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Amyloids — a functional coat for microorganisms [PDF]

open access: yesNature Reviews Microbiology, 2005
Amyloids are filamentous protein structures ~10 nm wide and 0.1–10 µm long that share a structural motif, the cross-β structure. These fibrils are usually associated with degenerative diseases in mammals.
Han Wösten   +2 more
exaly   +3 more sources
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Function of amyloid and amyloid protein precursor

Clinical Neurology and Neurosurgery, 1992
A short review is given of the functions of amyloid (beta/A4) and its precursor protein (APP). The possible relationship between amyloid deposition and dementia is discussed.
R A, Roos, J, Haan
openaire   +2 more sources

Degradation of Serum Amyloid A in Amyloid‐Susceptible and Amyloid‐Resistant Mouse Strains

Scandinavian Journal of Immunology, 1996
Degradation of serum amyloid A (apoSAA) by resident peritoneal cells (RPCS) and conditioned medium (CDM), prepared with RPCS, from amyloid‐susceptible CBA/J mice, amyloid‐resistant CE/J mice and their amyloid‐resistant CBA/J × CE/J F1 progeny was investigated in vitro.
R, Elliott-Bryant   +3 more
openaire   +2 more sources

A Coumarin-Based Array for the Discrimination of Amyloids

open access: yesACS Sensors
Self-assembly of misfolded proteins can lead to the formation of amyloids, which are implicated in the onset of many pathologies including Alzheimer’s disease and Parkinson’s disease.
Margaret Sunde, Elizabeth New
exaly   +2 more sources

Characterization of Amyloid

Annual Review of Medicine, 1974
The nature of the unique proteinaceous deposits in tissues in both systemic and localized amyloidosis has eluded investigative efforts for well over a century. Recent chemical and immunochemical evidence has demonstrated that in many cases of amyloidosis, the amyloid fibrils, which constitute one of the distinguishing features of the deposits, have as ...
G G, Glenner, W D, Terry
openaire   +2 more sources

Amyloid in the Lung

Seminars in Respiratory and Critical Care Medicine, 2020
AbstractAmyloidosis is the term given to abnormal deposition of misfolded precursor proteins at single or multiple sites, leading to organ dysfunction or clinical signs and symptoms. Pulmonary manifestations are nonspecific and may be associated with several amyloid protein subtypes, commonly AL (light chain) and AA (autoimmune) amyloids.
Misbah, Baqir, Anja C, Roden, Teng, Moua
openaire   +2 more sources

Amyloid and the Gut

Digestive Diseases, 2008
The systemic amyloidoses are serious and potentially fatal disorders caused by deposition of autologous proteins in an abnormal fibrilllar from. The clinical features are highly variable but gut involvement is common and random gastrointestinal biopsies are diagnostic in 80% of patients.
L B, Lovat, M B, Pepys, P N, Hawkins
openaire   +2 more sources

Amyloid and the Heart

Current Cardiology Reports, 2019
While morbidity and mortality remain high for amyloid cardiomyopathy (AC), increased awareness, earlier diagnosis, and advances in treatment have improved patient outcomes. This review will discuss the pathophysiology, contemporary diagnostic strategies, and novel and investigational therapeutic strategies for light-chain (AL) and transthyretin (ATTR ...
Aaron M, Wolfson   +2 more
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Amyloid and Amyloid Fibrils

2016
When proteins do not fold correctly, it can lead to very serious diseases. One such group of diseases is the amyloid diseases, of which Alzheimer’s disease (AD), Parkinson’s disease, and type 2 diabetes mellitus (T2DM) are members. The amyloid diseases are characterized by the aggregation of a specific protein into amyloid fibrils. During this process,
openaire   +1 more source

Amyloid structure

Essays in Biochemistry, 2014
Amyloid fibrils are formed by numerous proteins and peptides that share little sequence homology. The structures formed are highly ordered and extremely stable, being composed of β-sheet structure and stabilized along their length by hydrogen bonding. The fibrils are formed by several protofilaments that wind around one another in rope-like structures,
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