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alzheimer's disease prion diseases

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https://www.readbyqxmd.com/read/28342697/recent-publications-from-the-alzheimer-s-disease-neuroimaging-initiative-reviewing-progress-toward-improved-ad-clinical-trials
#1
REVIEW
Michael W Weiner, Dallas P Veitch, Paul S Aisen, Laurel A Beckett, Nigel J Cairns, Robert C Green, Danielle Harvey, Clifford R Jack, William Jagust, John C Morris, Ronald C Petersen, Andrew J Saykin, Leslie M Shaw, Arthur W Toga, John Q Trojanowski
INTRODUCTION: The Alzheimer's Disease Neuroimaging Initiative (ADNI) has continued development and standardization of methodologies for biomarkers and has provided an increased depth and breadth of data available to qualified researchers. This review summarizes the 450+ publications using ADNI data during 2014 and 2015. METHODS: We used standard searches to find publications using ADNI data. RESULTS: (1) Structural and functional changes, including subtle changes to hippocampal shape and texture, atrophy in areas outside of hippocampus, and disruption to functional networks, are detectable in presymptomatic subjects before hippocampal atrophy; (2) In subjects with abnormal β-amyloid deposition (Aβ+), biomarkers become abnormal in the order predicted by the amyloid cascade hypothesis; (3) Cognitive decline is more closely linked to tau than Aβ deposition; (4) Cerebrovascular risk factors may interact with Aβ to increase white-matter (WM) abnormalities which may accelerate Alzheimer's disease (AD) progression in conjunction with tau abnormalities; (5) Different patterns of atrophy are associated with impairment of memory and executive function and may underlie psychiatric symptoms; (6) Structural, functional, and metabolic network connectivities are disrupted as AD progresses...
March 22, 2017: Alzheimer's & Dementia: the Journal of the Alzheimer's Association
https://www.readbyqxmd.com/read/28320943/prion-protein-dynamics-before-aggregation
#2
Kinshuk Raj Srivastava, Lisa J Lapidus
Prion diseases, like Alzheimer's disease and Parkinson disease, are rapidly progressive neurodegenerative disorders caused by misfolding followed by aggregation and accumulation of protein deposits in neuronal cells. Here we measure intramolecular polypeptide backbone reconfiguration as a way to understand the molecular basis of prion aggregation. Our hypothesis is that when reconfiguration is either much faster or much slower than bimolecular diffusion, biomolecular association is not stable, but as the reconfiguration rate becomes similar to the rate of biomolecular diffusion, the association is more stable and subsequent aggregation is faster...
March 20, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28320296/biological-basis-for-amyloidogenesis-in-alzheimer-s-disease
#3
REVIEW
T V Andreeva, W J Lukiw, E I Rogaev
Certain cellular proteins normally soluble in the living organism under certain conditions form aggregates with a specific cross-β sheet structure called amyloid. These intra- or extracellular insoluble aggregates (fibers or plaques) are hallmarks of many neurodegenerative pathologies including Alzheimer's disease (AD), Huntington's disease, Parkinson's disease, prion disease, and other progressive neurological diseases that develop in the aging human central nervous system. Amyloid diseases (amyloidoses) are widespread in the elderly human population, a rapidly expanding demographic in many global populations...
February 2017: Biochemistry. Biokhimii︠a︡
https://www.readbyqxmd.com/read/28280572/thioflavin-t-as-an-amyloid-dye-fibril-quantification-optimal-concentration-and-effect-on-aggregation
#4
Christine Xue, Tiffany Yuwen Lin, Dennis Chang, Zhefeng Guo
Formation of amyloid fibrils underlies a wide range of human disorders, including Alzheimer's and prion diseases. The amyloid fibrils can be readily detected thanks to thioflavin T (ThT), a small molecule that gives strong fluorescence upon binding to amyloids. Using the amyloid fibrils of Aβ40 and Aβ42 involved in Alzheimer's disease, and of yeast prion protein Ure2, here we study three aspects of ThT binding to amyloids: quantification of amyloid fibrils using ThT, the optimal ThT concentration for monitoring amyloid formation and the effect of ThT on aggregation kinetics...
January 2017: Royal Society Open Science
https://www.readbyqxmd.com/read/28272432/melanosomal-formation-of-pmel-core-amyloid-is-driven-by-aromatic-residues
#5
Jia Shee Hee, Susan M Mitchell, Xinran Liu, Ralf M Leonhardt
PMEL is a pigment cell protein that forms physiological amyloid in melanosomes. Many amyloids and/or their oligomeric precursors are toxic, causing or contributing to severe, incurable diseases including Alzheimer's and prion diseases. Striking similarities in intracellular formation pathways between PMEL and various pathological amyloids including Aβ and PrP(Sc) suggest PMEL is an excellent model system to study endocytic amyloid. Learning how PMEL fibrils assemble without apparent toxicity may help developing novel therapies for amyloid diseases...
March 8, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28271922/prion-like-proteins-and-their-computational-identification-in-proteomes
#6
Cristina Batlle, Valentin Iglesias, Susanna Navarro, Salvador Ventura
The aberrant or misfolded forms of the prion protein have been described as the causative agents of rare transmissible spongiform encephalopathies. In addition, proteins associated with frequently occurring neurodegenerative disorders, such as Alzheimer's and Parkinson's, are shown to share prion-like properties and to spread the disease in the brain. Areas covered: Interest in the prion phenomenon has crystallized in a series of computational methods aimed at uncovering prion-like proteins at the proteome level...
March 20, 2017: Expert Review of Proteomics
https://www.readbyqxmd.com/read/28269779/alzheimer-s-disease-characterization-of-the-brain-sites-of-the-initial-tau-cytoskeletal-pathology-will-improve-the-success-of-novel-immunological-anti-tau-treatment-approaches
#7
Udo Rüb, Katharina Stratmann, Helmut Heinsen, Kay Seidel, Mohamed Bouzrou, Horst-Werner Korf
Alzheimer's disease (AD) represents the most frequent neurodegenerative disease of the human brain worldwide. Currently practiced treatment strategies for AD only include some less effective symptomatic therapeutic interventions, which unable to counteract the disease course of AD. New therapeutic attempts aimed to prevent, reduce, or remove the extracellular depositions of the amyloid-β protein did not elicit beneficial effects on cognitive deficits or functional decline of AD. In view of the failure of these amyloid-β-based therapeutic trials and the close correlation between the brain pathology of the cytoskeletal tau protein and clinical AD symptoms, therapeutic attention has since shifted to the tau cytoskeletal protein as a novel drug target...
March 2, 2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28259709/consensus-classification-of-posterior-cortical-atrophy
#8
Sebastian J Crutch, Jonathan M Schott, Gil D Rabinovici, Melissa Murray, Julie S Snowden, Wiesje M van der Flier, Bradford C Dickerson, Rik Vandenberghe, Samrah Ahmed, Thomas H Bak, Bradley F Boeve, Christopher Butler, Stefano F Cappa, Mathieu Ceccaldi, Leonardo Cruz de Souza, Bruno Dubois, Olivier Felician, Douglas Galasko, Jonathan Graff-Radford, Neill R Graff-Radford, Patrick R Hof, Pierre Krolak-Salmon, Manja Lehmann, Eloi Magnin, Mario F Mendez, Peter J Nestor, Chiadi U Onyike, Victoria S Pelak, Yolande Pijnenburg, Silvia Primativo, Martin N Rossor, Natalie S Ryan, Philip Scheltens, Timothy J Shakespeare, Aida Suárez González, David F Tang-Wai, Keir X X Yong, Maria Carrillo, Nick C Fox
INTRODUCTION: A classification framework for posterior cortical atrophy (PCA) is proposed to improve the uniformity of definition of the syndrome in a variety of research settings. METHODS: Consensus statements about PCA were developed through a detailed literature review, the formation of an international multidisciplinary working party which convened on four occasions, and a Web-based quantitative survey regarding symptom frequency and the conceptualization of PCA...
March 2, 2017: Alzheimer's & Dementia: the Journal of the Alzheimer's Association
https://www.readbyqxmd.com/read/28256219/mapping-the-broad-structural-and-mechanical-properties-of-amyloid-fibrils
#9
Guillaume Lamour, Roy Nassar, Patrick H W Chan, Gunes Bozkurt, Jixi Li, Jennifer M Bui, Calvin K Yip, Thibault Mayor, Hongbin Li, Hao Wu, Jörg A Gsponer
Amyloids are fibrillar nanostructures of proteins that are assembled in several physiological processes in human cells (e.g., hormone storage) but also during the course of infectious (prion) and noninfectious (nonprion) diseases such as Creutzfeldt-Jakob and Alzheimer's diseases, respectively. How the amyloid state, a state accessible to all proteins and peptides, can be exploited for functional purposes but also have detrimental effects remains to be determined. Here, we measure the nanomechanical properties of different amyloids and link them to features found in their structure models...
February 28, 2017: Biophysical Journal
https://www.readbyqxmd.com/read/28246183/bioassays-and-inactivation-of-prions
#10
Kurt Giles, Amanda L Woerman, David B Berry, Stanley B Prusiner
The experimental study of prions requires a model for their propagation. However, because prions lack nucleic acids, the simple techniques used to replicate bacteria and viruses are not applicable. For much of the history of prion research, time-consuming bioassays in animals were the only option for measuring infectivity. Although cell models and other in vitro tools for the propagation of prions have been developed, they all suffer limitations, and animal bioassays remain the gold standard for measuring infectivity...
February 28, 2017: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/28238712/the-prion-model-for-progression-and-diversity-of-neurodegenerative-diseases
#11
REVIEW
Barbara E Stopschinski, Marc I Diamond
The neuropathology of different neurodegenerative diseases begins in different brain regions, and involves distinct brain networks. Evidence indicates that transcellular propagation of protein aggregation, which is the basis of prion disease, might underlie the progression of pathology in neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, and Huntington's disease. The prion model predicts specific patterns of neuronal vulnerability and network involvement on the basis of the conformation of pathological proteins...
February 23, 2017: Lancet Neurology
https://www.readbyqxmd.com/read/28223916/the-emerging-roles-of-early-protein-folding-events-in-the-secretory-pathway-in-the-development-of-neurodegenerative-maladies
#12
REVIEW
Tatyana Dubnikov, Ehud Cohen
Although, protein aggregation and deposition are unifying features of various neurodegenerative disorders, recent studies indicate that different mechanisms can lead to the development of the same malady. Among these, failure in early protein folding and maturation emerge as key mechanistic events that lead to the manifestation of a myriad of illnesses including Alzheimer's disease and prion disorders. Here we delineate the cascade of maturation steps that nascent polypeptides undergo in the secretory pathway to become functional proteins, and the chaperones that supervise and assist this process, focusing on the subgroup of proline cis/trans isomerases...
2017: Frontiers in Neuroscience
https://www.readbyqxmd.com/read/28222507/recent-progress-in-alzheimer-s-disease-research-part-1-pathology
#13
Francis T Hane, Brenda Y Lee, Zoya Leonenko
The field of Alzheimer's disease (AD) research has grown exponentially over the past few decades, especially since the isolation and identification of amyloid-β from postmortem examination of the brains of AD patients. Recently, the Journal of Alzheimer's Disease (JAD) put forth approximately 300 research reports which were deemed to be the most influential research reports in the field of AD since 2010. JAD readers were asked to vote on these most influential reports. In this 3-part review, we review the results of the 300 most influential AD research reports to provide JAD readers with a readily accessible, yet comprehensive review of the state of contemporary research...
2017: Journal of Alzheimer's Disease: JAD
https://www.readbyqxmd.com/read/28217771/detection-inhibition-and-disintegration-of-amyloid-fibrils-the-role-of-optical-probes-and-macrocyclic-receptors
#14
Achikanath C Bhasikuttan, Jyotirmayee Mohanty
Amyloid fibrils are formed by the aberrant aggregation of proteins into highly ordered β-sheet structures and are believed to be the root cause of several neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, Prion diseases, etc. and have been the subject of extensive biochemical, biophysical and clinical studies. Developing methods for the early detection of fibril formation using optical spectroscopic techniques and inhibition/disintegration of amyloid fibrils/plaques by introducing small molecules have been a major challenge to establish a clinically facile therapeutic intervention to combat these neurodegenerative diseases...
February 20, 2017: Chemical Communications: Chem Comm
https://www.readbyqxmd.com/read/28211008/injected-amyloid-beta-in-the-olfactory-bulb-transfers-to-other-brain-regions-via-neural-connections-in-mice
#15
Baixuan He, Minying Zheng, Qiang Liu, Zhe Shi, Simei Long, Xilin Lu, Zhong Pei, Ti-Fei Yuan, Huanxing Su, Xiaoli Yao
Alzheimer's disease (AD) is characterized by progressive neuronal degeneration and pathological accumulation of amyloid plaques in the brain. It has been proposed that the prion-like spreading of amyloid beta (Aβ) protein could contribute to the progression of the disease. Olfactory bulb (OB) is one of the earliest brain regions affected in AD and olfaction is easily impaired prior to cognitive symptoms. However, it remains unclear whether Aβ accumulation in the OB would spread along olfactory projections to other connected brain regions and trigger further neurodegeneration...
February 16, 2017: Molecular Neurobiology
https://www.readbyqxmd.com/read/28193770/%C3%AE-amyloid-prions-and-the-pathobiology-of-alzheimer-s-disease
#16
Joel C Watts, Stanley B Prusiner
Alzheimer's disease (AD) is the most common neurodegenerative disease in humans and will pose a considerable challenge to healthcare systems in the coming years. Aggregation of the β-amyloid (Aβ) peptide within the brain is thought to be an initiating event in AD pathogenesis. Many recent studies in transgenic mice have provided evidence that Aβ aggregates become self-propagating during disease, leading to a cascade of protein aggregation in the brain, which may underlie the progressive nature of AD. The ability to self-propagate and the existence of distinct "strains" reveals that Aβ aggregates exhibit many properties indistinguishable from those of prions composed of PrP(Sc) proteins...
February 13, 2017: Cold Spring Harbor Perspectives in Medicine
https://www.readbyqxmd.com/read/28193724/neurodegenerative-disease-transmission-and-transgenesis-in-mice
#17
Brittany N Dugger, Daniel P Perl, George A Carlson
Although the discovery of the prion protein (PrP) resulted from its co-purification with scrapie infectivity in Syrian hamsters, work with genetically defined and genetically modified mice proved crucial for understanding the fundamental processes involved not only in prion diseases caused by PrP misfolding, aggregation, and spread but also in other, much more common, neurodegenerative brain diseases. In this review, we focus on methodological and conceptual approaches used to study scrapie and related PrP misfolding diseases in mice and how these approaches have advanced our understanding of related disorders including Alzheimer's and Parkinson's disease...
February 13, 2017: Cold Spring Harbor Perspectives in Biology
https://www.readbyqxmd.com/read/28178353/cystatin-f-is-a-biomarker-of-prion-pathogenesis-in-mice
#18
Mario Nuvolone, Nicolas Schmid, Gino Miele, Silvia Sorce, Rita Moos, Christian Schori, Roger R Beerli, Monika Bauer, Philippe Saudan, Klaus Dietmeier, Ingolf Lachmann, Michael Linnebank, Roland Martin, Ulf Kallweit, Veronika Kana, Elisabeth J Rushing, Herbert Budka, Adriano Aguzzi
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases. Experimental and epidemiological evidence point toward a protracted, clinically silent phase in prion diseases, yet there is no diagnostic test capable of identifying asymptomatic individuals incubating prions. In an effort to identify early biomarkers of prion diseases, we have compared global transcriptional profiles in brains from pre-symptomatic prion-infected mice and controls...
2017: PloS One
https://www.readbyqxmd.com/read/28164765/commonalities-in-biological-pathways-genetics-and-cellular-mechanism-between-alzheimer-disease-and-other-neurodegenerative-diseases-an-in-silico-updated-overview
#19
Khurshid Ahmad, Mohammad Hassan Baig, Gohar Mushtaq, Mohammad Amjad Kamal, Nigel H Greig, Inho Choi
Alzheimer's disease (AD) is the most common and well-studied neurodegenerative disease (ND). Biological pathways, pathophysiology and genetics of AD show commonalities with other NDs viz. Parkinson's disease (PD), Amyotrophic lateral sclerosis (ALS), Huntington's disease (HD), Prion Disease and Dentatorubral-pallidoluysian atrophy (DRPLA). Many of the NDs, sharing the common features and molecular mechanisms suggests that pathology may be directly comparable and be implicated in disease prevention and development of highly effective therapies...
February 3, 2017: Current Alzheimer Research
https://www.readbyqxmd.com/read/28159831/prion-like-protein-aggregates-and-type-2-diabetes
#20
Abhisek Mukherjee, Claudio Soto
Type 2 diabetes (T2D) is a highly prevalent metabolic disease characterized by chronic insulin resistance and β-cell dysfunction and loss, leading to impaired insulin release and hyperglycemia. Although the mechanism responsible for β-cell dysfunction and death is not completely understood, recent findings suggest that the accumulation of misfolded aggregates of the islet amyloid polypeptide (IAPP) in the islets of Langerhans may play an important role in pancreatic damage. Misfolding and aggregation of diverse proteins and their accumulation as amyloid in different organs is the hallmark feature in a group of chronic, degenerative diseases termed protein misfolding disorders (PMDs)...
February 3, 2017: Cold Spring Harbor Perspectives in Medicine
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