Results 71 to 80 of about 170,313 (323)

Remote‐Controllable Immune‐Priming Spot Formation Via Nanocomplexed Hydrogel‐Assisted Histotripsy: Immunoasis

open access: yesAdvanced Materials, EarlyView.
A novel immunotherapeutic strategy combines injectable, adjuvant‐loaded hydrogels with externally controlled histotripsy to create immune‐priming sites within tumors. This approach generates millimeter‐sized immune‐activated lesions with flexible, patient‐tailored treatment scheduling, enabling precise immune activation through tumor ablation‐mediated ...
Sung Hoon Kim   +9 more
wiley   +1 more source

Cytoplasmic protein misfolding titrates Hsp70 to activate nuclear Hsf1

open access: yeseLife, 2019
Hsf1 is an ancient transcription factor that responds to protein folding stress by inducing the heat-shock response (HSR) that restore perturbed proteostasis. Hsp70 chaperones negatively regulate the activity of Hsf1 via stress-responsive mechanisms that
Anna E Masser   +6 more
doaj   +1 more source

Heat shock protein 70 protects the lungs from hyperoxic injury in a neonatal rat model of bronchopulmonary dysplasia.

open access: yesPLoS ONE, 2023
Hyperoxia plays a significant role in the pathogenesis of lung injury, such as bronchopulmonary dysplasia (BPD), in premature infants or newborns. BPD management aims to minimize further injury, provide an optimal environment to support growth and ...
Cheng-Han Lee   +5 more
doaj   +1 more source

Insulin-induced Expression of Human Heat-shock Protein Gene hsp70

open access: yesJournal of Biological Chemistry, 1989
In human hepatoma cell line Hep3B/T2, the human heat-shock-inducible gene hsp70 could be induced by insulin. The dose-dependent insulin effect correlates very well with the dissociation constant of the insulin receptor, indicating that the insulin effect is mediated by the insulin receptor. The expression of hsp70 gene was neither significantly induced
L P, Ting, C L, Tu, C K, Chou
openaire   +2 more sources

Identification of heat shock protein hsp70 homologues in chloroplasts. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1990
Cytoplasmic members of the heat shock protein hsp70 family have recently been implicated in the transport of proteins to the endoplasmic reticulum and mitochondria. In addition, other hsp70 homologues have been found in the endoplasmic reticulum and mitochondria and, at least for the endoplasmic reticulum hsp70 homologue, may be involved in the proper ...
J S, Marshall   +3 more
openaire   +2 more sources

Mitochondrial protein import [PDF]

open access: yes, 1994
The transport of nuclear-encoded proteins from the cytosol into mitochondria is mediated by targeting (signal) sequences present on precursor forms.
Neupert, Walter, Schwarz, Elisabeth
core   +1 more source

Temporal and Cell‐Specific Regulation of Synaptic Homeostasis by the Chromatin Remodeler Chd1

open access: yesAdvanced Science, EarlyView.
Chd1, the Drosophila homologue of mammalian CHD2 ‐ a gene linked to autism, epilepsy, and intellectual disability, is required for synaptic homeostatic plasticity. Chd1 in glia is necessary for the rapid induction of synaptic homeostasis, whereas Chd1 in motoneurons, muscle, and glia is critical for long‐term maintenance.
Danielle T. Morency   +19 more
wiley   +1 more source

Heat shock-induced chaperoning by Hsp70 is enabled in-cell.

open access: yesPLoS ONE, 2019
Recent work has shown that weak protein-protein interactions are susceptible to the cellular milieu. One case in point is the binding of heat shock proteins (Hsps) to substrate proteins in cells under stress. Upregulation of the Hsp70 chaperone machinery
Drishti Guin   +3 more
doaj   +1 more source

Role of the heat shock transcription factor, Hsf1, in a major fungal pathogen that is obligately associated with warm-blooded animals [PDF]

open access: yes, 2009
Peer reviewedPublisher ...
Brown, Alistair J. P.   +3 more
core   +1 more source

Single‐Cell Atlas of Subchondral Bone Marrow Lesions Reveals Proteostasis Dysfunction as a Druggable Mechanism for Early Osteoarthritis

open access: yesAdvanced Science, EarlyView.
This study reveals that abnormal mechanical stress downregulates the expression of HSP70 and impairs proteasome function in osteoarthritic bone cells, leading to misfolded collagen I accumulation and ER stress. When intracellular proteostasis capacity is exceeded, USP19 mediates the secretion of misfolded proteins into the extracellular space ...
Hailun Xu   +20 more
wiley   +1 more source

Home - About - Disclaimer - Privacy