Results 101 to 110 of about 3,689,678 (299)
Protein fibrillation and nanoparticle interactions: opportunities and challenges
Due to their ultra-small size, nanoparticles (NPs) have distinct properties compared with the bulk form of the same materials. These properties are rapidly revolutionizing many areas of medicine and technology. NPs are recognized as promising and powerful tools to fight against the human brain diseases such as multiple sclerosis or Alzheimer's disease.
Mahmoudi, M. +3 more
openaire +3 more sources
Malformin A1–mediated cytotoxicity in ovarian cancer cells occurs through pyroptosis and autophagy
This study investigated the effects of the natural compound Malformin A1 (MA1) on the cytoskeleton that regulates cell proliferation and migration. Disruption of the cytoskeleton can impair these processes and promote cancer cell death. MA1 disrupted cytoskeletal organization, induced DNA damage, inflammation, activated autophagy, and pyroptosis ...
Nada Abdullah Hassan +11 more
wiley +1 more source
KDAC6 has been associated with cell motility and actin structures, but specific domain contributions are not established. The two catalytic domains have differential effects on motility and F‐actin regulation, affecting cortical F‐actin density, motility, stress fibers, and cell spreading.
Taylor V. Joseph +7 more
wiley +1 more source
Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]
Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David +9 more
core +1 more source
Protein misfolding and aggregation resulting in amyloid formation is directly linked to various diseases. Hence, there is keen interest in developing probes for the selective detection of such misfolded aggregated proteins.
Saurajit Ghosh (17296471) +3 more
core +1 more source
Characterization of the Amyloid Fibril as a Cross- Protein
The major component of amyloid is a fibrous protein (1) with a unique organization as seen by high resolution electron microscopy (2). A second component, a pentagonal rod, has been isolated from amyloid deposits and demonstrated to be identical with a circulating a globulia (P-component) (3).
L, Bonar, A S, Cohen, M M, Skinner
openaire +2 more sources
Adenosine triphosphate as a modulator of protein interactions and stability
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley +1 more source
Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase. [PDF]
Partitioning of polypeptides between protein folding and amyloid formation is of outstanding pathophysiological importance. Using yeast phosphoglycerate kinase as model, here we identify the features of the energy landscape that decide the fate of the ...
Gottfried Köhler +7 more
core +1 more source
Cell surface CD11c as a neutrophil aging marker molecule
Cell surface CD11chi neutrophils were more aged and had better phagocytic function than CD11c−/lo neutrophils. Transcriptomic analysis of CD11chi neutrophils and CD11c−/lo neutrophils in pediatric population showed that the most difference was seen in infants.
Sophia Koutsogiannaki +5 more
wiley +1 more source
Amyloidogenesis of a Type III-dependent Hpa1 and Structural analysis of a drug-pump repressor DNA complex [PDF]
Part I Amyloidogenesis of Type III-dependent Hpa1 from Xanthomonas oryzae pv. oryzicola The first harpin, HrpN from Erwinia amylovora, the bacterium that causes fire blight of pear, apple and other rosaceous plants, was reported as an HR ...
ZHANG, BING
core

