Results 31 to 40 of about 3,632,451 (277)
The Sheaths of Methanospirillum Are Made of a New Type of Amyloid Protein
Frontiers in Microbiology, 2018 The genera Methanospirillum and Methanosaeta contain species of anaerobic archaea that grow and divide within proteinaceous tubular sheaths that protect them from environmental stressors.
Line Friis Bakmann Christensen +6 more
doaj +1 more source
Molecules, 2022 TIR-domain-containing adapter-inducing interferon-β (TRIF) is an innate immune protein that serves as an adaptor for multiple cellular signalling outcomes in the context of infection. TRIF is activated via ligation of Toll-like receptors 3 and 4.
Max O. D. G. Baker +7 more
doaj +1 more source
Exploring the sequence–structure relationship for amyloid peptides [PDF]
, 2012 Amyloid fibril formation is associated with misfolding diseases, as well as fulfilling a functional role. The cross-β molecular architecture has been reported in increasing numbers of amyloid-like fibrillar systems. The Waltz algorithm is able to predict
Morris, Kyle L. +14 more
core +1 more source
In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
Pathogens, 2019 Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an ...
David Partouche +5 more
doaj +1 more source
Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin [PDF]
, 2005 Human islet amyloid polypeptide (hIAPP) forms amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM). Pre-fibrillar hIAPP oligomers (in contrast to monomeric IAPP or mature fibrils) increase membrane permeability, suggesting an important ...
Bradshaw, Jeremy +11 more
core +1 more source
Prion, 2010 Evidence is growing at an increasing -pace that amyloid fibers are not just the result of aberrant protein folding associated with neurodegenerative diseases, but are widespread in nature for beneficial reasons. Amyloid is an attractive building material because its robust design and simple repetitive structure make for very durable and metabolically ...
openaire +3 more sources
Amyloid tracers detect multple binding sites in Alzheimer´s disease brain tissue. [PDF]
, 2013 Imaging fibrillar amyloid-β deposition in the human brain in vivo by positron emission tomography has improved our understanding of the time course of amyloid-β pathology in Alzheimer’s disease. The most widely used amyloid-β imaging tracer so far is 11C-
Nordberg, A, +9 more
core +1 more source
Zinc–dysprosium functionalized amyloid fibrils [PDF]
Dalton Transactions, 2019 The heterometallic Zn 2 Dy 2 entity bearing partially saturated metal centres covalently decorates a highly ordered amyloid fibril core and the functionalised assembly exhibits catalytic Lewis acid behaviour.
Stavroula I. Sampani +4 more
openaire +3 more sources
Heterotypic interactions in amyloid function and disease [PDF]
The FEBS Journal, 2021 Amyloid aggregation results from the self‐assembly of identical aggregation‐prone sequences into cross‐beta‐sheet structures. The process is best known for its association with a wide range of human pathologies but also as a functional mechanism in all kingdoms of life.
Konstantoulea, Katerina +3 more
openaire +3 more sources
The activity of amyloid beta binding alcohol dehydrogenase in Alzheimer's disease [PDF]
, 2012 The mitochondria are a vibrant hub for many problems that occur in Alzheimer’s disease. The enzyme amyloid-ß binding alcohol dehydrogenase (ABAD) and Cyclophilin D (CypD) are two key mitochondrial proteins that have essential functions in Alzheimer’s ...
Allen, Zoe Eleanor
core +2 more sources