Results 51 to 60 of about 9,646 (179)
Filamentous tau-positive protein inclusions in neurons and glia are prominent features of a number of neurodegenerative disorders termed tauopathies. These inclusions are further characterized by the presence of heat shock proteins (HSPs).
Lisa Schwarz +2 more
doaj +1 more source
Calcium Homeostasis and Muscle Energy Metabolism Are Modified in HspB1-Null Mice
Hsp27—encoded by HspB1—is a member of the small heat shock proteins (sHsp, 12–43 kDa (kilodalton)) family. This protein is constitutively present in a wide variety of tissues and in many cell lines.
Brigitte Picard +6 more
doaj +1 more source
Abstract Recent evidence suggests that heat treatment (HT) and resistance training can limit skeletal muscle mass loss during immobilization. However, the effects of repeated HT sessions combined with hybrid exercises (EX), which promote both endurance and resistance responses, on muscle protein turnover following hindlimb unloading (HU) remain ...
Tom Normand‐Gravier +9 more
wiley +1 more source
ABSTRACT Organotin (IV) compounds are known to induce apoptosis via the intrinsic mitochondrial pathway, which is a key mechanism of effective anticancer therapy. Their ability to selectively promote apoptotic cell death highlights their potential as chemotherapeutic agents. In this study, the in vitro effects of two triorganotin compounds, tributyltin
Dana Strouhalova +3 more
wiley +1 more source
Under stress cells and tissues perform a series of physiologic adjustments, including the heat shock protein production (Hsp), these proteins play a role as molecular chaperons, they are divided in five main families: Hsp27, Hsp 60, Hsp70, Hsp90 and ...
R. Villalobos-Hurtado +3 more
doaj +1 more source
Protein kinase Cδ and pharmacomechanical coupling: Re‐envisioning cerebral vascular control
Abstract figure legend Top, G‐protein coupled receptors trigger electromechanical and pharmacomechanical coupling, the latter via signal transduction pathways that inhibit myosin light chain phosphatase. Middle, the relative contribution of electromechanical and pharmacomechanical coupling varies with the concentration and the vessel area to which ...
Nadia Haghbin +10 more
wiley +1 more source
Heat shock protein 27 phosphorylation state is associated with cancer progression
Understanding the mechanisms that control stress-induced survival is critical to explain how tumors frequently resist to treatment and to improve current anti-cancer therapies.
Maria eKatsogiannou +11 more
doaj +1 more source
Heat Shock Protein 90: From Molecular Chaperone Function to Therapeutic Targeting in Malignancies
In this review, an integrated conceptual framework linking HSP90's molecular chaperone functions to its pathological roles in cancer is proposed. HSP90 serves as a central node that integrates oncogenic signaling, buffers proteotoxic stress, maintains cancer stem cell plasticity, and shapes tumor‐immune interactions, all of which converge to drive ...
Beibei Zhang +4 more
wiley +1 more source
We developed HMCCNs@MAN, a biomimetic drug–gas codelivery platform for precise mild photothermal immunotherapy of liver fibrosis. Coated with hybrid macrophage‐aHSC membranes, it enables dual‐targeted delivery of MAN to the hepatic fibrosis site. Under NIR laser irradiation, HMCCNs@MAN can generate oxygen, release MAN, and produce heat.
Ming‐Xuan Liu +9 more
wiley +1 more source
Dephosphorylation of the small heat shock protein Hsp27 in vivo by protein phosphatase 2A.
The phosphorylation of the Hsp27 complex is rapidly altered in MRC-5 cells when they are exposed to mitogens, cytokines, stress, or serine/threonine protein phosphatase inhibitors. Here we performed experiments to identify which cellular protein phosphatase (PP1, PP2A, or PP2B) is responsible for the in vivo phosphorylation/dephosphorylation of Hsp27 ...
Cairns, J. +4 more
openaire +2 more sources

