Results 41 to 50 of about 225,633 (278)

Chaperones as integrators of cellular networks: Changes of cellular integrity in stress and diseases

open access: yes, 2008
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

Amyloid prions in fungi [PDF]

open access: yes, 2016
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

Enhanced Extracellular Type III Pullulan Hydrolase Production by Co-expressing Molecular Chaperone in Brevibacillus choshinensis and Fermentation Optimization

open access: yesShipin gongye ke-ji
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

open access: yesFrontiers in Pharmacology, 2019
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]

open access: yes, 2014
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

Structural instability impairs function of the UDP‐xylose synthase 1 Ile181Asn variant associated with short‐stature genetic syndrome in humans

open access: yesFEBS Letters, EarlyView.
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

open access: yesFEBS Letters, EarlyView.
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

open access: yesBio-Protocol, 2017
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

open access: yesRedox Biology, 2022
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

open access: yesFEBS Letters, EarlyView.
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

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