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1. Full Text Tau aggregation influences cognition and hippocampal atrophy in the absence of beta-amyloid: a clinico-imaging-pathological study of primary age-related tauopathy (PART)
by Josephs, Keith A and Murray, Melissa E and Tosakulwong, Nirubol and Whitwell, Jennifer L and Knopman, David S and Machulda, Mary M and Weigand, Stephen D and Boeve, Bradley F and Kantarci, Kejal and Petrucelli, Leonard and Lowe, Val J and Jack, Clifford R and Petersen, Ronald C and Parisi, Joseph E and Dickson, Dennis W
Acta neuropathologica, ISSN 0001-6322, 05/2017, Volume 133, Issue 5, pp. 705 - 715
Neurofibrillary tangles | Alzheimer’s disease | MRI | PART | TDP-43 | Beta-amyloid | Cognition | Tauopathy | Hippocampus | Pathology | Neurosciences | Clinical Neurology | Neurosciences & Neurology | Life Sciences & Biomedicine | Science & Technology | Neurofibrillary Tangles - pathology | Age Factors | Humans | Magnetic Resonance Imaging - methods | Tauopathies - pathology | tau Proteins - metabolism | Male | Hippocampus - pathology | Atrophy | Amyloidogenic Proteins - metabolism | Tauopathies - diagnosis | Aged, 80 and over | Cognition - physiology | Female | Alzheimer's disease | Diagnostic imaging | Index Medicus | beta-amyloid | tauopathy | cognition | hippocampus | neurofibrillary tangles
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2. Full Text The acetylation of tau inhibits its function and promotes pathological tau aggregation
by Trojanowski, John Q and Lee, Virginia M. Y and Kwong, Linda K and Mills, Ian P and Guo, Jing L and Hurtado, David E and Cohen, Todd J
Nature communications, ISSN 2041-1723, 03/2011, Volume 2, Issue 1, pp. 252 - 252
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Immunohistochemistry | Neurons - pathology | Phosphorylation | Humans | Middle Aged | Male | Alzheimer Disease - pathology | Brain - metabolism | Microtubules - metabolism | Transfection | Mass Spectrometry | HEK293 Cells | Aged, 80 and over | Female | Lysine - metabolism | Membrane Proteins - metabolism | Neurons - metabolism | Acetylation | Lysine - analysis | Microtomy | Recombinant Proteins - metabolism | Membrane Proteins - genetics | Mice, Transgenic | Recombinant Proteins - genetics | Microtubules - pathology | Lysine - genetics | Animals | Alzheimer Disease - metabolism | Brain - pathology | Protein Binding | Aged | Mice | Protein Processing, Post-Translational | Alzheimer Disease - genetics | Index Medicus
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3. Full Text Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
by Chiti, Fabrizio and Dobson, Christopher M
Annual review of biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 27 - 68
amyloidosis | quality control | protein aggregation | protein homeostasis | conformational diseases | chaperones | functional amyloid | Protein aggregation | Quality control | Functional amyloid | Amyloidosis | Chaperones | Protein homeostasis | Conformational diseases | Proteostasis Deficiencies - metabolism | Molecular Chaperones - metabolism | History, 21st Century | Parkinson Disease - history | Humans | Proteostasis Deficiencies - history | Protein Aggregation, Pathological - history | Drugs, Investigational | Parkinson Disease - drug therapy | Amyloid - chemistry | Diabetes Mellitus, Type 2 - metabolism | Diabetes Mellitus, Type 2 - history | Molecular Targeted Therapy | Alzheimer Disease - pathology | Amyloid - metabolism | Protein Aggregation, Pathological - pathology | Protein Aggregation, Pathological - prevention & control | Parkinson Disease - metabolism | Immunoglobulin Light-chain Amyloidosis | Amyloid - genetics | Alzheimer Disease - history | Parkinson Disease - pathology | Amyloidosis - pathology | Amyloidosis - history | Gene Expression Regulation | Molecular Chaperones - genetics | Proteostasis Deficiencies - pathology | Alzheimer Disease - drug therapy | Amyloidosis - drug therapy | Protein Folding | Proteostasis Deficiencies - prevention & control | Alzheimer Disease - metabolism | Protein Conformation | Diabetes Mellitus, Type 2 - pathology | Proteostasis Deficiencies - drug therapy | Diabetes Mellitus, Type 2 - drug therapy | Amyloidosis - metabolism | Protein Aggregation, Pathological - metabolism | Physiological aspects | Development and progression | Genetic aspects | Protein folding | Amyloid beta-protein | Peptides | Diabetes mellitus | Fibrils | Parkinsons disease | Disorders | Agglomeration | Tissues | Human tissues | Proteins | Aggregates | β-Amyloid | Genetic factors | Alzheimers disease | Protein interaction | Index Medicus
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4. Full Text Targeting protein aggregation for the treatment of degenerative diseases
by Eisele, Yvonne S and Monteiro, Cecilia and Fearns, Colleen and Encalada, Sandra E and Wiseman, R. Luke and Powers, Evan T and Kelly, Jeffery W
Nature reviews. Drug discovery, ISSN 1474-1776, 11/2015, Volume 14, Issue 11, pp. 759 - 780
Pharmacology & Pharmacy | Life Sciences & Biomedicine | Biotechnology & Applied Microbiology | Science & Technology | Neurodegenerative Diseases - pathology | Humans | Treatment Outcome | Protein Transport - drug effects | Structure-Activity Relationship | Neurodegenerative Diseases - metabolism | Neurodegenerative Diseases - drug therapy | Protein Aggregation, Pathological - drug therapy | Prealbumin - antagonists & inhibitors | Biological Factors - therapeutic use | Animals | Prealbumin - metabolism | Protein Aggregation, Pathological - pathology | Protein Folding - drug effects | Prealbumin - chemistry | Biological Factors - pharmacology | Protein Aggregation, Pathological - metabolism | Degeneration (Pathology) | Care and treatment | Amyloidosis | Genetic aspects | Research | Index Medicus
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