Results 71 to 80 of about 147,841 (291)

An atlas of chaperone–protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell

open access: yesMolecular Systems Biology, 2009
Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is still absent.
Yunchen Gong   +6 more
doaj   +1 more source

RNAi-Mediated Reverse Genetic Screen Identified Drosophila Chaperones Regulating Eye and Neuromuscular Junction Morphology

open access: yesG3: Genes, Genomes, Genetics, 2017
Accumulation of toxic proteins in neurons has been linked with the onset of neurodegenerative diseases, which in many cases are characterized by altered neuronal function and synapse loss.
Sandeep Raut   +5 more
doaj   +1 more source

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]

open access: yes, 2008
Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano   +8 more
core   +3 more sources

Molecular Chaperones and Co-Chaperones in Parkinson Disease [PDF]

open access: yesThe Neuroscientist, 2012
Parkinson disease, a progressive neurodegenerative disorder, is caused by the pathological accumulation of proteins, including the ubiquitous presynaptic protein α-synuclein. Alterations in the metabolism of α-synuclein have clearly been linked to neurodegeneration, and early steps in the pathological sequence of this protein include the formation of ...
Hemi, Dimant   +2 more
openaire   +2 more sources

Infusible Extracellular Matrix Biomaterial Enhances Cell‐Specific Pro‐Repair Responses Following Acute Myocardial Infarction

open access: yesAdvanced Healthcare Materials, EarlyView.
We measure the cell‐specific responses of administering infusible ECM (iECM) in acute myocardial infarction (MI) across multiple timepoints. Using single‐nucleus RNA sequencing and spatial transcriptomics, we measure macrophage activation, fibroblast remodeling, increased vascular development, lymphangiogenesis, cardioprotection, and neurogenesis ...
Joshua M. Mesfin   +18 more
wiley   +1 more source

The Histone Chaperones SET/TAF‐1β and NPM1 Exhibit Conserved Functionality in Nucleosome Remodeling and Histone Eviction in a Cytochrome c‐Dependent Manner

open access: yesAdvanced Science, 2023
Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription.
Pedro Buzón   +5 more
doaj   +1 more source

The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. [PDF]

open access: yes, 1996
Ssa1/2p, members of one of the yeast cytosolic hsp70 subfamilies, have been implicated in the translocation of secretory proteins into the lumen of the ER.
Bush, GL, Meyer, DI
core  

Engineering Extracellular Vesicle Production Through Magnetic Ion Channel Activation for Bone Regeneration

open access: yesAdvanced Healthcare Materials, EarlyView.
Magnetic Ion Channel Activation (MICA) enables remote stimulation of mechanosensitive ion channels using functionalised magnetic nanoparticles, enhancing extracellular vesicle (EV) biogenesis is pre‐osteoblasts. MICA desrived EVs exhibit typical nano‐vesicular characteristics but display superior pro‐osteogeneic activity, promoting mesenchymal stem ...
Afeesh Rajan Unnithan   +9 more
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

Protein evolution speed depends on its stability and abundance and on chaperone concentrations. [PDF]

open access: yes, 2018
Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein's folding stability and aggregation propensity. By combining the hydrophobic-polar (HP) model with the Zwanzig-Szabo-Bagchi rate theory,
Agozzino, Luca, Dill, Ken A
core   +1 more source

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