Results 51 to 60 of about 105,054 (297)

The HSP70 family and cancer [PDF]

open access: yesCarcinogenesis, 2013
The HSP70 family of heat shock proteins consists of molecular chaperones of approximately 70kDa in size that serve critical roles in protein homeostasis. These adenosine triphosphatases unfold misfolded or denatured proteins and can keep these proteins in an unfolded, folding-competent state.
openaire   +2 more sources

HSP70-HSP90 chaperone networking in protein-misfolding disease

open access: yes, 2022
Molecular chaperones and their associated co-chaperones are essential in health and disease as they are key facilitators of protein-folding, quality control and function.
Xavier Aran Guiu (5369765)   +5 more
core   +1 more source

Changes of cellular stress response related hsp70 and abcb1 transcript and Hsp70 protein levels in Siberian freshwater amphipods upon exposure to cadmium chloride in the lethal concentration range [PDF]

open access: yesPeerJ, 2020
The induction of cellular stress response systems, heat shock protein hsp70/Hsp70 and multixenobiotic transporter abcb1, by cadmium chloride (CdCl2) was explored in amphipod species with different stress adaptation strategies from the Lake Baikal area ...
Marina V. Protopopova   +2 more
doaj   +2 more sources

Maintenance of the Expression of c-FLIPL by Hsp70 to Resist Licochalcone A-Induced Anti-Colorectal Cancer Effect through ERK-Mediated Autophagy Induction

open access: yesFrontiers in Bioscience-Landmark, 2023
Background: The mortality rate of colorectal cancer (CRC) ranks second worldwide. Previous research had indicated that licochalcone A (LA) was a flavonoid in licorice with diverse anticancer effects.
Tianpeng Li   +11 more
doaj   +1 more source

The relationship between HSP70 and level of leptin and luteinizing hormones in female rats exposed to chronic and acute heat stress [PDF]

open access: yesIraqi Journal of Veterinary Sciences, 2020
The current search experiments designed to study the effect of chronic and acute heat stress on the relationship between HSP70, leptin and luteinizing hormones level in female rats.
Hiyam N. Matty, Ashwaq A. Hassan
doaj   +1 more source

The Effects of Heat Shock Proteins on Delivery of HIV-1 Nef Antigen in Mammalian Cells

open access: yesVaccine Research, 2020
Introduction: Vaccine design is mainly considered as a therapeutic strategy to elicit HIV-specific immunity. DNA vaccines encoding an antigen and also an adjuvant can induce an effective adaptive immunity. Due to having numerous roles in viral infection,
Alireza Milani   +3 more
doaj  

HSP70 promotes MLKL polymerization and necroptosis

open access: yesMolecular & Cellular Oncology, 2020
Mixed lineage kinase domain-like protein (MLKL) is the proposed executioner of necroptosis. Our recent findings identify a novel inhibitor necroptosis-blocking compound 1 (NBC1) which specifically conjugates to two cysteines of heat shock protein 70 ...
Andrea N. Johnston, Zhigao Wang
doaj   +1 more source

Comparison of heat-shock responses between the hydrothermal vent shrimp Rimicaris exoculata and the related coastal shrimp Palaemonetes varians [PDF]

open access: yes, 2010
The deep-sea vent shrimp Rimicaris exoculata is believed to occur at the hot end of the hydrothermal biotope in order to provide essential elements to its epibiosis. Because it is found close to hot venting water, R.
Thomas Chertemps   +11 more
core   +1 more source

The atheroprotective properties of Hsp70: a role for Hsp70-endothelial interactions? [PDF]

open access: yesCell Stress and Chaperones, 2009
Although heat shock (stress) proteins are typically regarded as being exclusively intracellular molecules, it is now apparent that they can be released from cells in the absence of cellular necrosis. We and others have reported the presence of Hsp60 (HSPD1) and Hsp70 (HSPA1A) in the circulation of normal individuals and our finding that increases in ...
A Graham, Pockley   +2 more
openaire   +2 more sources

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad   +2 more
wiley   +1 more source

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