Results 31 to 40 of about 18,838 (278)
, 2012 Many bacteria can assemble functional amyloid fibers on their cell surface. The majority of bacterial amyloids contribute to biofilm or other community behaviors where cells interact with a surface or with another cell. Bacterial amyloids, like all functional amyloids, share structural and biochemical properties with disease-associated eukaryotic ...
Yizhou, Zhou +3 more
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Direct Identification of Functional Amyloid Proteins by Label-Free Quantitative Mass Spectrometry
Biomolecules, 2017 Functional amyloids are important structural and functional components of many biofilms, yet our knowledge of these fascinating polymers is limited to a few examples for which the native amyloids have been isolated in pure form.
Heidi N. Danielsen +6 more
doaj +1 more source
Clinical Kidney Journal, 2014 Amyloidosis is an uncommon disease that is characterized by abnormal extracellular deposition of misfolded protein fibrils leading to organ dysfunction. The deposited proteins display common chemical and histologic properties but can vary dramatically in their origin. Kidney disease is a common manifestation in patients with systemic amyloidosis with a
Khalighi, Mazdak A. +2 more
openaire +2 more sources
Amyloid Fragmentation and Disaggregation in Yeast and Animals
Biomolecules, 2021 Amyloids are filamentous protein aggregates that are associated with a number of incurable diseases, termed amyloidoses. Amyloids can also manifest as infectious or heritable particles, known as prions. While just one prion is known in humans and animals,
Vitaly V. Kushnirov +2 more
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Molecular Basis of Orb2 Amyloidogenesis and Blockade of Memory Consolidation.
PLoS Biology, 2016 Amyloids are ordered protein aggregates that are typically associated with neurodegenerative diseases and cognitive impairment. By contrast, the amyloid-like state of the neuronal RNA binding protein Orb2 in Drosophila was recently implicated in memory ...
Rubén Hervás +15 more
doaj +1 more source
Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology [PDF]
, 2017 Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as
Arosio, Paolo +6 more
core +1 more source
The Role of Functional Amyloids in Multicellular Growth and Development of Gram-Positive Bacteria [PDF]
, 2017 Amyloid fibrils play pivotal roles in all domains of life. In bacteria, these fibrillar structures are often part of an extracellular matrix that surrounds the producing organism and thereby provides protection to harsh environmental conditions. Here, we
Claessen, Dennis +2 more
core +4 more sources
An Amyloid Organelle: Solid State NMR Evidence for Cross-Beta Assembly of Gas Vesicles [PDF]
, 2011 Functional amyloids have been identified in a wide range of organisms, taking on a variety of biological roles and being controlled by remarkable mechanisms of directed assembly.
Bayro +35 more
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Toxins, 2021 Pseudomonas aeruginosa is an opportunistic, Gram-negative pathogen and an important cause of hospital acquired infections, especially in immunocompromised patients. Highly virulent P.
Kierra S. Hardy +3 more
doaj +1 more source
The LBFGS Quasi-Newtonian Method for Molecular Modeling Prion AGAAAAGA Amyloid Fibrils [PDF]
, 2012 Experimental X-ray crystallography, NMR (Nuclear Magnetic Resonance) spectroscopy, dual polarization interferometry, etc are indeed very powerful tools to determine the 3-Dimensional structure of a protein (including the membrane protein); theoretical ...
Hou, Yating +4 more
core +3 more sources