Guo, J.L.; McBride, J.D.; Narasimhan, S.; Kim, H.; Changolkar, L.; Zhang, B.; Gathagan, R.J.; Yue, C.; Dengler, C.; et al. Amyloid-β plaques enhance Alzheimer’s brain tau-seeded pathologies by facilitating neuritic plaque tau aggregation. Nat. Med. 2018, 24, 29–38. Park, S.; Lee, J.H.; Jeon, J.H.; Lee, M.J. Degradation or aggregation: The ramifications of post-translational modifications on tau. BMB Rep. 2018, 51, 265–273, Erratum in BMB Rep. 2020, 53, 391. Elbaum-Garfinkle, S.; Rhoades, E. Identification of an aggregation-prone structure of tau. J. Am. Chem. Soc. 2012, 134, 16607–16613. Lee, V.M.; Balin, B.J.; Otvos, L., Jr.; Trojanowski, J.Q. A68: A major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991, 251, 675–678. Weissmann, C.; Reyher, H.J.; Gauthier, A.; Steinhoff, H.J.; Junge, W.; Brandt, R. Microtubule binding and trapping at the tip of neurites regulate tau motion in living neurons. Traffic 2009, 10, 1655–1668. Lathuilière, A.; Valdés, P.; Papin, S.; Cacquevel, M.; Maclachlan, C.; Knott, G.W.; Muhs, A.; Paganetti, P.; Schneider, B.L. Motifs in the tau protein that control binding to microtubules and aggregation determine pathological effects. Sci. Rep. 2017, 7, 13556. Barthélemy, N.R.; Li, Y.; Joseph-Mathurin, N.; Gordon, B.A.; Hassenstab, J.; Benzinger, T.L.; Buckles, V.; Fagan, A.M.; Perrin, R.J.; Goate, A.M.; et al. A soluble phosphorylated tau signature links tau, amyloid and the evolution of stages of dominantly inherited Alzheimer’s disease. Nat. Med. 2020, 26, 398–407. Mocanu, M.M.; Nissen, A.; Eckermann, K.; Khlistunova, I.; Biernat, J.; Drexler, D.; Petrova, O.; Schönig, K.; Bujard, H.; Mandelkow, E.; et al. The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J. Neurosci. 2008, 28, 737–748. Olsen, M.; Aguilar, X.; Sehlin, D.; Fang, X.T.; Antoni, G.; Erlandsson, A.; Syvänen, S. Astroglial Responses to Amyloid-Beta Progression in a Mouse Model of Alzheimer’s Disease. Mol. Imaging Biol. 2018, 20, 605–614. Valotassiou, V.; Malamitsi, J.; Papatriantafyllou, J.; Dardiotis, E.; Tsougos, I.; Psimadas, D.; Alexiou, S.; Hadjigeorgiou, G.; Georgoulias, P. SPECT and PET imaging in Alzheimer’s disease. Ann. Nucl. Med. 2018, 32, 583–593. Ferrer, I.; Andrés-Benito, P.; Zelaya, M.V.; Aguirre, M.E.E.; Carmona, M.; Ausín, K.; Lachén-Montes, M.; Fernández-Irigoyen, J.; Santamaría, E.; Del Rio, J.A. Familial globular glial tauopathy linked to MAPT mutations: Molecular neuropathology and seeding capacity of a prototypical mixed neuronal and glial tauopathy. Acta. Neuropathol. 2020, 139, 735–771. Novak, P.; Cehlar, O.; Skrabana, R.; Novak, M. Tau Conformation as a Target for Disease-Modifying Therapy: The Role of Truncation. J. Alzheimers Dis. 2018, 64, S535–S546. Amadoro, G.; Latina, V.; Corsetti, V.; Calissano, P. N-terminal tau truncation in the pathogenesis of Alzheimer’s disease (AD): Developing a novel diagnostic and therapeutic approach. Biochim. Biophys. Acta. Mol. Basis Dis. 2020, 1866, 165584. Maeda, S.; Sahara, N.; Saito, Y.; Murayama, M.; Yoshiike, Y.; Kim, H.; Miyasaka, T.; Murayama, S.; Ikai, A.; Takashima, A. Granular tau oligomers as intermediates of tau filaments. Biochemistry 2007, 46, 3856–3861. Michel, C.H.; Kumar, S.; Pinotsi, D.; Tunnacliffe, A.; St George-Hyslop, P.; Mandelkow, E.; Mandelkow, E.M.; Kaminski, C.F.; Kaminski Schierle, G.S. Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology. J. Biol. Chem. 2014, 289, 956–967. Weaver, C.L.; Espinoza, M.; Kress, Y.; Davies, P. Conformational change as one of the earliest alterations of tau in Alzheimer’s disease. Neurobiol. Aging 2000, 21, 719–727. Chaudhary, A.R.; Berger, F.; Berger, C.L.; Hendricks, A.G. Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams. Traffic 2018, 19, 111–121. Lim, S.; Haque, M.M.; Kim, D.; Kim, D.J.; Kim, Y.K. Cell-based Models To Investigate Tau Aggregation. Comput. Struct. Biotechnol. J. 2014, 12, 7–13. Lee, V.M.; Goedert, M.; Trojanowski, J.Q. Neurodegenerative tauopathies. Annu. Rev. Neurosci. 2001, 24, 1121–1159. Rademakers, R.; Cruts, M.; van Broeckhoven, C. The role of tau (MAPT) in frontotemporal dementia and related tauopathies. Hum. Mutat. 2004, 24, 277–295. Cowan, C.M.; Mudher, A. Are tau aggregates toxic or protective in tauopathies? Front. Neurol. 2013, 4, 114. Furcila, D.; Domínguez-Álvaro, M.; DeFelipe, J.; Alonso-Nanclares, L. Subregional Density of Neurons, Neurofibrillary Tangles and Amyloid Plaques in the Hippocampus of Patients With Alzheimer’s Disease. Front. Neuroanat. 2019, 13, 99. He, Z.; Guo, J.L.; McBride, J.D.; Narasimhan, S.; Kim, H.; Changolkar, L.; Zhang, B.; Gathagan, R.J.; Yue, C.; Dengler, C.; et al. Amyloid-β plaques enhance Alzheimer’s brain tau-seeded pathologies by facilitating neuritic plaque tau aggregation. Nat. Med. 2018, 24, 29–38. Park, S.; Lee, J.H.; Jeon, J.H.; Lee, M.J. Degradation or aggregation: The ramifications of post-translational modifications on tau. BMB Rep. 2018, 51, 265–273, Erratum in BMB Rep. 2020, 53, 391. Elbaum-Garfinkle, S.; Rhoades, E. Identification of an aggregation-prone structure of tau. J. Am. Chem. Soc. 2012, 134, 16607–16613. Lee, V.M.; Balin, B.J.; Otvos, L., Jr.; Trojanowski, J.Q. A68: A major subunit of paired helical filaments and derivatized forms of normal tau. Science 1991, 251, 675–678. Weissmann, C.; Reyher, H.J.; Gauthier, A.; Steinhoff, H.J.; Junge, W.; Brandt, R. Microtubule binding and trapping at the tip of neurites regulate tau motion in living neurons. Traffic 2009, 10, 1655–1668. Lathuilière, A.; Valdés, P.; Papin, S.; Cacquevel, M.; Maclachlan, C.; Knott, G.W.; Muhs, A.; Paganetti, P.; Schneider, B.L. Motifs in the tau protein that control binding to microtubules and aggregation determine pathological effects. Sci. Rep. 2017, 7, 13556. Barthélemy, N.R.; Li, Y.; Joseph-Mathurin, N.; Gordon, B.A.; Hassenstab, J.; Benzinger, T.L.; Buckles, V.; Fagan, A.M.; Perrin, R.J.; Goate, A.M.; et al. A soluble phosphorylated tau signature links tau, amyloid and the evolution of stages of dominantly inherited Alzheimer’s disease. Nat. Med. 2020, 26, 398–407. Mocanu, M.M.; Nissen, A.; Eckermann, K.; Khlistunova, I.; Biernat, J.; Drexler, D.; Petrova, O.; Schönig, K.; Bujard, H.; Mandelkow, E.; et al. The potential for beta-structure in the repeat domain of tau protein determines aggregation, synaptic decay, neuronal loss, and coassembly with endogenous Tau in inducible mouse models of tauopathy. J. Neurosci. 2008, 28, 737–748. Olsen, M.; Aguilar, X.; Sehlin, D.; Fang, X.T.; Antoni, G.; Erlandsson, A.; Syvänen, S. Astroglial Responses to Amyloid-Beta Progression in a Mouse Model of Alzheimer’s Disease. Mol. Imaging Biol. 2018, 20, 605–614. Valotassiou, V.; Malamitsi, J.; Papatriantafyllou, J.; Dardiotis, E.; Tsougos, I.; Psimadas, D.; Alexiou, S.; Hadjigeorgiou, G.; Georgoulias, P. SPECT and PET imaging in Alzheimer’s disease. Ann. Nucl. Med. 2018, 32, 583–593. Ferrer, I.; Andrés-Benito, P.; Zelaya, M.V.; Aguirre, M.E.E.; Carmona, M.; Ausín, K.; Lachén-Montes, M.; Fernández-Irigoyen, J.; Santamaría, E.; Del Rio, J.A. Familial globular glial tauopathy linked to MAPT mutations: Molecular neuropathology and seeding capacity of a prototypical mixed neuronal and glial tauopathy. Acta. Neuropathol. 2020, 139, 735–771. Novak, P.; Cehlar, O.; Skrabana, R.; Novak, M. Tau Conformation as a Target for Disease-Modifying Therapy: The Role of Truncation. J. Alzheimers Dis. 2018, 64, S535–S546. Amadoro, G.; Latina, V.; Corsetti, V.; Calissano, P. N-terminal tau truncation in the pathogenesis of Alzheimer’s disease (AD): Developing a novel diagnostic and therapeutic approach. Biochim. Biophys. Acta. Mol. Basis Dis. 2020, 1866, 165584. Maeda, S.; Sahara, N.; Saito, Y.; Murayama, M.; Yoshiike, Y.; Kim, H.; Miyasaka, T.; Murayama, S.; Ikai, A.; Takashima, A. Granular tau oligomers as intermediates of tau filaments. Biochemistry 2007, 46, 3856–3861. Michel, C.H.; Kumar, S.; Pinotsi, D.; Tunnacliffe, A.; St George-Hyslop, P.; Mandelkow, E.; Mandelkow, E.M.; Kaminski, C.F.; Kaminski Schierle, G.S. Extracellular monomeric tau protein is sufficient to initiate the spread of tau protein pathology. J. Biol. Chem. 2014, 289, 956–967. Weaver, C.L.; Espinoza, M.; Kress, Y.; Davies, P. Conformational change as one of the earliest alterations of tau in Alzheimer’s disease. Neurobiol. Aging 2000, 21, 719–727. The authors state that the scientific conclusions are unaffected. This correction was approved by the Academic Editor. The original publication has also been updated.
Author(s): Dominguez-Meijide A, Vasili E, Outeiro TF
Publication type: Note
Publication status: Published
Journal: Brain Sciences
Year: 2024
Volume: 14
Issue: 9
Print publication date: 01/09/2024
Online publication date: 09/09/2024
Acceptance date: 08/08/2024
ISSN (electronic): 2076-3425
Publisher: Multidisciplinary Digital Publishing Institute (MDPI)
URL: https://doi.org/10.3390/brainsci14090909
DOI: 10.3390/brainsci14090909
