Results 41 to 50 of about 225,633 (278)
Chaperones as integrators of cellular networks: Changes of cellular integrity in stress and diseases
Cellular networks undergo rearrangements during stress and diseases. In un-stressed state the yeast protein-protein interaction network (interactome) is highly compact, and the centrally organized modules have a large overlap.
Albanese +54 more
core +2 more sources
Prions are infectious protein polymers that have been found to cause fatal diseases in mammals. Prions have also been identified in fungi (yeast and filamentous fungi), where they behave as cytoplasmic non-Mendelian genetic elements.
Aguzzi +122 more
core +2 more sources
This study aimed to increase the expression and secretion of type III pullulan hydrolase (TK-PUL) by Brevibacillus choshinensis through the co-expression of molecular chaperone proteins and the optimization of fermentation conditions.
Jing ZENG +3 more
doaj +1 more source
Small Heat Shock Proteins, Big Impact on Protein Aggregation in Neurodegenerative Disease
Misfolding, aggregation, and aberrant accumulation of proteins are central components in the progression of neurodegenerative disease. Cellular molecular chaperone systems modulate proteostasis, and, therefore, are primed to influence aberrant protein ...
Jack M. Webster +3 more
doaj +1 more source
A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. [PDF]
Hsp90 is a conserved chaperone that facilitates protein homeostasis. Our crystal structure of the mitochondrial Hsp90, TRAP1, revealed an extension of the N-terminal β-strand previously shown to cross between protomers in the closed state. In this study,
Agard, David A +5 more
core +2 more sources
The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li +2 more
wiley +1 more source
Structural biology of ferritin nanocages
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry
The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins.
Manish Bhuwan +3 more
doaj +1 more source
An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA
Under physiological conditions, Escherichia coli RidA is an enamine/imine deaminase, which promotes the release of ammonia from reactive enamine/imine intermediates.
Marharyta Varatnitskaya +13 more
doaj +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy +4 more
wiley +1 more source

