Results 121 to 130 of about 129,105 (287)
LONP1 is a conserved mitochondrial AAA + protease central to mitochondrial proteostasis. This review summarizes its structural features, protease-chaperone functions, and roles in metabolic regulation (heme/sulfur/steroid pathways) and disease. In cancer,
Wenwen Xi +5 more
doaj +1 more source
Background: Heat shock protein (Hsp90KDa) is a molecular chaperone involved in the process of cellular oncogenesis, hence its importance as a therapeutic target in clinical trials.
Ricardo Vivas-Reyes +8 more
doaj +1 more source
Aberrant Autophagic Response in The Muscle of A Knock-in Mouse Model of Spinal and Bulbar Muscular Atrophy [PDF]
Spinal and bulbar muscular atrophy (SBMA) is characterized by loss of motoneurons and sensory neurons, accompanied by atrophy of muscle cells. SBMA is due to an androgen receptor containing a polyglutamine tract (ARpolyQ) that misfolds and aggregates ...
Aggarwal, Tanya +15 more
core +2 more sources
Cryo‐EM analysis reveals an asymmetric MMOH–MMOB complex with distinct protomers, where MMOB binding triggers structural rearrangements from the surface to the active site. This conformational asymmetry shortens the Fe···Fe distance to 2.7 Å in one protomer, forming a geometry suitable for O2 activation and supporting a sequential catalytic mechanism ...
Yunha Hwang +9 more
wiley +1 more source
We present a novel DNA vaccine platform featuring intrinsic, non‐targeting dsRNA that significantly enhances immune responses by activating the regulated IRE1‐dependent decay‐RIG‐I signaling pathway. This research elucidates a previously uncharacterized mechanism for dsRNA‐mediated innate immune activation.
Min‐Syuan Huang +10 more
wiley +1 more source
Heat shock protein 90 inhibition: rationale and clinical potential
Heat shock protein 90 (HSP90) is a molecular chaperone protein essential for cellular survival. Functionally, HSPs promote proper protein folding, prevent misfolding, and restore three-dimensional protein structure which is critical following toxic ...
Robert B. Den, Bo Lu
doaj +1 more source
Structure, Function, and Clinical Relevance of Molecular Chaperones – A Review Article
Proteins known as molecular chaperones are essential components of cellular protein homeostasis since these proteins assist others in folding and stabilizing or degrading the polypeptides. The principle is that if misfolded or aggregated proteins—common in many pathologies such as cancer, neurodegenerative, and genetic diseases—are inhibited from ...
Salih Mahdi Alkhafaji +2 more
openaire +1 more source
Thermally Gated Dual‐Cascade Nanozyme for Enhanced Mild‐Temperature Photothermal Therapy
A thermo‐responsive cascade nanozyme (Ru‐GOx‐PNN) synergistically enhances mild photothermal therapy by dual suppression of HSP70 through ROS‐induced lipid peroxidation and ATP depletion. This intelligent system effectively overcomes thermotolerance and amplifies apoptosis, offering a safe and precise strategy for tumor treatment.
Shuyu Wang +7 more
wiley +1 more source
Gaucher disease (GD) is a lysosomal storage disorder caused by a deficiency in the GBA1‐encoded enzyme, β‐glucocerebrosidase. Enzyme replacement therapy is ineffective for neuronopathic Gaucher disease (nGD).
Kanako Higashi +28 more
doaj +1 more source
Identification and characterization of the antiplasmodial activity of Hsp90 inhibitors
Background The recent reduction in mortality due to malaria is being threatened by the appearance of Plasmodium falciparum parasites that are resistant to artemisinin in Southeast Asia.
Claribel Murillo-Solano +3 more
doaj +1 more source

