Results 11 to 20 of about 560,049 (292)

The Association of Amyloid‐β and Tau With Synaptic Dysfunction in Alzheimer's Disease [PDF]

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective To clarify the relative contributions of amyloid and tau to synaptic dysfunction in Alzheimer's disease (AD). Methods We included 109 cognitively unimpaired and impaired individuals from the Geneva Memory Center with available CSF synaptic biomarkers (neurogranin, SNAP‐25, GAP‐43). Participants were stratified according to amyloid (A)
Fausto Roveta, Augusto J. Mendes, Valentina Garibotto, Cecilia Boccalini, Aurelien Lathuiliere, Innocenzo Rainero, Elisa Rubino, Henrik Zetterberg, Nicholas J. Ashton, Federica Ribaldi, Giovanni B. Frisoni, for the Alzheimer's Disease Neuroimaging Initiative   +11 more
wiley   +2 more sources

Improving the Diagnostic Accuracy of Plasma Alzheimer's Disease Biomarkers With Objective and Subjective Cognitive Screening [PDF]

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Background Blood‐based biomarkers are increasingly used to identify Alzheimer's disease (AD) pathology and may play an important role in early disease screening and participant selection for clinical trials. However, their performance across stages of cognitive impairment remains unclear. This study examined whether plasma biomarkers differ in
Maryam Abdolmaleki, Leslie S. Gaynor, Dandan Liu, Timothy J. Hohman, Katherine A. Gifford, Henrik Zetterberg, Angela L. Jefferson, Corey J. Bolton   +7 more
wiley   +2 more sources

Injectable Peptide‐Based Functional Amyloid Hydrogels as Tunable Depots for Sustained Drug Delivery [PDF]

Advanced Science, EarlyView.
An injectable and tunable peptide‐based functional amyloid hydrogel provides sustained insulin release while preserving insulin stability and bioactivity. The hydrogel enables prolonged glycemic regulation in vivo, exhibits excellent biocompatibility, and shows no detectable IAPP and α‐Syn heterologous cross‐seeding, highlighting its potential as a ...
Ranjit Shaw, Niyamat M. A. Chimthanawala, Shouvik Manna, Sadhana Sathaye, Samir K. Maji   +4 more
wiley   +2 more sources

Structural Studies of Cystatin B Amyloid Fibre and Oligomer [PDF]

, 2013
Amyloid fibres are characteristic of over 25 degenerative human diseases including Alzheimer’s and Parkinson’s disease. Amyloid fibres are insoluble, highly stable, ordered cross-β sheet structures, which form as a result of conformational change and ...
Davis, Peter J.
core   +5 more sources

Ubiquitous Amyloids [PDF]

Applied Biochemistry and Biotechnology, 2012
The common view of amyloids and prion proteins is that they are associated with many currently incurable diseases and present a great danger to an organism. This danger comes from the fact that not only prion proteins, but also the infectious form(s) of amyloids, as it has been shown recently, are able to transmit the disease.
Pulawski W, Ghoshdastider U, ANDRISANO, VINCENZA, Filipek S.   +3 more
openaire   +2 more sources

AmyloGraph: a comprehensive database of amyloid–amyloid interactions

Nucleic Acids Research, 2022
Abstract Information about the impact of interactions between amyloid proteins on their fibrillization propensity is scattered among many experimental articles and presented in unstructured form. We manually curated information located in almost 200 publications (selected out of 562 initially considered), obtaining details of 883 ...
Michal Burdukiewicz, Dominik Rafacz, Agnieszka Barbach, Katarzyna Hubicka, Laura Bakala, Anna Lassota, Jakub Stecko, Natalia Szymanska, Jakub Wojciechowski, Dominika Kozakiewicz, Natalia Szulc, Jaroslaw Chilimoniuk, Izabela Jeskowiak, Marlena Gasior-Glogowska, Malgorzata Kotulska   +14 more
openaire   +6 more sources

Amyloid cardiomyopathy [PDF]

Biomedical Papers, 2017
Amyloidosis is a heterogeneous group of diseases characterized by the deposition of amyloid. It is caused by extracellular deposition of insoluble fibrils with beta-pleated sheet configuration. The protein misfolding abnormalities result in amyloid fibrils and may manifest as primary, secondary, or familial amyloidosis.
Lucie Karafiatova, Tomas Pika
openaire   +3 more sources

Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters [PDF]

, 2010
Amyloid assemblies are associated with several debilitating human disorders. Understanding the intra- and extracellular assembly of normally soluble proteins and peptides into amyloid aggregates and how they disrupt normal cellular functions is therefore
Xue, Wei-Feng, Hellewell, Andrew L., Hewitt, Eric W., Radford, Sheena E., Eric W. Hewitt, Andrew L. Hellewell, Wei-Feng Xue, Sheena E. Radford   +7 more
core   +1 more source

Mitochondrial β-amyloid in Alzheimer's disease [PDF]

, 2011
This research is supported by Alzheimer's Research UK, the Wellcome Trust and the Biotechnology and Biological Sciences Research Council.It is well established that the intracellular accumulation of beta-amyloid is associated with Alzheimer’s disease and
Ainge, JA, James A. Ainge, Muirhead, Kirsty Elizabeth Adair, Gunn-Moore, FJ, Muirhead, KE, Laura Aitken, Aitken, Laura, Zoe E. Allen, Allen, Zoe Eleanor, Gunn-Moore, Frank J, Conway, Stuart, Frank J. Gunn-Moore, Allen, ZE, Borger, E, Aitken, L, Borger, Eva, Ainge, James Alexander, Kirsty E.A. Muirhead, Eva Borger, Stuart J. Conway, Borger, Eva; id_orcid, Ainge, James Alexander; id_orcid, Aitken, Laura; id_orcid, Gunn-Moore, Frank J; id_orcid   +23 more
core   +1 more source

Microbial amyloids in neurodegenerative amyloid diseases

The FEBS Journal, 2023
Human‐disease associated amyloidogenic proteins are not unique in their ability to form amyloid fibrillar structures. Numerous microbes produce amyloidogenic proteins that have distinct functions for their physiology in their amyloid form, rather than solely detrimental. Emerging data indicate associations between various microbial organisms, including
openaire   +2 more sources