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Tytuł :
An HDAC6-dependent surveillance mechanism suppresses tau-mediated neurodegeneration and cognitive decline.
Autorzy :
Trzeciakiewicz H; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, 27599-7260, USA.
Ajit D; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Tseng JH; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Chen Y; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Ajit A; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Tabassum Z; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Lobrovich R; Penn Digital Neuropathology Laboratory, Department of Neurology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-4283, USA.
Peterson C; Penn Digital Neuropathology Laboratory, Department of Neurology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-4283, USA.
Riddick NV; Division of Comparative Medicine, University of North Carolina, Chapel Hill, NC, 27599-7146, USA.
Itano MS; Department of Cell Biology and Physiology, Carolina Institute for Developmental Disabilities, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA.
Tripathy A; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, 27599-7260, USA.
Moy SS; Department of Psychiatry, Carolina Institute for Developmental Disabilities, University of North Carolina, Chapel Hill, NC, 27599-7146, USA.
Lee VMY; Department of Pathology & Laboratory Medicine, Center for Neurodegenerative Disease Research (CNDR), Institute on Aging, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-4283, USA.
Trojanowski JQ; Department of Pathology & Laboratory Medicine, Center for Neurodegenerative Disease Research (CNDR), Institute on Aging, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-4283, USA.
Irwin DJ; Penn Digital Neuropathology Laboratory, Department of Neurology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104-4283, USA.
Cohen TJ; Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC, 27599-7260, USA. .; Department of Neurology, UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC, 27599-7250, USA. .
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Źródło :
Nature communications [Nat Commun] 2020 Nov 02; Vol. 11 (1), pp. 5522. Date of Electronic Publication: 2020 Nov 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms :
Cognitive Dysfunction/*pathology
Histone Deacetylase 6/*metabolism
Tauopathies/*pathology
tau Proteins/*metabolism
Acetylation ; Aged ; Aged, 80 and over ; Animals ; Brain/pathology ; Cognitive Dysfunction/genetics ; Disease Models, Animal ; Disease Progression ; Female ; Histone Deacetylase 6/genetics ; Humans ; Male ; Mice ; Mice, Transgenic ; Middle Aged ; Phosphorylation ; Protein Processing, Post-Translational ; Tauopathies/genetics ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
PEG-Ceramide Nanomicelles Induce Autophagy and Degrade Tau Proteins in N2a Cells.
Autorzy :
Gao J; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.; Institute of Translational Medicine, Shanghai University, Shanghai 200444, People's Republic of China.
Chen X; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Ma T; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
He B; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Li P; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Zhao Y; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Ma Y; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Zhuang J; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
Yin Y; Department of Neurology, Changzheng Hospital, Second Military Medical University, Shanghai 200003, People's Republic of China.
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Źródło :
International journal of nanomedicine [Int J Nanomedicine] 2020 Sep 11; Vol. 15, pp. 6779-6789. Date of Electronic Publication: 2020 Sep 11 (Print Publication: 2020).
Typ publikacji :
Journal Article
MeSH Terms :
Autophagy/*drug effects
Ceramides/*pharmacology
Nanostructures/*chemistry
Neurons/*drug effects
tau Proteins/*metabolism
Alzheimer Disease/drug therapy ; Alzheimer Disease/pathology ; Animals ; Autophagosomes/metabolism ; Autophagy/physiology ; Brain Neoplasms/pathology ; Cell Line, Tumor ; Ceramides/chemistry ; Humans ; Lysosomes/drug effects ; Lysosomes/metabolism ; Mice ; Microtubule-Associated Proteins ; Neuroblastoma/pathology ; Neurons/metabolism ; Polyethylene Glycols/chemistry ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
The distinctive role of tau and amyloid beta in mitochondrial dysfunction through alteration in Mfn2 and Drp1 mRNA Levels: A comparative study in Drosophila melanogaster.
Autorzy :
Abtahi SL; Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran.
Masoudi R; Department of Biology, College of Sciences, Shiraz University, Shiraz, Iran. Electronic address: .
Haddadi M; Department of Biology, Faculty of Basic Sciences, University of Zabol, Zabol, Iran.
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Źródło :
Gene [Gene] 2020 Sep 05; Vol. 754, pp. 144854. Date of Electronic Publication: 2020 Jun 07.
Typ publikacji :
Comparative Study; Journal Article
MeSH Terms :
Amyloid beta-Peptides/*metabolism
Animals, Genetically Modified/*metabolism
Drosophila melanogaster/*metabolism
Dynamins/*metabolism
GTP Phosphohydrolases/*metabolism
Mitochondrial Membrane Transport Proteins/*metabolism
RNA, Messenger/*metabolism
tau Proteins/*metabolism
Animals ; Animals, Genetically Modified/genetics ; Brain/metabolism ; Drosophila melanogaster/genetics ; Dynamins/genetics ; GTP Phosphohydrolases/genetics ; Gene Expression Regulation ; Memory Disorders/metabolism ; Memory Disorders/pathology ; Mitochondria/metabolism ; Mitochondrial Membrane Transport Proteins/genetics ; Phosphorylation ; RNA, Messenger/genetics ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
[Regulatory role of Ca MK-Ⅱ and PP2A on hyperphosphorylated tau induced by Al Cl_3 in SH-SY5Y cells].
Autorzy :
Lu X; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
Cui S; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
Zhang Y; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
Xu S; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
Ju X; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
Niu Q; Department of Occupational Health, School of Public Health, Shanxi Medical University, Taiyuan 030001, China.
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Źródło :
Wei sheng yan jiu = Journal of hygiene research [Wei Sheng Yan Jiu] 2020 Jul; Vol. 49 (4), pp. 534-539.
Typ publikacji :
Journal Article
MeSH Terms :
tau Proteins*
Cell Line, Tumor ; Cell Survival ; Phosphorylation
Czasopismo naukowe
Tytuł :
RNA-binding proteins Musashi and tau soluble aggregates initiate nuclear dysfunction.
Autorzy :
Montalbano M; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA.; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
McAllen S; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA.; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Puangmalai N; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA.; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Sengupta U; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA.; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Bhatt N; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA.; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Johnson OD; School of Medicine, University of Texas Medical Branch, Galveston, TX, 77555, USA.
Kharas MG; Division of Molecular Pharmacology, Memorial Sloan Kettering Institute Cancer Center, New York City, NY, USA.
Kayed R; Mitchell Center for Neurodegenerative Diseases, University of Texas Medical Branch, Galveston, TX, 77555, USA. .; Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX, 77555, USA. .
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Źródło :
Nature communications [Nat Commun] 2020 Aug 27; Vol. 11 (1), pp. 4305. Date of Electronic Publication: 2020 Aug 27.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cell Nucleus/*pathology
Nerve Tissue Proteins/*metabolism
Neurodegenerative Diseases/*pathology
RNA-Binding Proteins/*metabolism
tau Proteins/*metabolism
Active Transport, Cell Nucleus ; Aged ; Aged, 80 and over ; Animals ; Cell Nucleus/metabolism ; Chromatin Assembly and Disassembly ; Cytoplasm/metabolism ; Disease Models, Animal ; Female ; Frontal Lobe/cytology ; Frontal Lobe/pathology ; HEK293 Cells ; Humans ; Inclusion Bodies/pathology ; Male ; Mice ; Mice, Transgenic ; Middle Aged ; Protein Aggregates ; Protein Binding ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
Chemogenetic attenuation of neuronal activity in the entorhinal cortex reduces Aβ and tau pathology in the hippocampus.
Autorzy :
Rodriguez GA; Taub Institute for Research on Alzheimer's disease and the Aging Brain, Columbia University Irving Medical Center, New York, New York, United States of America.; Department of Pathology and Cell Biology, Columbia University Irving Medical Center, New York, New York, United States of America.
Barrett GM; Taub Institute for Research on Alzheimer's disease and the Aging Brain, Columbia University Irving Medical Center, New York, New York, United States of America.; Department of Pathology and Cell Biology, Columbia University Irving Medical Center, New York, New York, United States of America.
Duff KE; Taub Institute for Research on Alzheimer's disease and the Aging Brain, Columbia University Irving Medical Center, New York, New York, United States of America.; Department of Pathology and Cell Biology, Columbia University Irving Medical Center, New York, New York, United States of America.; UK Dementia Research Institute at University College London, London, United Kingdom.
Hussaini SA; Taub Institute for Research on Alzheimer's disease and the Aging Brain, Columbia University Irving Medical Center, New York, New York, United States of America.; Department of Pathology and Cell Biology, Columbia University Irving Medical Center, New York, New York, United States of America.
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Źródło :
PLoS biology [PLoS Biol] 2020 Aug 21; Vol. 18 (8), pp. e3000851. Date of Electronic Publication: 2020 Aug 21 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*genetics
Amyloid beta-Protein Precursor/*genetics
Entorhinal Cortex/*metabolism
Tauopathies/*genetics
tau Proteins/*genetics
Action Potentials/physiology ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Alzheimer Disease/therapy ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/genetics ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Dependovirus/genetics ; Dependovirus/metabolism ; Disease Models, Animal ; Electrodes, Implanted ; Entorhinal Cortex/pathology ; Female ; Gene Expression Regulation ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Hippocampus/metabolism ; Hippocampus/pathology ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Neurons/metabolism ; Neurons/pathology ; Protein Aggregates ; Stereotaxic Techniques ; Tauopathies/metabolism ; Tauopathies/pathology ; Tauopathies/therapy ; Theta Rhythm/physiology ; Transduction, Genetic ; Transgenes ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
Correlation of pyroglutamate amyloid β and ptau Ser202/Thr205 levels in Alzheimer's disease and related murine models.
Autorzy :
Neddens J; QPS Austria GmbH, Grambach, Austria.
Daurer M; QPS Austria GmbH, Grambach, Austria.
Flunkert S; QPS Austria GmbH, Grambach, Austria.
Beutl K; QPS Austria GmbH, Grambach, Austria.; FH Joanneum Graz, Graz, Austria.
Loeffler T; QPS Austria GmbH, Grambach, Austria.
Walker L; Translational and Clinical Research Institute and Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle upon Tyne, United Kingdom.
Attems J; Translational and Clinical Research Institute and Newcastle University Institute for Ageing, Campus for Ageing and Vitality, Newcastle upon Tyne, United Kingdom.
Hutter-Paier B; QPS Austria GmbH, Grambach, Austria.
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Źródło :
PloS one [PLoS One] 2020 Jul 09; Vol. 15 (7), pp. e0235543. Date of Electronic Publication: 2020 Jul 09 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*metabolism
Amyloid beta-Peptides/*metabolism
Brain/*metabolism
tau Proteins/*metabolism
Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/genetics ; Animals ; Brain/pathology ; Disease Models, Animal ; Female ; Humans ; Male ; Mice ; Middle Aged ; Phosphorylation ; Pyrrolidonecarboxylic Acid/chemistry ; Species Specificity ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
Tau deposition in the spinal cord is not specific for CTE-ALS.
Autorzy :
Fournier CN; From the Department of Neurology (C.N.F., M.G., J.D.G.), Emory University School of Medicine, Atlanta; Department of Veterans Affairs (C.N.F.), Atlanta VA Medical Center; and Department of Pathology (M.G., J.D.G.), Emory University School of Medicine, Atlanta, GA. .
Gearing M; From the Department of Neurology (C.N.F., M.G., J.D.G.), Emory University School of Medicine, Atlanta; Department of Veterans Affairs (C.N.F.), Atlanta VA Medical Center; and Department of Pathology (M.G., J.D.G.), Emory University School of Medicine, Atlanta, GA.
Glass JD; From the Department of Neurology (C.N.F., M.G., J.D.G.), Emory University School of Medicine, Atlanta; Department of Veterans Affairs (C.N.F.), Atlanta VA Medical Center; and Department of Pathology (M.G., J.D.G.), Emory University School of Medicine, Atlanta, GA.
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Źródło :
Neurology [Neurology] 2020 Jul 07; Vol. 95 (1), pp. 37-39. Date of Electronic Publication: 2020 Jun 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Amyotrophic Lateral Sclerosis/*pathology
Chronic Traumatic Encephalopathy/*pathology
Spinal Cord/*pathology
tau Proteins/*analysis
Amyotrophic Lateral Sclerosis/complications ; Amyotrophic Lateral Sclerosis/metabolism ; Chronic Traumatic Encephalopathy/complications ; Chronic Traumatic Encephalopathy/metabolism ; Female ; Humans ; Male ; Middle Aged ; Spinal Cord/metabolism ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
Expression and purification of amyloid β-protein, tau, and α-synuclein in Escherichia coli : a review.
Autorzy :
Jia L; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.; College of Food Science and Engineering, Tianjin University of Science and Technology, Tianjin, China.
Zhao W; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Wei W; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Guo X; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Wang W; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Wang Y; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Sang J; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Lu F; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
Liu F; Key Laboratory of Industrial Fermentation Microbiology, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin, China.
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Źródło :
Critical reviews in biotechnology [Crit Rev Biotechnol] 2020 Jun; Vol. 40 (4), pp. 475-489. Date of Electronic Publication: 2020 Mar 22.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Amyloidogenic Proteins/*metabolism
Escherichia coli/*metabolism
Escherichia coli Proteins/*metabolism
alpha-Synuclein/*metabolism
tau Proteins/*metabolism
Amyloidogenic Proteins/isolation & purification ; Escherichia coli/isolation & purification ; Escherichia coli Proteins/isolation & purification ; Humans ; Proteostasis Deficiencies/metabolism ; alpha-Synuclein/isolation & purification ; tau Proteins/isolation & purification
Czasopismo naukowe
Tytuł :
A synthetic heparinoid blocks Tau aggregate cell uptake and amplification.
Autorzy :
Stopschinski BE; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.; Department of Neurology, RWTH University Aachen, 52074 Aachen, Germany.
Thomas TL; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Nadji S; PharmaRen Discovery LLC, Berkeley, Missouri 63134-3115.
Darvish E; PharmaRen Discovery LLC, Berkeley, Missouri 63134-3115.
Fan L; Shanghai Acana Pharmtech Co. Ltd., Berkeley, Missouri 63134-3115.
Holmes BB; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.; Department of Neurology, University of California, San Francisco, California 94143.
Modi AR; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Finnell JG; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Kashmer OM; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Estill-Terpack S; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Mirbaha H; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Luu HS; Department of Pathology, Children's Health, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Diamond MI; Center for Alzheimer's and Neurodegenerative Diseases, Peter O'Donnell Jr. Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas 75390 .
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Mar 06; Vol. 295 (10), pp. 2974-2983. Date of Electronic Publication: 2020 Jan 23.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Heparin, Low-Molecular-Weight/*metabolism
tau Proteins/*metabolism
Animals ; HEK293 Cells ; Heparin, Low-Molecular-Weight/chemistry ; Heparin, Low-Molecular-Weight/pharmacology ; Hippocampus/metabolism ; Humans ; Mice ; Neurons/metabolism ; Partial Thromboplastin Time ; Prion Diseases/metabolism ; Prion Diseases/pathology ; Protein Aggregates/drug effects ; Protein Binding ; Prothrombin Time ; Recombinant Proteins/biosynthesis ; Recombinant Proteins/chemistry ; Recombinant Proteins/isolation & purification ; tau Proteins/chemistry ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
Distinct microscopic mechanisms for the accelerated aggregation of pathogenic Tau mutants revealed by kinetic analysis.
Autorzy :
Yao QQ; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China. .
Hong L
Wu S
Perrett S
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Źródło :
Physical chemistry chemical physics : PCCP [Phys Chem Chem Phys] 2020 Apr 14; Vol. 22 (14), pp. 7241-7249. Date of Electronic Publication: 2020 Mar 24.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Aggregation, Pathological/*physiopathology
tau Proteins/*chemistry
tau Proteins/*genetics
Alzheimer Disease/physiopathology ; Fluorescence Resonance Energy Transfer ; Humans ; Kinetics ; Mutation ; tau Proteins/toxicity ; tau Proteins/ultrastructure
Czasopismo naukowe
Tytuł :
Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer's disease brain.
Autorzy :
Al-Hilaly YK; Dementia Research Group, Sussex Neuroscience, School of Life Sciences, University of Sussex, E Sussex, UK.; Chemistry Department, College of Science, Mustansiriyah University, Baghdad, Iraq.
Foster BE; Dementia Research Group, Sussex Neuroscience, School of Life Sciences, University of Sussex, E Sussex, UK.
Biasetti L; Dementia Research Group, Sussex Neuroscience, School of Life Sciences, University of Sussex, E Sussex, UK.
Lutter L; School of Biosciences, University of Kent, Canterbury, UK.
Pollack SJ; Dementia Research Group, Sussex Neuroscience, School of Life Sciences, University of Sussex, E Sussex, UK.
Rickard JE; Institute of Medical Sciences, University of Aberdeen, UK.
Storey JMD; Department of Chemistry, University of Aberdeen, UK.; TauRx Therapeutics Ltd., Aberdeen, UK.
Harrington CR; Institute of Medical Sciences, University of Aberdeen, UK.; TauRx Therapeutics Ltd., Aberdeen, UK.
Xue WF; School of Biosciences, University of Kent, Canterbury, UK.
Wischik CM; Institute of Medical Sciences, University of Aberdeen, UK.; TauRx Therapeutics Ltd., Aberdeen, UK.
Serpell LC; Dementia Research Group, Sussex Neuroscience, School of Life Sciences, University of Sussex, E Sussex, UK.
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Źródło :
FEBS letters [FEBS Lett] 2020 Mar; Vol. 594 (5), pp. 944-950. Date of Electronic Publication: 2019 Dec 01.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*metabolism
Neurofibrillary Tangles/*ultrastructure
tau Proteins/*chemistry
tau Proteins/*metabolism
Brain/metabolism ; Humans ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; Protein Domains ; tau Proteins/ultrastructure
Czasopismo naukowe
Tytuł :
Tau Reduction Prevents Key Features of Autism in Mouse Models.
Autorzy :
Tai C; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Chang CW; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Yu GQ; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Lopez I; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Yu X; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Wang X; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Guo W; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA.
Mucke L; Gladstone Institute of Neurological Disease, Gladstone Institutes, San Francisco, CA 94158, USA; Department of Neurology and Weill Institute for Neurosciences, University of California, San Francisco, San Francisco, CA 94143, USA. Electronic address: .
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Źródło :
Neuron [Neuron] 2020 May 06; Vol. 106 (3), pp. 421-437.e11. Date of Electronic Publication: 2020 Mar 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Autistic Disorder/*genetics
Megalencephaly/*genetics
tau Proteins/*genetics
Animals ; Autistic Disorder/metabolism ; Binding Sites ; Brain/metabolism ; Brain/pathology ; Cells, Cultured ; HEK293 Cells ; Humans ; Megalencephaly/metabolism ; Membrane Proteins/genetics ; Mice ; Mice, Inbred C57BL ; NAV1.1 Voltage-Gated Sodium Channel/genetics ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; PTEN Phosphohydrolase/chemistry ; PTEN Phosphohydrolase/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Proline-Rich Protein Domains ; Protein Binding ; Rats ; Rats, Sprague-Dawley ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
Microglial activation arises after aggregation of phosphorylated-tau in a neuron-specific P301S tauopathy mouse model.
Autorzy :
van Olst L; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands. Electronic address: .
Verhaege D; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands; VIB Center for Inflammation Research, Gent, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium.
Franssen M; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
Kamermans A; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
Roucourt B; reMYND NV, Leuven, Belgium.
Carmans S; reMYND NV, Leuven, Belgium.
Ytebrouck E; reMYND NV, Leuven, Belgium.
van der Pol SMA; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
Wever D; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
Popovic M; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
Vandenbroucke RE; VIB Center for Inflammation Research, Gent, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent, Belgium.
Sobrino T; Clinical Neurosciences Research Laboratory, Department of Neurology, Clinical University Hospital, Health Research Institute of Santiago de Compostela, Spain.
Schouten M; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands.
de Vries HE; Department of Molecular Cell Biology and Immunology, Amsterdam Neuroscience, Amsterdam UMC, Amsterdam, the Netherlands; Department of Medical Biochemistry, Amsterdam Cardiovascular Sciences, University of Amsterdam, Amsterdam, the Netherlands.
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Źródło :
Neurobiology of aging [Neurobiol Aging] 2020 May; Vol. 89, pp. 89-98. Date of Electronic Publication: 2020 Jan 10.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*metabolism
Frontotemporal Dementia/*metabolism
Microglia/*metabolism
Microglia/*pathology
Neurons/*metabolism
Tauopathies/*metabolism
tau Proteins/*metabolism
Alzheimer Disease/pathology ; Animals ; Disease Models, Animal ; Membrane Proteins/metabolism ; Mice ; Mutation ; Phosphorylation ; Protein Aggregation, Pathological ; Tauopathies/pathology ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
Novel tau filament fold in corticobasal degeneration.
Autorzy :
Zhang W; MRC Laboratory of Molecular Biology, Cambridge, UK.
Tarutani A; Department of Dementia and Higher Brain Function, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Newell KL; Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Murzin AG; MRC Laboratory of Molecular Biology, Cambridge, UK.
Matsubara T; Department of Neuropathology, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.
Falcon B; MRC Laboratory of Molecular Biology, Cambridge, UK.
Vidal R; Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Garringer HJ; Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Shi Y; MRC Laboratory of Molecular Biology, Cambridge, UK.
Ikeuchi T; Department of Molecular Genetics, Brain Research Institute, Niigata University, Niigata, Japan.
Murayama S; Department of Neuropathology, Tokyo Metropolitan Institute of Gerontology, Tokyo, Japan.
Ghetti B; Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, Indianapolis, IN, USA.
Hasegawa M; Department of Dementia and Higher Brain Function, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Goedert M; MRC Laboratory of Molecular Biology, Cambridge, UK. .
Scheres SHW; MRC Laboratory of Molecular Biology, Cambridge, UK. .
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Źródło :
Nature [Nature] 2020 Apr; Vol. 580 (7802), pp. 283-287. Date of Electronic Publication: 2020 Feb 12.
Typ publikacji :
Case Reports; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cryoelectron Microscopy*
Basal Ganglia Diseases/*pathology
Cerebral Cortex/*pathology
Tauopathies/*metabolism
Tauopathies/*pathology
tau Proteins/*chemistry
tau Proteins/*ultrastructure
Aged ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amino Acid Sequence ; Basal Ganglia Diseases/metabolism ; Brain Chemistry ; Cerebral Cortex/metabolism ; Chronic Traumatic Encephalopathy/metabolism ; Chronic Traumatic Encephalopathy/pathology ; Female ; Frontal Lobe/metabolism ; Frontal Lobe/pathology ; Humans ; Male ; Middle Aged ; Models, Molecular ; Pick Disease of the Brain/metabolism ; Pick Disease of the Brain/pathology ; Protein Folding ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
Basic Limonoid modulates Chaperone-mediated Proteostasis and dissolve Tau fibrils.
Autorzy :
Gorantla NV; Neurobiology Group, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India.; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India.
Das R; Neurobiology Group, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India.; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India.
Chidambaram H; Neurobiology Group, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India.; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India.
Dubey T; Neurobiology Group, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India.; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India.
Mulani FA; Division of Organic Chemistry, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India.; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India.
Thulasiram HV; Division of Organic Chemistry, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India. .; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India. .
Chinnathambi S; Neurobiology Group, Division of Biochemical Sciences, CSIR-National Chemical Laboratory, Dr. Homi Bhabha Road, 411008, Pune, India. .; Academy of Scientific and Innovative Research (AcSIR), 411008, Pune, India. .
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Źródło :
Scientific reports [Sci Rep] 2020 Mar 04; Vol. 10 (1), pp. 4023. Date of Electronic Publication: 2020 Mar 04.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Limonins*/chemistry
Limonins*/pharmacology
Molecular Docking Simulation*
tau Proteins*/chemistry
tau Proteins*/metabolism
Cell Nucleus/*metabolism
HSP70 Heat-Shock Proteins/*metabolism
Protein Aggregation, Pathological/*metabolism
Proteostasis/*drug effects
HEK293 Cells ; Heat Shock Transcription Factors/metabolism ; Humans
Czasopismo naukowe
Tytuł :
Continental and Antarctic Lichens: isolation, identification and molecular modeling of the depside tenuiorin from the Antarctic lichen Umbilicaria antarctica as tau protein inhibitor.
Autorzy :
Salgado F; Departmento de Química, Facultad de Ciencias, Universidad de Chile, Santiago, Chile.
Caballero J; Centro de Bioinformática y Simulación Molecular, Facultad de Ingeniería, Universidad de Talca, Talca, Chile.
Vargas R; Departamento de Biología, Universidad Metropolitana de Ciencias de la Educación, Ñuñoa, Santiago, Chile.
Cornejo A; Facultad de Medicina, Escuela de Tecnología Médica, Universidad Andrés Bello, Primer Piso, Santiago, Chile.
Areche C; Departmento de Química, Facultad de Ciencias, Universidad de Chile, Santiago, Chile.
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Źródło :
Natural product research [Nat Prod Res] 2020 Mar; Vol. 34 (5), pp. 646-650. Date of Electronic Publication: 2018 Nov 02.
Typ publikacji :
Journal Article
MeSH Terms :
Ascomycota/*chemistry
Depsides/*isolation & purification
Lichens/*chemistry
Resorcinols/*isolation & purification
tau Proteins/*antagonists & inhibitors
Alzheimer Disease/drug therapy ; Antarctic Regions ; Ascomycota/metabolism ; Binding Sites ; Depsides/chemistry ; Humans ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Protein Binding ; Resorcinols/chemistry ; Resorcinols/metabolism ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
Diagnostic value of plasma phosphorylated tau181 in Alzheimer's disease and frontotemporal lobar degeneration.
Autorzy :
Thijssen EH; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.; Neurochemistry Laboratory, Department of Clinical Chemistry, Amsterdam University Medical Centers, Vrije Universiteit, Amsterdam Neuroscience, Amsterdam, the Netherlands.
La Joie R; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Wolf A; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Strom A; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Wang P; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Iaccarino L; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Bourakova V; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Cobigo Y; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Heuer H; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Spina S; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
VandeVrede L; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Chai X; Eli Lilly and Company, Indianapolis, IN, USA.
Proctor NK; Eli Lilly and Company, Indianapolis, IN, USA.
Airey DC; Eli Lilly and Company, Indianapolis, IN, USA.
Shcherbinin S; Eli Lilly and Company, Indianapolis, IN, USA.
Duggan Evans C; Eli Lilly and Company, Indianapolis, IN, USA.
Sims JR; Eli Lilly and Company, Indianapolis, IN, USA.
Zetterberg H; Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.; Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.; Department of Neurodegenerative Disease, University College London Institute of Neurology, Queen Square, London, UK.; UK Dementia Research Institute, University College London, London, UK.
Blennow K; Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, Sahlgrenska Academy at the University of Gothenburg, Mölndal, Sweden.; Clinical Neurochemistry Laboratory, Sahlgrenska University Hospital, Mölndal, Sweden.
Karydas AM; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Teunissen CE; Neurochemistry Laboratory, Department of Clinical Chemistry, Amsterdam University Medical Centers, Vrije Universiteit, Amsterdam Neuroscience, Amsterdam, the Netherlands.
Kramer JH; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Grinberg LT; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.; Department of Pathology, University of California San Francisco, San Francisco, CA, USA.
Seeley WW; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.; Department of Pathology, University of California San Francisco, San Francisco, CA, USA.
Rosen H; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Boeve BF; Department of Neurology, Mayo Clinic, Rochester, MN, USA.
Miller BL; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Rabinovici GD; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.; Department of Radiology & Biomedical Imaging, University of California San Francisco, San Francisco, CA, USA.
Dage JL; Eli Lilly and Company, Indianapolis, IN, USA.
Rojas JC; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA.
Boxer AL; Memory and Aging Center, Department of Neurology, University of California San Francisco, San Francisco, CA, USA. .
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Corporate Authors :
Advancing Research and Treatment for Frontotemporal Lobar Degeneration (ARTFL) investigators
Źródło :
Nature medicine [Nat Med] 2020 Mar; Vol. 26 (3), pp. 387-397. Date of Electronic Publication: 2020 Mar 02.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*blood
Alzheimer Disease/*diagnosis
Frontotemporal Lobar Degeneration/*blood
Frontotemporal Lobar Degeneration/*diagnosis
tau Proteins/*blood
Aged ; Alzheimer Disease/cerebrospinal fluid ; Amyloid/metabolism ; Amyloid beta-Peptides/blood ; Amyloid beta-Peptides/cerebrospinal fluid ; Biomarkers/blood ; Biomarkers/cerebrospinal fluid ; Cognition ; Female ; Frontotemporal Lobar Degeneration/genetics ; Frontotemporal Lobar Degeneration/pathology ; Gray Matter/diagnostic imaging ; Gray Matter/pathology ; Heterozygote ; Humans ; Male ; Middle Aged ; Mutation/genetics ; Neurofilament Proteins/blood ; Phosphorylation ; Positron-Emission Tomography ; Severity of Illness Index ; tau Proteins/cerebrospinal fluid ; tau Proteins/genetics
Czasopismo naukowe
Tytuł :
Retinal nerve fiber layer thickness predicts CSF amyloid/tau before cognitive decline.
Autorzy :
Asanad S; Doheny Eye Institute, Los Angeles, CA, United States of America.; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.
Fantini M; Doheny Eye Institute, Los Angeles, CA, United States of America.; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.; Department of Medicine, Ophthalmology, University of Udine, Udine, Italy.
Sultan W; Doheny Eye Institute, Los Angeles, CA, United States of America.
Nassisi M; Doheny Eye Institute, Los Angeles, CA, United States of America.; Department of Clinical Sciences and Community Health, Ophthalmological Unit, IRCCS-Cà Granda Foundation-Ospedale Maggiore Policlinico, University of Milan, Milan, Italy.
Felix CM; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.
Wu J; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.
Karanjia R; Doheny Eye Institute, Los Angeles, CA, United States of America.; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.; Department of Ophthalmology, University of Ottawa, Ottawa, Ontario, Canada.; Ottawa Hospital Research Institute, Ottawa, Ontario, Canada.
Ross-Cisneros FN; Doheny Eye Institute, Los Angeles, CA, United States of America.
Sagare AP; Department of Physiology and Neuroscience, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, United States of America.
Zlokovic BV; Department of Physiology and Neuroscience, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, United States of America.
Chui HC; Department of Neurology, University of Southern California, Los Angeles, CA, United States of America.
Pogoda JM; Cipher Biostatistics & Reporting, Reno, NV, United States of America.
Arakaki X; Huntington Medical Research Institutes, Pasadena, CA, United States of America.
Fonteh AN; Huntington Medical Research Institutes, Pasadena, CA, United States of America.
Sadun AA; Doheny Eye Institute, Los Angeles, CA, United States of America.; Department of Ophthalmology, David Geffen School of Medicine at UCLA, Los Angeles, CA, United States of America.
Harrington MG; Huntington Medical Research Institutes, Pasadena, CA, United States of America.
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Źródło :
PloS one [PLoS One] 2020 May 29; Vol. 15 (5), pp. e0232785. Date of Electronic Publication: 2020 May 29 (Print Publication: 2020).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*genetics
Amyloid beta-Peptides/*genetics
Cognitive Dysfunction/*genetics
tau Proteins/*genetics
Aged ; Aged, 80 and over ; Alzheimer Disease/cerebrospinal fluid ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/cerebrospinal fluid ; Amyloidosis/cerebrospinal fluid ; Amyloidosis/diagnostic imaging ; Amyloidosis/genetics ; Amyloidosis/pathology ; Biomarkers/cerebrospinal fluid ; Cognitive Dysfunction/cerebrospinal fluid ; Cognitive Dysfunction/diagnostic imaging ; Cognitive Dysfunction/pathology ; Female ; Humans ; Male ; Middle Aged ; Nerve Fibers/metabolism ; Nerve Fibers/pathology ; Optic Disk/diagnostic imaging ; Optic Disk/metabolism ; Optic Disk/pathology ; Retina/diagnostic imaging ; Retina/metabolism ; Retina/pathology ; Retinal Ganglion Cells/metabolism ; Retinal Ganglion Cells/pathology ; Tomography, Optical Coherence ; tau Proteins/cerebrospinal fluid
Czasopismo naukowe

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